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</a>><br>Date: Mon, 17 Jul 2006 23:02:44<br>Subject: Articles found by RefScout for your requests<br>To: <a href="mailto:jayusp@gmail.com">jayusp@gmail.com</a><br><br></span><div><span class="q">
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This is RefScout-Newsletter 29/2006 for user Jeff155960.<br><br>
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REQUEST: [ leishmania ]<br>
(18 articles match this request. 1 article matching other requests removed)<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16790764" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16790764" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16790764</a>
<input name="id_16790764" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16790764" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16790764" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
<b>Leishmania</b> infection impairs beta1-integrin function and chemokine receptor expression in mononuclear phagocytes.</a><br>
AUTHORS: Nathanael F Pinheiro, Micely D R Hermida, Mariana P Macedo, José Mengel, Andre Bafica, Washington L C dos-Santos<br>
AFFILIATION: LPBI, Centro de Pesquisas Gonçalo Moniz, Fundação
Oswaldo Cruz, Rua Waldemar Falcão no. 121, Candeal, Salvador, BA
40296-710, Brazil.<br>
REFERENCE: Infect Immun 2006 Jul 74(7):3912-21<br>
<b>Leishmania</b> spp. are intracellular parasites that cause lesions in the
skin, mucosa, and viscera. We have previously shown that <b>Leishmania</b>
infection reduces mononuclear phagocyte adhesion to inflamed connective
tissue. In this study, we examined the role of adhesion molecules and
chemokines in this process. Infection rate (r = -0.826, P = 0.003) and
parasite burden (r = -0.917, P = 0.028) negatively correlated to mouse
phagocyte adhesion. The decrease (58.7 to 75.0% inhibition, P = 0.005)
in phagocyte adhesion to connective tissue, induced by <b>Leishmania</b>,
occurred as early as 2 h after infection and was maintained for at least
24 h. Interestingly, impairment of cell adhesion was sustained by
phagocyte infection, since it was not observed following phagocytosis of
killed parasites (cell adhesion varied from 15.2% below to 24.0% above
control levels, P > 0.05). In addition, <b>Leishmania</b> infection diminished
cell adhesion to fibronectin (54.1 to 96.2%, P < 0.01), collagen (15.
7 to 83.7%, P < 0.05), and laminin (59.1 to 82.2%, P < 0.05). The
CD11b(hi) subpopulation was highly infected (49.6 to 97.3%). Calcium and
Mg(2+) replacement by Mn(2+), a treatment that is known to induce
integrins to a high state of affinity for their receptors, reverted the
inhibition in adhesion caused by <b>Leishmania</b>. This reversion was
completely blocked by anti-VLA4 antibodies. Furthermore, expression of
CCR4 and CCR5, two chemokine receptors implicated in cell adhesion, was
found to be downregulated 16 h after infection (2.8 to 4.1 times and 1.9
to 2.8 times, respectively). Together, these results suggest that
mechanisms regulating integrin function are implicated in the change of
macrophage adhesion in leishmaniasis.<br>
<br><br>
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PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16790767" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16790767" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16790767</a>
<input name="id_16790767" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16790767" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16790767" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Cloning, characterization, and serodiagnostic evaluation of <b>Leishmania</b> infantum tandem repeat proteins.</a><br>
AUTHORS: Yasuyuki Goto, Rhea N Coler, Jeffrey Guderian, Raodoh Mohamath, Steven G Reed<br>
AFFILIATION: Infectious Disease Research Institute, 1124 Columbia St., Suite 400, Seattle, WA 98104, USA.<br>
REFERENCE: Infect Immun 2006 Jul 74(7):3939-45<br>
Visceral leishmaniasis (VL) is a form of leishmaniasis, which is caused
by infection with the protozoan parasite <b>Leishmania</b>, and is often fatal
unless it is treated. Rapid and accurate diagnosis of VL is important
for effective treatment. Here we report the cloning of previously
undescribed tandem repeat (TR) proteins of <b>Leishmania</b> infantum and an
evaluation of VL patient antibody responses to the corresponding
proteins. By screening an L. infantum expression library with sera from
human VL patients or infected hamsters, we identified 43 genes encoding
B-cell antigens. Surprisingly, 19 of the 43 genes (44%) were TR proteins
, and that percentage was significantly higher than that for genes
picked randomly from the database. We then expressed the TR regions of
LinJ16.1750, LinJ22.1590, and LinJ33.2870 and the entire LinJ28.2310
protein. These recombinant proteins were all recognized by Sudanese VL
patient sera in an enzyme-linked immunosorbent assay. Recombinant LinJ16
.1750 (rLinJ16.1750) showed the best performance among these antigens in
terms of both sensitivity and specificity. Serological evaluation
revealed that 97% (34 of 35) of Sudanese VL patients had significantly
elevated antibody levels to rLinJ16.1750. Furthermore, when eight of the
patient sera which had low reactivities to rK39 were tested with the
novel recombinant antigens, some of the sera showed stronger antibody
responses to these antigens than to rK39. Our results suggest that TR
regions from the novel L. infantum proteins identified in this study are
immunodominant B-cell epitopes and may represent good candidates for
