WFRF:(Bally Marta)
Search: WFRF:(Bally Marta) > Structure and Role ...
- 47 of 62
- Previous record
- Next record
- To hitlist
Structure and Role of O-Linked Glycans in Viral Envelope Proteins
-
- Olofsson, Sigvard, 1948 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine,Department of Infectious Diseases, Institute of Biomedicine, Sahlgrenska Academy at the University of Gothenburg, Gothenburg, Sweden; email:
-
- Bally, Marta (author)
- Umeå universitet,Institutionen för klinisk mikrobiologi,Umeå Centre for Microbial Research (UCMR),Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM)
-
- Trybala, Edward, 1955 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine,Department of Infectious Diseases, Institute of Biomedicine, Sahlgrenska Academy at the University of Gothenburg, Gothenburg, Sweden; email: sigvard.olofsson@gu.se
- show more...
- show less...
- (creator_code:org_t)
- Annual Reviews, 2023
- 2023
- English.
- In: Annual Review of Virology. - : Annual Reviews. - 2327-056X. ; 10:1, s. 283-304
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- N- and O-glycans are both important constituents of viral envelope glycoproteins. O-linked glycosylation can be initiated by any of 20 different human polypeptide O-acetylgalactosaminyl transferases, resulting in an important functional O-glycan heterogeneity. O-glycans are organized as solitary glycans or in clusters of multiple glycans forming mucin-like domains. They are functional both in the viral life cycle and in viral colonization of their host. Negatively charged O-glycans are crucial for the interactions between glycosaminoglycan-binding viruses and their host. A novel mechanism, based on controlled electrostatic repulsion, explains how such viruses solve the conflict between optimized viral attachment to target cells and efficient egress of progeny virus. Conserved solitary O-glycans appear important for viral uptake in target cells by contributing to viral envelope fusion. Dual roles of viral O-glycans in the host B cell immune response, either epitope blocking or epitope promoting, may be exploitable for vaccine development. Finally, specific virus-induced O-glycans may be involved in viremic spread.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
Keyword
- mucin-like domain
- heparan sulfate
- chondroitin sulfate
- vaccine
- attachment
- virion
- egress
- attachment
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
- Annual Review of Virology (Search for host publication in LIBRIS)
To the university's database
- 47 of 62
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Olofsson, Sigvar ...
- Bally, Marta
- Trybala, Edward, ...
- Bergström, Tomas ...
- About the subject
-
- MEDICAL AND HEALTH SCIENCES
- MEDICAL AND HEAL ...
- and Basic Medicine
- and Microbiology in ...
-
- MEDICAL AND HEALTH SCIENCES
- MEDICAL AND HEAL ...
- and Medical Biotechn ...
- and Medical Biotechn ...
- Articles in the publication
- Annual Review of ...
- Annual review of ...
- By the university
- University of Gothenburg
- Umeå University
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
