Exploitation of glycosylation in enveloped virus pathobiology
Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including...
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Published in | Biochimica et biophysica acta. General subjects Vol. 1863; no. 10; pp. 1480 - 1497 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.10.2019
The Author(s). Published by Elsevier B.V |
Subjects | |
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Abstract | Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection. In this review, we highlight the imperative and auxiliary roles glycans play, and how specific oligosaccharide structures facilitate these functions during viral pathogenesis. We discuss the growing efforts to exploit viral glycobiology in the development of anti-viral vaccines and therapies.
•Enveloped viruses often hijack host-cell glycosylation pathways.•Viral glycans have multifaceted influences on pathobiology.•Glycans have intrinsic functionalities but can also be influenced by immune selection.•Viral glycobiology is emerging as an important parameter during vaccine design. |
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AbstractList | Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection. In this review, we highlight the imperative and auxiliary roles glycans play, and how specific oligosaccharide structures facilitate these functions during viral pathogenesis. We discuss the growing efforts to exploit viral glycobiology in the development of anti-viral vaccines and therapies.Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection. In this review, we highlight the imperative and auxiliary roles glycans play, and how specific oligosaccharide structures facilitate these functions during viral pathogenesis. We discuss the growing efforts to exploit viral glycobiology in the development of anti-viral vaccines and therapies. Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection. In this review, we highlight the imperative and auxiliary roles glycans play, and how specific oligosaccharide structures facilitate these functions during viral pathogenesis. We discuss the growing efforts to exploit viral glycobiology in the development of anti-viral vaccines and therapies. Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection. In this review, we highlight the imperative and auxiliary roles glycans play, and how specific oligosaccharide structures facilitate these functions during viral pathogenesis. We discuss the growing efforts to exploit viral glycobiology in the development of anti-viral vaccines and therapies. • Enveloped viruses often hijack host-cell glycosylation pathways. • Viral glycans have multifaceted influences on pathobiology. • Glycans have intrinsic functionalities but can also be influenced by immune selection. • Viral glycobiology is emerging as an important parameter during vaccine design. Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection. In this review, we highlight the imperative and auxiliary roles glycans play, and how specific oligosaccharide structures facilitate these functions during viral pathogenesis. We discuss the growing efforts to exploit viral glycobiology in the development of anti-viral vaccines and therapies. •Enveloped viruses often hijack host-cell glycosylation pathways.•Viral glycans have multifaceted influences on pathobiology.•Glycans have intrinsic functionalities but can also be influenced by immune selection.•Viral glycobiology is emerging as an important parameter during vaccine design. |
Author | Crispin, Max Wilson, Ian A. Watanabe, Yasunori Bowden, Thomas A. |
AuthorAffiliation | d Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA a School of Biological Sciences and Institute of Life Sciences, University of Southampton, Southampton SO17 1BJ, UK e Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA b Division of Structural Biology, University of Oxford, Wellcome Centre for Human Genetics, Oxford OX3 7BN, UK c Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK |
AuthorAffiliation_xml | – name: a School of Biological Sciences and Institute of Life Sciences, University of Southampton, Southampton SO17 1BJ, UK – name: c Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK – name: d Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – name: e Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – name: b Division of Structural Biology, University of Oxford, Wellcome Centre for Human Genetics, Oxford OX3 7BN, UK |
Author_xml | – sequence: 1 givenname: Yasunori surname: Watanabe fullname: Watanabe, Yasunori organization: School of Biological Sciences and Institute of Life Sciences, University of Southampton, Southampton SO17 1BJ, UK – sequence: 2 givenname: Thomas A. surname: Bowden fullname: Bowden, Thomas A. organization: Division of Structural Biology, University of Oxford, Wellcome Centre for Human Genetics, Oxford OX3 7BN, UK – sequence: 3 givenname: Ian A. surname: Wilson fullname: Wilson, Ian A. organization: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 4 givenname: Max surname: Crispin fullname: Crispin, Max email: max.crispin@soton.ac.uk organization: School of Biological Sciences and Institute of Life Sciences, University of Southampton, Southampton SO17 1BJ, UK |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31121217$$D View this record in MEDLINE/PubMed |
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SubjectTerms | animal pathogens Dengue virus Ebolavirus Glycan shielding glycomics Glycoprotein Glycoproteins - metabolism Glycosylation Host-Pathogen Interactions Human immunodeficiency virus 1 Humans Immune Evasion Lassa mammarenavirus Molecular Mimicry oligosaccharides Orthomyxoviridae parasites pathogenesis polysaccharides Polysaccharides - metabolism Protein Folding Protein Transport Structure vaccines viral envelope proteins Virus Virus Physiological Phenomena Virus-host interactions viruses Viruses - immunology Viruses - metabolism Zika virus |
Title | Exploitation of glycosylation in enveloped virus pathobiology |
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