serodiagnosis of VL.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16790814" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16790814" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16790814</a>
<input name="id_16790814" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16790814" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16790814" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Responses to <b>Leishmania</b> donovani in mice deficient in interleukin-12 (IL-12), IL-12/IL-23, or IL-18.</a><br>
AUTHORS: Henry W Murray, Christine W Tsai, Jianguo Liu, Xiaojing Ma<br>
AFFILIATION: Department of Medicine, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA. <a href="mailto:hwmurray@med.cornell.edu" title="mailto:hwmurray@med.cornell.edu" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
hwmurray@med.cornell.edu</a><br>
REFERENCE: Infect Immun 2006 Jul 74(7):4370-4<br>
Interleukin-12 (IL-12) orchestrates acquired resistance in intracellular
<b>Leishmania</b> donovani infection in the liver, inducing gamma interferon
and, in turn, macrophage activation and parasite killing. Nevertheless,
testing in IL-18(-/-) mice compared to wild-type mice and in IL-12p40
(-/-) compared to IL-12p35(-/-) mice also suggested both early-acting (
IL-18) and late-acting (IL-23) antileishmanial effects independent of IL
-12.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16243007" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16243007" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16243007</a>
<input name="id_16243007" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16243007" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16243007" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Evidence
for the existence of two distinct species: Psammomys obesus and
Psammomys vexillaris within the sand rats (Rodentia, Gerbillinae),
reservoirs of cutaneous leishmaniasis in Tunisia.</a><br>
AUTHORS: Ben Hamou Mostafa, Ben Abderrazak Souha, Frigui Sabeh, Chatti Noureddine, Ben Ismail Riadh<br>
AFFILIATION: Laboratoire d'Epidémiologie et d'Ecologie Parasitaire,
Institut Pasteur de Tunis, BP 74, 1002 Tunis Belvédère, Tunisia.<br>
REFERENCE: Infect Genet Evol 2006 Jul 6(4):301-8<br>
A thorough taxonomic knowledge about putative animal reservoirs of
transmissible diseases is an absolute prerequisite to any ecological
investigation and epidemiological survey of zoonoses. Indeed, accurate
identification of these reservoirs is essential for predicting species-
specific population outbreaks and therefore to develop accurate
ecological control strategies. The systematic status of sand rats (genus
Psammomys) remains unclear despite the pivotal role of these rodents in
the epidemiology of Zoonotic Cutaneous Leishmaniasis (ZCL) disease as
sand rats are the main known reservoir hosts of the protozoan parasite
<b>Leishmania</b> major. In the present work, we expose morphological,
biochemical, genetic and cytogenetic evidence supporting the
identification of at least two cryptic species within the genus
Psammomys in Tunisia. First, significant morphometric differences were
observed and were correlated associated with external features and
biogeographic origins. Second, differences in patterns of two isoenzymic
systems (Glutamate Oxaloacetate Transaminase (GOT) and 6-
PhosphoGluconate Dehydrogenase (6PGD)) were found, which makes it
possible to amount these isoenzyme characters to two diagnostic loci.
Third, based on the mitochondrial cytochrome b (cyt b) gene, a high
magnitude of genetic distance (13.89%) was also observed. Fourth,
cytogenetic analysis showed that these two populations groups differ in
their diploid chromosome numbers, i.e. 2N=46 versus 2N=48. We consider
that all these variations are enough important to be considered as
demonstrative and we propose that these two lineages should be
considered as two distinct species that we refer to the fat sand rat
Psammomys obesus Cretzschmar, 1828 and the thin sand rat Psammomys
vexillaris Thomas, 1925. Implications of such results on the eco-
epidemiology of ZCL in Tunisia are discussed.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16597468" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16597468" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16597468</a>
<input name="id_16597468" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16597468" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16597468" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
<b>Leishmania</b> donovani singly deficient in HGPRT, APRT or XPRT are viable in vitro and within mammalian macrophages.</a><br>
AUTHORS: Jan M Boitz, Buddy Ullman<br>
AFFILIATION: Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, 97239, USA.<br>
REFERENCE: Mol Biochem Parasitol 2006 Jul 148(1):24-30<br>
<b>Leishmania</b> species express three phosphoribosyltransferase enzymes,
hypoxanthine-guanine phosphoribosyltransferase (HGPRT), adenine
phosphoribosyltransferase (APRT), and xanthine phosphoribosyltransferase
(XPRT), which enable this genus to acquire purine nutrients from their
hosts. To test whether any of these enzymes is essential for viability,
transformation into amastigotes, and infectivity and proliferation
within mammalian macrophages, Deltahgprt, Deltaaprt, and Deltaxprt null
mutants were created by targeted gene replacement within a virulent
background of <b>Leishmania</b> donovani. Each of the three knockout strains
was viable as promastigotes and axenic amastigotes and capable of
maintaining an infection in bone marrow-derived murine macrophages.
