Insights into the salivary N-glycome of Lutzomyia longipalpis, vector of visceral leishmaniasis

Karina Mondragon-Shem, Katherine Wongtrakul-Kish, Radoslaw P. Kozak, Shi Yan, Iain B. H. Wilson, Katharina Paschinger, Matthew E. Rogers, Daniel I. R. Spencer, Alvaro Acosta-Serrano*

*Corresponding author for this work

Research output: Contribution to journalArticle

Abstract

During Leishmania transmission sand flies inoculate parasites and saliva into the skin of vertebrates. Saliva has anti-haemostatic and anti-inflammatory activities that evolved to facilitate bloodfeeding, but also modulate the host’s immune responses. Sand fly salivary proteins have been extensively studied, but the nature and biological roles of protein-linked glycans remain overlooked. Here, we characterised the profile of N-glycans from the salivary glycoproteins of Lutzomyia longipalpis, vector of visceral leishmaniasis in the Americas. In silico predictions suggest half of Lu. longipalpis salivary proteins may be N-glycosylated. SDS-PAGE coupled to LC–MS analysis of sand fly saliva, before and after enzymatic deglycosylation, revealed several candidate glycoproteins. To determine the diversity of N-glycan structures in sand fly saliva, enzymatically released sugars were fluorescently tagged and analysed by HPLC, combined with highly sensitive LC–MS/MS, MALDI-TOF–MS, and exoglycosidase treatments. We found that the N-glycan composition of Lu. longipalpis saliva mostly consists of oligomannose sugars, with Man5GlcNAc2 being the most abundant, and a few hybrid-type species. Interestingly, some glycans appear modified with a group of 144 Da, whose identity has yet to be confirmed. Our work presents the first detailed structural analysis of sand fly salivary glycans.
Original languageEnglish
Article number12903
Number of pages11
JournalScientific Reports
Volume10
DOIs
Publication statusPublished - 31 Jul 2020
Externally publishedYes

Bibliographical note

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