Role of Glycosylation/Deglycolysation Processes in Francisella tularensis Pathogenesis
is able to invade, survive and replicate inside a variety of cell types. However, preferentially enters host macrophages where it rapidly escapes to the cytosol to avoid phagosomal stresses and to multiply to high numbers. We previously showed that human monocyte infection by LVS triggered deglycosy...
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Published in | Frontiers in cellular and infection microbiology Vol. 7; p. 71 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Switzerland
Frontiers Media S.A
21.03.2017
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Subjects | |
Online Access | Get full text |
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Summary: | is able to invade, survive and replicate inside a variety of cell types. However,
preferentially enters host macrophages where it rapidly escapes to the cytosol to avoid phagosomal stresses and to multiply to high numbers. We previously showed that human monocyte infection by
LVS triggered deglycosylation of the glutamine transporter SLC1A5. However, this deglycosylation, specifically induced by
infection, was not restricted to SLC1A5, suggesting that host protein deglycosylation processes in general might contribute to intracellular bacterial adaptation. Indeed, we later found that
infection modulated the transcription of numerous glycosidase and glycosyltransferase genes in human macrophages and analysis of cell extracts revealed an important increase of N and O-protein glycosylation. In eukaryotic cells, glycosylation has significant effects on protein folding, conformation, distribution, stability, and activity and dysfunction of protein glycosylation may lead to development of diseases like cancer and pathogenesis of infectious diseases. Pathogenic bacteria have also evolved dedicated glycosylation machineries and have notably been shown to use these glycoconjugates as ligands to specifically interact with the host. In this review, we will focus on
and summarize our current understanding of the importance of these post-translational modifications on its intracellular niche adaptation. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 Reviewed by: Jiri Stulik, University of Defence, Czechia; Paul Edward Carlson, Food and Drug Administration, USA Edited by: Marina Santic', University of Rijeka, Croatia |
ISSN: | 2235-2988 2235-2988 |
DOI: | 10.3389/fcimb.2017.00071 |