These data support the hypothesis that none of the three
phosphoribosyltransferases is essential for purine salvage or viability
by itself and that purine salvage occurs through multiple anabolic
routes in both parasite life cycle stages. In addition these studies
revealed the presence of an adenine aminohydrolase enzyme in L. donovani
axenic amastigotes, an activity previously thought to be restricted to
promastigotes.<br>
<br><br>
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PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16600399" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16600399" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16600399</a>
<input name="id_16600399" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16600399" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16600399" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Isolation and characterization of mitochondrial ribosomes and ribosomal subunits from <b>Leishmania</b> tarentolae.</a><br>
AUTHORS: Dmitri A Maslov, Manjuli R Sharma, Evelin Butler, Arnold M
Falick, Mari Gingery, Rajendra K Agrawal, Linda L Spremulli, Larry
Simpson<br>
AFFILIATION: Department of Biology, University of California, Riverside, 92521, USA. <a href="mailto:maslov@ucr.edu" title="mailto:maslov@ucr.edu" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">maslov@ucr.edu
</a><br>
REFERENCE: Mol Biochem Parasitol 2006 Jul 148(1):69-78<br>
We have analyzed <b>Leishmania</b> tarentolae mitochondrial ribonucleoprotein (
RNP) complexes using the 9S small subunit (SSU) rRNA and the 12S large
subunit (LSU) rRNA as markers, and have identified a 50S RNP particle as
the putative mitochondrial monosome, a 40S particle as the putative LSU
and a 30S particle as the putative SSU. These assignments are supported
by morphological analysis by cryo-electron microscopy and proteomics
analyses by mass spectrometry. The presence of additional rRNA-
containing particles complicated the analysis and most likely was the
basis for previous difficulties in identification of these ribosomes;
thus, in addition to the monosomes and their subunits, there are
abundant stable 45S particles (SSU(*)) containing only 9S rRNA, which
may represent homodimers of the SSU or SSU associated with additional
proteins, and variable minor amounts of 65S and 70S particles, which
represent homodimers of the LSU and SSU(*), respectively. These
additional rRNA particles might be due to the lengthy mitochondrial
isolation and ribosome isolation procedures or may be present in vivo
and play yet undetermined roles.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16835450" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16835450" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16835450</a>
<input name="id_16835450" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16835450" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16835450" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Farnesyl Diphosphate Synthase Is a Cytosolic Enzyme in <b>Leishmania</b> major Promastigotes and Its Overexpression Confers Resistance to Risedronate.</a><br>
AUTHORS: Aurora Ortiz-Gómez, Carmen Jiménez, Antonio M Estévez,
Juana Carrero-Lérida, Luis M Ruiz-Pérez, Dolores González-Pacanowska<br>
AFFILIATION: Instituto de ParasitologÃa y Biomedicina López-Neyra,
Consejo Superior de Investigaciones CientÃficas, Avda. del
Conocimiento s/n, Parque Tecnológico Ciencias de la Salud, 18100
Armilla, Granada, Spain. <a href="mailto:dgonzalez@ipb.csic.es" title="mailto:dgonzalez@ipb.csic.es" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">dgonzalez@ipb.csic.es</a>.<br>
REFERENCE: Eukaryot Cell 2006 Jul 5(7):1057-64<br>
Farnesyl diphosphate synthase is the most likely molecular target of
aminobisphosphonates (e.g., risedronate), a set of compounds that have
been shown to have antiprotozoal activity both in vitro and in vivo.
This protein, together with other enzymes involved in isoprenoid
biosynthesis, is an attractive drug target, yet little is known about
the compartmentalization of the biosynthetic pathway. Here we show the
intracellular localization of the enzyme in wild-type <b>Leishmania</b> major
promastigote cells and in transfectants overexpressing farnesyl
diphosphate synthase by using purified antibodies generated towards a
homogenous recombinant <b>Leishmania</b> major farnesyl diphosphate synthase
protein. Indirect immunofluorescence, together with immunoelectron
microscopy, indicated that the enzyme is mainly located in the cytoplasm
of both wild-type cells and transfectants. Digitonin titration
experiments also confirmed this observation. Hence, while the initial
step of isoprenoid biosynthesis catalyzed by 3-hydroxy-3-methylglutaryl-
coenzyme A reductase is located in the mitochondrion, synthesis of
farnesyl diphosphate by farnesyl diphosphate synthase is a cytosolic
process. <b>Leishmania</b> major promastigote transfectants overexpressing
farnesyl diphosphate synthase were highly resistant to risedronate, and
the degree of resistance correlated with the increase in enzyme activity
. Likewise, when resistance was induced by stepwise selection with the
drug, the resulting resistant promastigotes exhibited increased levels
of farnesyl diphosphate synthase. The overproduction of protein under
different conditions of exposure to risedronate further supports the
hypothesis that this enzyme is the main target of aminobisphosphonates
in <b>Leishmania</b> cells.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16735512" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16735512" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16735512</a>
<input name="id_16735512" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16735512" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16735512" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
The {alpha}-Subunit of <b>Leishmania</b> F1 ATP Synthase Hydrolyzes ATP in Presence of tRNA.</a><br>
AUTHORS: Srikanta Goswami, Samit Adhya<br>
AFFILIATION: Genetic Engineering Laboratory, Indian Institute of
Chemical Biology, 4 Raja S.C. Mullick Road, Calcutta 700032, India.<br>
REFERENCE: J Biol Chem 2006 Jul 281(28):18914-7<br>
Import of tRNAs into the mitochondria of the kinetoplastid protozoon
<b>Leishmania</b> requires the tRNA-dependent hydrolysis of ATP leading to the
generation of membrane potential through the pumping of protons. Subunit
RIC1 of the inner membrane RNA import complex is a bi-functional
protein that is identical to the alpha-subunit of F(1)F(0) ATP synthase
and specifically binds to a subset (Type I) of importable tRNAs. We show
that recombinant, purified RIC1 is a Type I tRNA-dependent ATP
