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The role of surface glycoconjugates in Leishmania midgut attachment examined by competitive binding assays and experimental development in sand flies

Published online by Cambridge University Press:  23 April 2013

LUCIE JECNA
Affiliation:
Department of Parasitology, Faculty of Science, Charles University, Vinicna 7, 128 44 Prague 2, Czech Republic
ANNA DOSTALOVA
Affiliation:
Department of Parasitology, Faculty of Science, Charles University, Vinicna 7, 128 44 Prague 2, Czech Republic
RAY WILSON
Affiliation:
Centre for Immunity, Infection and Evolution, Institute for Immunology and Infection Research, School of Biological Sciences, University of Edinburgh, Edinburgh, UK
VERONIKA SEBLOVA
Affiliation:
Department of Parasitology, Faculty of Science, Charles University, Vinicna 7, 128 44 Prague 2, Czech Republic
KWANG-POO CHANG
Affiliation:
Department of Microbiology/Immunology, Chicago Medical School/Rosalind Franklin University, North Chicago, Illinois 60064, USA
PAUL A. BATES
Affiliation:
Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK
PETR VOLF*
Affiliation:
Department of Parasitology, Faculty of Science, Charles University, Vinicna 7, 128 44 Prague 2, Czech Republic
*
*Corresponding author. Department of Parasitology, Charles University, Vinicna 7, 12844 Prague 2, Czech Republic. E-mail: [email protected]

Summary

Binding of promastigotes to the sand fly midgut epithelium is regarded as an essential part of the Leishmania life cycle in the vector. Among Leishmania surface molecules putatively involved in attachment to the sand fly midgut, two GPI-anchored molecules are the most prominent: lipophosphoglycan (LPG) and promastigote surface protease gp63. In this work, we examined midgut attachment of Leishmania lines mutated in GPI-anchored molecules and compared results from 2 different techniques: in vivo development in sand flies and in vitro competitive binding assays using fluorescently labelled parasites. In combination with previous studies, our data provide additional support for (1) an LPG-independent parasite-binding mechanism of Leishmania major within the midgut of the permissive vector Phlebotomus perniciosus, and provide strong support for (2) the crucial role of L. major LPG in specific vector Phlebotomus papatasi, and (3) a role for Leishmania amazonensis gp63 in Lutzomyia longipalpis midgut binding. Moreover, our results suggest a critical role for GPI-anchored proteins and gp63 in Leishmania mexicana attachment to L. longipalpis midguts, as the wild type (WT) line accounted for over 99% of bound parasites.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2013 

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