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Sökning: onr:"swepub:oai:gup.ub.gu.se/239532" > Global Mapping of O...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003987naa a2200481 4500
001oai:gup.ub.gu.se/239532
003SwePub
008240528s2016 | |||||||||||000 ||eng|
0247 a https://gup.ub.gu.se/publication/2395322 URI
0247 a https://doi.org/10.1074/jbc.M116.7217462 DOI
040 a (SwePub)gu
041 a eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Bagdonaite, I.4 aut
2451 0a Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus
264 1c 2016
520 a 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.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicinx Infektionsmedicin0 (SwePub)302092 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Clinical Medicinex Infectious Medicine0 (SwePub)302092 hsv//eng
653 a herpes-simplex-virus
653 a cell-cell fusion
653 a insulin-degrading enzyme
653 a transferase gene family
653 a n-linked glycans
653 a glycoprotein b
653 a envelope
653 a protein
653 a epithelial-cells
653 a viral replication
653 a crystal-structure
653 a Biochemistry & Molecular Biology
7001 a Nordén, Rickard,d 1977u Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine4 aut0 (Swepub:gu)xnorri
7001 a Joshi, H. J.4 aut
7001 a King, S. L.4 aut
7001 a Vakhrushev, S. Y.4 aut
7001 a Olofsson, Sigvard,d 1948u Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine4 aut0 (Swepub:gu)xolosi
7001 a Wandall, H. H.4 aut
7102 a Göteborgs universitetb Institutionen för biomedicin, avdelningen för infektionssjukdomar4 org
7730 t Journal of Biological Chemistryg 291:23, s. 12014-12028q 291:23<12014-12028x 0021-9258
8564 8u https://gup.ub.gu.se/publication/239532
8564 8u https://doi.org/10.1074/jbc.M116.721746

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