hydrolase. The activity was insensitive to oligomycin, sensitive to
mutations within the import signal of the tRNA, and required the
cooperative interaction between the ATP-binding and C-terminal domains
of RIC1. The ATPase activity of the intact complex was inhibited by anti
-RIC1 antibody, while knockdown of RIC1 in <b>Leishmania</b> tropica resulted
in deficiency of the tRNA-dependent ATPase activity of the mitochondrial
inner membrane. Moreover, RIC1 knockdown extracts failed to generate a
membrane potential across reconstituted proteoliposomes, as shown by a
rhodamine 123 uptake assay, but activity was restored by adding back
purified RIC1. These observations identify RIC1 as a novel form of the F
(1) ATP synthase alpha-subunit that acts as the major energy transducer
for tRNA import.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16830009" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16830009" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16830009</a>
<input name="id_16830009" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16830009" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16830009" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Progress towards a <b>Leishmania</b> vaccine.</a><br>
AUTHORS: Khaled S Tabbara<br>
AFFILIATION: Department of Microbiology, Immunology and Infectious
Diseases, College of Medicine and Medical Sciences, Arabian Gulf
University, PO Box 22979, Manama, Kingdom of Bahrain. Tel. +973 (1)
7239733. Fax. +973 (1) 7877195. E-mail: <a href="mailto:kst1@batelco.com.bh" title="mailto:kst1@batelco.com.bh" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">kst1@batelco.com.bh</a>.<br>
REFERENCE: Saudi Med J 2006 Jul 27(7):942-50<br>
Leishmaniasis is a vector-born protozoan disease. Approximately 12
million individuals are affected worldwide with an estimated annual
incidence of 1.5-2 million. Two clinical manifestations are recognized,
cutaneous, and visceral, both of which are common in the Middle East. In
both forms, infection is chronic, with potential deformities,
persistence following cure, and lifelong risk of reactivation. Attempts
to develop an effective human <b>Leishmania</b> vaccine have not yet succeeded
. Leishmanization, a crude form of live vaccination historically
originated in this part of the world. Experimental vaccination has been
extensively studied in model animals in the past 2 decades. In this
review, major human killed vaccine trials are surveyed, and modern
trends in <b>Leishmania</b> vaccine development, including subunit vaccines,
naked DNA vaccines, and transmission blocking vaccines are explored.
Recent findings of a link between persistence of live parasites, and
maintenance of long-term immunity suggest live vaccination with
attenuated strains, as a future vaccination strategy.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16783261" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16783261" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16783261</a>
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TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16783261" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16783261" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
[Visceral leishmaniasis in an immunocompetent subject, acquired in the Pyrenees region]</a><br>
AUTHORS: Denis Malvy, Félix Djossou, C Ibanez, Rémy Vatan, Maïté Longy-Boursier, Michel Le Bras<br>
AFFILIATION: Fédération de médecine interne, maladies infectieuses et tropicales, Hôpital Saint-André, Bordeaux (33).<br>
REFERENCE: Presse Med 2006 Jun 35(6 Pt 1):987-8<br>
INTRODUCTION: Visceral leishmaniasis can develop in immunocompetent
subjects exposed to a risk of infestation during physical activities
outdoors. CASE: A 35-year-old woman was hospitalized for impaired health
status with fever, hepatomegaly, splenomegaly, and pancytopenia, which
worsened during her stay. Leishmaniasis was finally diagnosed, based on
serologic testing and the finding of <b>Leishmania</b> infantum in the sternal
aspiration. Eight months earlier, she had spent two weeks at a lake in
the Pyrenees. Treatment with meglumine antimoniate was efficacious.
COMMENTS: This case is original because of the extent of the
organomegaly and its onset after vacation in an area far from those
where it is thought to be endemic.<br>
<br><br>
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PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16722639" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16722639" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16722639</a>
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TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16722639" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16722639" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
2H-benzimidazole 1,3-dioxide derivatives: a new family of water-soluble anti-trypanosomatid agents.</a><br>
AUTHORS: Mariana Boiani, LucÃa Boiani, Ana Denicola, Susana Torres de
Ortiz, Elva Serna, Ninfa Vera de Bilbao, Luis Sanabria, Gloria Yaluff,
Héctor Nakayama, Antonieta Rojas de Arias, Celeste Vega, Miriam Rolan,
Alicia Gómez-Barrio, Hugo Cerecetto, Mercedes Gonzalez<br>
AFFILIATION: Departamento de QuÃmica Organica, Facultad de
Ciencias-Facultad de QuÃmica, Universidad de la República, Uruguay.<br>
REFERENCE: J Med Chem 2006 Jun 49(11):3215-24<br>
Three series of benzimidazole N-oxide derivatives were developed and
were examined for their activity against trypanosomatid parasites (
Trypanosoma cruzi and <b>Leishmania</b> spp.). 2H-benzimidazole 1,3-dioxides
displayed remarkable in vitro activities against both parasites, with
derivatives 28, 29, and 32 being the most potent (IC50 < 5 microM)
against the epimastigote form of T. cruzi and 28, 33, and 35 the most
potent against the promastigote form of <b>Leishmania</b> spp. Unspecific
cytotoxicity was evaluated using murine macrophages, and derivative 33
was not toxic at a concentration 30 times that of its IC50 against T.
cruzi that was completely toxic for <b>Leishmania</b> spp., implying that the
series of 2H-benzimidazole 1,3-dioxides is selective toward both
trypanosomatid parasites. Derivatives 33 and 35 were submitted to an in
vivo assay using an acute model of Chagas' disease and a short-term
treatment (30 mg/kg/day orally administrated as aqueous solution, during
10 days). While in the control (untreated) and Benznidazole (50 mg/kg/
day) groups survival fraction was 60.0% and 87.5%, respectively, none of
the animals treated with derivatives 33 and 35 died. From the
preliminary structure-activity relationship studies reduction potential
and electrophilicity were found relevant to anti-T. cruzi activity.
