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Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus

The Journal of biological chemistry, 2016-06, Vol.291 (23), p.12014-12028 [Peer Reviewed Journal]

2016 © 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. 2016 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M116.721746 ;PMID: 27129252

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Title:
Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus
Author: Bagdonaite, Ieva ; Nordén, Rickard ; Joshi, Hiren J. ; King, Sarah L. ; Vakhrushev, Sergey Y. ; Olofsson, Sigvard ; Wandall, Hans H.
Subjects: Binding Sites ; Biochemistry & Molecular Biology ; Cell Line ; cell-cell fusion ; crystal-structure ; Cytomegalovirus - metabolism ; Cytomegalovirus - physiology ; envelope ; epithelial-cells ; Fibroblasts - virology ; Glycobiology and Extracellular Matrices ; glycoprotein b ; Glycoproteins - metabolism ; Glycosylation ; herpes-simplex-virus ; Herpesvirus 3, Human - metabolism ; Herpesvirus 3, Human - physiology ; Herpesvirus 4, Human - metabolism ; Herpesvirus 4, Human - physiology ; Host-Pathogen Interactions ; Humans ; Infectious Medicine ; Infektionsmedicin ; insulin-degrading enzyme ; Mass Spectrometry - methods ; n-linked glycans ; Polysaccharides - metabolism ; protein ; Proteome - metabolism ; Proteomics - methods ; transferase gene family ; Viral Envelope Proteins - metabolism ; viral replication ; Virus Diseases - virology ; Virus Internalization
Is Part Of: The Journal of biological chemistry, 2016-06, Vol.291 (23), p.12014-12028
Description: Herpesviruses are among the most complex and widespread viruses, infection and propagation of which depend on envelope proteins. These proteins serve as mediators of cell entry as well as modulators of the immune response and are attractive vaccine targets. Although envelope proteins are known to carry glycans, little is known about the distribution, nature, and functions of these modifications. This is particularly true for O-glycans; thus we have recently developed a “bottom up” mass spectrometry-based technique for mapping O-glycosylation sites on herpes simplex virus type 1. We found wide distribution of O-glycans on herpes simplex virus type 1 glycoproteins and demonstrated that elongated O-glycans were essential for the propagation of the virus. Here, we applied our proteome-wide discovery platform for mapping O-glycosites on representative and clinically significant members of the herpesvirus family: varicella zoster virus, human cytomegalovirus, and Epstein-Barr virus. We identified a large number of O-glycosites distributed on most envelope proteins in all viruses and further demonstrated conserved patterns of O-glycans on distinct homologous proteins. Because glycosylation is highly dependent on the host cell, we tested varicella zoster virus-infected cell lysates and clinically isolated virus and found evidence of consistent O-glycosites. These results present a comprehensive view of herpesvirus O-glycosylation and point to the widespread occurrence of O-glycans in regions of envelope proteins important for virus entry, formation, and recognition by the host immune system. This knowledge enables dissection of specific functional roles of individual glycosites and, moreover, provides a framework for design of glycoprotein vaccines with representative glycosylation.
Publisher: United States: Elsevier Inc
Language: English
Identifier: ISSN: 0021-9258
EISSN: 1083-351X
DOI: 10.1074/jbc.M116.721746
PMID: 27129252
Source: MEDLINE
PubMed Central
Alma/SFX Local Collection

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Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus

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