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Characterization of a midgut mucin-like glycoconjugate of Lutzomyia longipalpis with a potential role in Leishmania attachment

Overview of attention for article published in Parasites & Vectors, July 2016
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Title
Characterization of a midgut mucin-like glycoconjugate of Lutzomyia longipalpis with a potential role in Leishmania attachment
Published in
Parasites & Vectors, July 2016
DOI 10.1186/s13071-016-1695-y
Pubmed ID
Authors

Jitka Myšková, Anna Dostálová, Lucie Pěničková, Petr Halada, Paul A. Bates, Petr Volf

Abstract

Leishmania parasites are transmitted by phlebotomine sand flies and a crucial step in their life-cycle is the binding to the sand fly midgut. Laboratory studies on sand fly competence to Leishmania parasites suggest that the sand flies fall into two groups: several species are termed "specific/restricted" vectors that support the development of one Leishmania species only, while the others belong to so-called "permissive" vectors susceptible to a wide range of Leishmania species. In a previous study we revealed a correlation between specificity vs permissivity of the vector and glycosylation of its midgut proteins. Lutzomyia longipalpis and other four permissive species tested possessed O-linked glycoproteins whereas none were detected in three specific vectors examined. We used a combination of biochemical, molecular and parasitological approaches to characterize biochemical and biological properties of O-linked glycoprotein of Lu. longipalpis. Lectin blotting and mass spectrometry revealed that this molecule with an apparent molecular weight about 45-50 kDa corresponds to a putative 19 kDa protein with unknown function detected in a midgut cDNA library of Lu. longipalpis. We produced a recombinant glycoprotein rLuloG with molecular weight around 45 kDa. Anti-rLuloG antibodies localize the native glycoprotein on epithelial midgut surface of Lu. longipalpis. Although we could not prove involvement of LuloG in Leishmania attachment by blocking the native protein with anti-rLuloG during sand fly infections, we demonstrated strong binding of rLuloG to whole surface of Leishmania promastigotes. We characterized a novel O-glycoprotein from sand fly Lutzomyia longipalpis. It has mucin-like properties and is localized on the luminal side of the midgut epithelium. Recombinant form of the protein binds to Leishmania parasites in vitro. We propose a role of this molecule in Leishmania attachment to sand fly midgut.

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Mendeley readers

The data shown below were compiled from readership statistics for 23 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 23 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 6 26%
Student > Ph. D. Student 5 22%
Student > Bachelor 5 22%
Student > Master 2 9%
Other 1 4%
Other 1 4%
Unknown 3 13%
Readers by discipline Count As %
Agricultural and Biological Sciences 9 39%
Biochemistry, Genetics and Molecular Biology 7 30%
Immunology and Microbiology 1 4%
Physics and Astronomy 1 4%
Chemistry 1 4%
Other 0 0%
Unknown 4 17%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 15 December 2017.
All research outputs
#9,428,332
of 12,299,992 outputs
Outputs from Parasites & Vectors
#2,040
of 3,120 outputs
Outputs of similar age
#172,552
of 266,590 outputs
Outputs of similar age from Parasites & Vectors
#99
of 137 outputs
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