Active compounds are better electrophiles and more easily reduced than
inactive ones.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16697632" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16697632" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16697632</a>
<input name="id_16697632" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16697632" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16697632" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Turkish
freshwater and marine macrophyte extracts show in vitro antiprotozoal
activity and inhibit FabI, a key enzyme of Plasmodium falciparum fatty
acid biosynthesis.</a><br>
AUTHORS: I Orhan, B Sener, T Atici, R Brun, R Perozzo, D Tasdemir<br>
AFFILIATION: Department of Pharmacognosy, Faculty of Pharmacy, Gazi University, TR-06330 Ankara, Turkey.<br>
REFERENCE: Phytomedicine 2006 Jun 13(6):388-93<br>
The ethanolic extracts of a number of Turkish freshwater macrophytes (
Potamogeton perfoliatus, Ranunculus tricophyllus and Cladophora
glomerata) and marine macroalgae (Dictyota dichotoma, Halopteris
scoparia, Posidonia oceanica, Scinaia furcellata, Sargassum natans and
Ulva lactuca) were assayed for their in vitro antiprotozoal activity.
Trypanosoma brucei rhodesiense, Trypanosoma cruzi, <b>Leishmania</b> donovani
and Plasmodium falciparum were used as test organisms. The cytotoxicity
of the extracts was also assessed against primary rat skeletal myoblasts
(L6 cells). Whereas none of the extracts were active against T. cruzi,
all crude extracts displayed appreciable trypanocidal activity against T
. brucei rhodesiense, with S. natans being the most active one (IC(50) 7
.4microg/ml). Except for the marine alga H. scoparia, all extracts also
possessed leishmanicidal potential. The best antileishmanial activity
was exerted by U. lactuca and P. oceanica (IC(50)'s 5.9 and 8.0microg/ml
, respectively). Five extracts that demonstrated inhibitory activity
towards P. falciparum (IC(50)'s 18.1-48.8microg/ml) were simultaneously
assayed against FabI, a crucial enzyme of the fatty acid system of P.
falciparum, to find out whether FabI was their target. The extracts of C
. glomerata and U. lactuca efficiently inhibited the FabI enzyme with IC
(50) values of 1.0 and 4.0microg/ml, respectively. None of the extracts
were cytotoxic towards mammalian L6 cells. This work reports for the
first time antiprotozoal activity of some Turkish marine and freshwater
algae, as well as a target-based antiplasmodial screening for the
identification of P. falciparum FabI inhibitors from aquatic and marine
macrophytes.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16635538" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16635538" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16635538</a>
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TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16635538" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16635538" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Immunotherapy against visceral leishmaniasis with the nucleoside hydrolase-DNA vaccine of <b>Leishmania</b> donovani.</a><br>
AUTHORS: R Gamboa-León, E Paraguai de Souza, G P Borja-Cabrera, F N
Santos, L M Myashiro, R O Pinheiro, E Dumonteil, C B Palatnik-de-Sousa<br>
AFFILIATION: Instituto de Microbiologia, Prof. Paulo de Góes,
Universidade Federal do Rio de Janeiro, UFRJ, CCS, Cidade
Universitária, Ilha do Fundão, Caixa Postal 68040, CEP 21941-590, Rio
de Janeiro, RJ, Brazil.<br>
REFERENCE: Vaccine 2006 May 24(22):4863-73<br>
The nucleoside hydrolase (NH36) of <b>Leishmania</b> (L.) donovani is a vital
enzyme which releases purines or pyrimidines of foreign DNA to be used
in the synthesis of parasite DNA. As a bivalent DNA vaccine, the VR1012-
NH36 was immunoprotective against visceral and cutaneous murine
leishmaniasis. In this work we tested the immunotherapy against
<b>Leishmania</b> (L.) chagasi infection, using two doses of 100 or 20 microg
VR1012-NH36 vaccine (i.m. route), and, as a possible immunomodulator,
aqueous garlic extract (8 mg/kg/day by the i.p. route), which was
effective in immunotherapy of cutaneous murine leishmaniasis. Liver
parasitic load was significantly reduced following treatment with 100
microg (91%) and 20 microg (77%) of the DNA vaccine, and by 20 microg
DNA vaccine and garlic extract (76%) (p=0.023). Survival was 33% for
saline controls, 100% for the 100 microg vaccine, and 83 and 67% for the
20 microg vaccine with and without garlic extract addition,
respectively. Garlic treatment alone did not reduce parasite load (p>0.
