Ecotin-like serine peptidase inhibitor ISP1 of Leishmania major plays a role in flagellar pocket dynamics and promastigote differentiation
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10123309" target="_blank" >RIV/00216208:11310/12:10123309 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1111/j.1462-5822.2012.01798.x" target="_blank" >http://dx.doi.org/10.1111/j.1462-5822.2012.01798.x</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/j.1462-5822.2012.01798.x" target="_blank" >10.1111/j.1462-5822.2012.01798.x</a>
Alternative languages
Result language
angličtina
Original language name
Ecotin-like serine peptidase inhibitor ISP1 of Leishmania major plays a role in flagellar pocket dynamics and promastigote differentiation
Original language description
Leishmania ISPs are ecotin-like natural peptide inhibitors of trypsin-family serine peptidases, enzymes that are absent from the Leishmania genome. This led to the proposal that ISPs inhibit host serine peptidases and we have recently shown that ISP2 inhibits neutrophil elastase, thereby enhancing parasite survival in murine macrophages. In this study we show that ISP1 has less serine peptidase inhibitory activity than ISP2, and in promastigotes both are generally located in the cytosol and along the flagellum. However, in haptomonad promastigotes there is a prominent accumulation of ISP1 and ISP2 in the hemidesmosome and for ISP2 on the cell surface. An L. major mutant deficient in all three ISP genes (?isp1/2/3) was generated and compared with ?isp2/3 mutants to elucidate the physiological role of ISP1. In in vitro cultures, the ?isp1/2/3 mutant contained more haptomonad, nectomonad and leptomonad promastigotes with elongated flagella and reduced motility compared with ?isp2/3 popula
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Cellular Microbiology
ISSN
1462-5814
e-ISSN
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Volume of the periodical
14
Issue of the periodical within the volume
8
Country of publishing house
GB - UNITED KINGDOM
Number of pages
16
Pages from-to
1271-1286
UT code for WoS article
000306405000011
EID of the result in the Scopus database
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