05), but increased survival (100%). The NH36-DNA vaccine was highly
effective as a new tool for the therapy and control of visceral
leishmaniasis, while the mild protective effect of garlic might be
related to an unspecific enhancement of IFN-gamma secretion.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16757380" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16757380" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16757380</a>
<input name="id_16757380" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16757380" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16757380" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
DNA topoisomerase I from parasitic protozoa: a potential target for chemotherapy.</a><br>
AUTHORS: R M Reguera, C M Redondo, R Gutierrez de Prado, Y Pérez-Pertejo, R Balaña-Fouce<br>
AFFILIATION: Dpto. FarmacologÃa y ToxicologÃa (INTOXCAL), Universidad de León, Campus de Vegazana s/n, 24071 León, Spain.<br>
REFERENCE: Biochim Biophys Acta 2006 Mar-Apr 1759(3-4):117-31<br>
The growing occurrence of drug resistant strains of unicellular
prokaryotic parasites, along with insecticide-resistant vectors, are the
factors contributing to the increased prevalence of tropical diseases
in underdeveloped and developing countries, where they are endemic.
Malaria, cryptosporidiosis, African and American trypanosomiasis and
leishmaniasis threaten human beings, both for the high mortality rates
involved and the economic loss resulting from morbidity. Due to the fact
that effective immunoprophylaxis is not available at present;
preventive sanitary measures and pharmacological approaches are the only
sources to control the undesirable effects of such diseases. Current
anti-parasitic chemotherapy is expensive, has undesirable side effects
or, in many patients, is only marginally effective. Under this point of
view molecular biology techniques and drug discovery must walk together
in order to find new targets for chemotherapy intervention. The
identification of DNA topoisomerases as a promising drug target is based
on the clinical success of camptothecin derivatives as anticancer
agents. The recent detection of substantial differences between
trypanosome and <b>leishmania</b> DNA topoisomerase IB with respect to their
homologues in mammals has provided a new lead in the study of the
structural determinants that can be effectively targeted. The present
report is an up to date review of the new findings on type IB DNA
topoisomerase in unicellular parasites and the role of these enzymes as
targets for therapeutic agents.</form></div><div><span class="q"><br>
<br><br>
********************************************************************************************************************<br>
The following references are revised files and are brought to you in accordance to license agreement with the NLM.<br>
********************************************************************************************************************<br><br></span></div><div>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=15876463" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=15876463" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
15876463</a>
<input name="id_15876463" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=15876463" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=15876463" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Regulation of genes encoding the major surface protease of <b>Leishmania</b> chagasi via mRNA stability.</a><br>
AUTHORS: Jay E Purdy, John E Donelson, Mary E Wilson<br>
AFFILIATION: Department of Internal Medicine, University of Iowa, Iowa City, IA 52242, USA. <a href="mailto:jay-purdy@uiowa.edu" title="mailto:jay-purdy@uiowa.edu" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
jay-purdy@uiowa.edu</a><br>
REFERENCE: Mol Biochem Parasitol 2005 Jul 142(1):88-97<br>
The intercoding regions between many <b>Leishmania</b> sp. genes regulate their
mRNA expression. The MSPL mRNA, encoding a subclass of the major
surface protease (MSP) of <b>Leishmania</b> chagasi, increases in abundance,
when protein synthesis is arrested, while alpha-tubulin (alpha-TUB) mRNA
and most other mRNAs do not. We found that the intercoding region
between MSPL-coding regions, when cloned downstream of the beta-
galactosidase reporter gene (beta-GAL), caused beta-GAL mRNA to increase
8- to 10-fold after inhibiting protein synthesis with cycloheximide.
Stable L. chagasi transfectants containing hybrid MSPL/alpha-TUB
intercoding regions cloned downstream of beta-GAL were made. The alpha-
TUB intercoding region induced high-level baseline beta-GAL mRNA that
increased only 1.3-fold after incubation with cycloheximide. In contrast
, the MSPL intercoding region, as well as constructs containing
nucleotides 303-505 from the MSPL 3'UTR, caused steady-state beta-GAL
mRNA levels in the absence of cycloheximide that were approximately 10%
of alpha-TUB constructs. These levels increased between 4.4- and 13.2-
fold after cycloheximide was added. Constructs containing half of this
region (303-394 or 395-505) produced intermediate levels of beta-GAL
mRNA and intermediate levels of cycloheximide induction. The kinetics of
cycloheximide induction of beta-GAL mRNA was similar with region 303-
505 constructs as with constructs bearing the entire endogenous MSPL
intercoding region. Furthermore, region 303-505 increased reporter mRNA
abundance after cycloheximide by increasing mRNA half-life. Hence, we
have identified a 202-nucleotide region within the MSPL 3'UTR that is in
part responsible for cycloheximide induction. We hypothesize that this
region may interact with labile regulatory protein factor(s).<br>
<br><br>
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16020728</a>
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TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16020728" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16020728" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
The genome of the kinetoplastid parasite, <b>Leishmania</b> major.</a><br>
AUTHORS: Alasdair C Ivens, Christopher S Peacock, Elizabeth A Worthey,
Lee Murphy, Gautam Aggarwal, Matthew Berriman, Ellen Sisk, Marie-Adele
Rajandream, Ellen Adlem, Rita Aert, Atashi Anupama, Zina Apostolou,
Philip Attipoe, Nathalie Bason, Christopher Bauser, Alfred Beck,
Stephen M Beverley, Gabriella Bianchettin, Katja Borzym, Gordana Bothe,
Carlo V Bruschi, Matt Collins, Eithon Cadag, Laura Ciarloni, Christine
Clayton, Richard M R Coulson, Ann Cronin, Angela K Cruz, Robert M
Davies, Javier De Gaudenzi, Deborah E Dobson, Andreas Duesterhoeft,
Gholam Fazelina, Nigel Fosker, Alberto Carlos Frasch, Audrey Fraser,
Monika Fuchs, Claudia Gabel, Arlette Goble, André Goffeau, David
Harris, Christiane Hertz-Fowler, Helmut Hilbert, David Horn, Yiting
Huang, Sven Klages, Andrew Knights, Michael Kube, Natasha Larke,
Lyudmila Litvin, Angela Lord, Tin Louie, Marco Marra, David Masuy,
Keith Matthews, Shulamit Michaeli, Jeremy C Mottram, Silke
Müller-Auer, Heather Munden, Siri Nelson, Halina Norbertczak, Karen
Oliver, Susan O'neil, Martin Pentony, Thomas M Pohl, Claire Price,
Bénédicte Purnelle, Michael A Quail, Ester Rabbinowitsch, Richard
Reinhardt, Michael Rieger, Joel Rinta, Johan Robben, Laura Robertson,
Jeronimo C Ruiz, Simon Rutter, David Saunders, Melanie Schäfer,
Jacquie Schein, David C Schwartz, Kathy Seeger, Amber Seyler, Sarah
Sharp, Heesun Shin, Dhileep Sivam, Rob Squares, Steve Squares,
Valentina Tosato, Christy Vogt, Guido Volckaert, Rolf Wambutt, Tim
Warren, Holger Wedler, John Woodward, Shiguo Zhou, Wolfgang Zimmermann,
Deborah F Smith, Jenefer M Blackwell, Kenneth D Stuart, Bart Barrell,
Peter J Myler<br>
AFFILIATION: Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridgeshire CB10 1SA, UK. <a href="mailto:alicat@sanger.ac.uk" title="mailto:alicat@sanger.ac.uk" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
alicat@sanger.ac.uk</a><br>
REFERENCE: Science 2005 Jul 309(5733):436-42<br>
<b>Leishmania</b> species cause a spectrum of human diseases in tropical and
subtropical regions of the world. We have sequenced the 36 chromosomes
of the 32.8-megabase haploid genome of <b>Leishmania</b> major (Friedlin strain
) and predict 911 RNA genes, 39 pseudogenes, and 8272 protein-coding
genes, of which 36% can be ascribed a putative function. These include
genes involved in host-pathogen interactions, such as proteolytic
enzymes, and extensive machinery for synthesis of complex surface
glycoconjugates. The organization of protein-coding genes into long,
strand-specific, polycistronic clusters and lack of general
transcription factors in the L. major, Trypanosoma brucei, and
Trypanosoma cruzi (Tritryp) genomes suggest that the mechanisms
regulating RNA polymerase II-directed transcription are distinct from
those operating in other eukaryotes, although the trypanosomatids appear
capable of chromatin remodeling. Abundant RNA-binding proteins are
encoded in the Tritryp genomes, consistent with active
posttranscriptional regulation of gene expression.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=15888291" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=15888291" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
15888291</a>
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TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=15888291" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=15888291" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
<b>Leishmania</b>
chagasi: the alpha-tubulin intercoding region results in constant
levels of mRNA abundance despite protein synthesis inhibition and
growth state.</a><br>
AUTHORS: Jay E Purdy, John E Donelson, Mary E Wilson<br>
AFFILIATION: Department of Internal Medicine, University of Iowa, Iowa City, IA 52242, USA.<br>
REFERENCE: Exp Parasitol 2005 Jun 110(2):102-7<br>
The intercoding regions of many <b>Leishmania</b> sp. genes have been
implicated in the regulation of mRNA processing, stability, and
translation. Herein we show that the intercoding region of the
<b>Leishmania</b> chagasi alpha-tubulin gene (alpha-TUB) confers stable beta-
galactosidase (beta-GAL) reporter mRNA levels during promastigote growth
and development in vitro and during protein synthesis inhibition. The
abundance of both endogenous alpha-TUB mRNA and beta-GAL mRNA from a
beta-GAL coding region situated upstream of the alpha-TUB intercoding
region did not change significantly as promastigotes grew from
logarithmic to stationary phase in vitro and the half-life of the beta-
GAL mRNA remained constant. The abundance of both the endogenous alpha-
TUB and the beta-GAL mRNA increased by less than 2-fold after protein
synthesis inhibition corresponding to a moderate increase in mRNA half-
life. These data suggest that the alpha-TUB intercoding region is an
excellent control for the study of the regulation of other
differentially expressed genes.<br>
<br><br>
REQUEST: [ sand fly NOT culicoides ]<br>
(2 articles match this request)<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16830703" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16830703" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16830703</a>
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TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16830703" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16830703" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Taxonomic revision of phlebotomine <b>sand fly</b>
species in the series davisi and panamensis of the subgenus
Psychodopygus Mangabeira, 1941 (Diptera: Psychodidae: Phlebotominae).</a><br>
AUTHORS: Gustavo Mayr Lima de Carvalho, Alda Lima Falcão, José Dilermando Andrade Filho<br>
AFFILIATION: Laboratório de Leishmanioses, Centro de Pesquisas René
Rachou-Fiocruz, Av. Augusto de Lima 1715, 30190-002 Belo Horizonte, MG,
Brasil. <a href="mailto:gumayr@cpqrr.fiocruz.br" title="mailto:gumayr@cpqrr.fiocruz.br" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">gumayr@cpqrr.fiocruz.br</a><br>
REFERENCE: Mem Inst Oswaldo Cruz 2006 Mar 101(2):129-36<br>
Several species of the subgenus Psychodopygus Mangabeira, 1941 are known
to be leishmaniosis vectors in Brazil. Some of them are morphologically
similar, which makes their identification quite difficult concerning
epidemiological studies. The aim of the current work is to study the
morphology of adult specimens of the subgenus Psychodopygus, in
accordance with the morphological similarity and still taking into
account the epidemiological importance of some species. Thus 11 species
have been studied, including four subspecies of adult specimens
deposited in the phlebotomine collection of Centro de Pesquisas René
Rachou-Fiocruz. Morphological characters found in the literature and new
features observed in this study were recorded in a taxonomic discussion
format. These characters make it easy to separate such species. Four
taxa, previously considered as subspecies, were raised to the category
of species.<br>
<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16830705" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16830705" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16830705</a>
<input name="id_16830705" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16830705" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16830705" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Description
of Pintomyia (Pifanomyia) brazilorum sp. nov. a new fossil species from
the Dominican Republic (Diptera: Psychodidae: Phlebotominae).</a><br>
AUTHORS: José Dilermando Andrade Filho, Eunice A Bianchi Galati, Alda Lima Falcão<br>
AFFILIATION: Laboratório de Leishmanioses, Centro de Pesquisas René
Rachou-Fiocruz, Av. Augusto de Lima 1715, 30190-002 Belo Horizonte, MG,
Brasil. <a href="mailto:jandrade@cpqrr.fiocruz.br" title="mailto:jandrade@cpqrr.fiocruz.br" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">jandrade@cpqrr.fiocruz.br</a><br>
REFERENCE: Mem Inst Oswaldo Cruz 2006 Mar 101(2):141-2<br>
A <b>sand fly</b> fossil was found in amber; a vegetal resin, which allows all
the external phlebotomine structures to be seen. The piece that contains
the new species is 14 mm long x 8 mm wide x 3 mm high. All the
structures from the head, thorax, and abdomen were examined under the
microscope and measured with a calibrated micrometric eyepiece. The
morphological aspects of the new species suggest its inclusion in the
Pintomyia genus, Pifanomyia subgenus though it is not possible to
include it in any of the series known for this subgenus. The presence of
two atrophied spines on the gonostyles and gonocoxites without tufts of
setae permit the exclusion of the new species from the other species of
the subgenus Pifanomyia. The new species is named Pintomyia (Pifanomyia
) brazilorum sp. nov.<br>
<br><br>
REQUEST: [ sandfly NOT culicoides ]<br>
(1 article matches this request)<br><br>
PMID: <a href="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16830711" title="http://refscout.com/cgi-bin/exportAbstract.pl?base=medline-28-9.xml&id=16830711" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
16830711</a>
<input name="id_16830711" value="Y" type="checkbox"><br>
TITLE: <a href="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16830711" title="http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=16830711" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">
Phlebotomines (Diptera: Psychodidae) in forested areas of the Serra da Bodoquena, state of Mato Grosso do Sul, Brazil.</a><br>
AUTHORS: Eunice A B Galati, Vânia L B Nunes, Paulo C Boggiani, Maria
Elizabeth C Dorval, Geucira Cristaldo, Hilda C Rocha, Elisa T Oshiro,
Geraldo A Damasceno-Júnior<br>
AFFILIATION: Departamento de Epidemiologia, Faculdade de Saúde
Pública, USP, Av. Dr. Arnaldo 715, 01246-904 São Paulo, SP, Brasil. <a href="mailto:egalati@usp.br" title="mailto:egalati@usp.br" target="_blank" onclick="return top.js.OpenExtLink(window,event,this)">egalati@usp.br</a>
<br>
REFERENCE: Mem Inst Oswaldo Cruz 2006 Mar 101(2):175-93<br>
Investigation was undertaken on the behaviour of the phlebotomine fauna
in caves, forests, and anthropic environments of the Serra da Bodoquena
, between January 1998 and January 2000. This paper reports on the
phlebotomines captured in forested areas with automatic light traps (ALT
), Shannon traps (ST), aspiration (AN), at natural resting sites and by
human attractiveness (HA) during 24 h. The diversity and abundance of
the species were investigated with ALT installed at 16 points (ground
level) and 6 in the canopy. Natural infection by flagellates was
investigated in females captured with ST AN, and HA. The <b>sandfly</b> fauna
was represented by 23 species. Twenty-two of these were captured with
ALT 15 of them on the western side, and 20 on the eastern. Lutzomyia
longipalpis and Nyssomyia whitmani were the most abundant on the former
and this species together with Lutzomyia almerioi on the latter side. On
the eastern side the ecotopes located close to caves rendered a
significantly greater number (P < or = 0.01) of specimens than did
more distant sites. On this side Lu. almerioi contributed with 56% of
the total number of specimens. Lu. almerioi females were predominantly
attracted by humans (96.4%) and by ST (93.2%) and three of the 2173
dissected (0.138%) presented natural infection by flagellates. The
attraction of Lu. almerioi to humans occurred during all seasons,
predominantly in the summer, and in nocturnal and diurnal periods. Thus
it is bothersome to inhabitants of and visitors to the Bodoquena ridge
and a potential vector of flagellates.<br>
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