Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design
Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design
The surface of enveloped viruses can be extensively glycosylated. Unlike the glycans coating pathogens such as bacteria and fungi, glycans on viruses are added and processed by the host-cell during biosynthesis. Glycoproteins are typically subjected to α-mannosidase processing and Golgi-mediated glycosyltransferase extension to form complex-type glycans. In envelope viruses, exceptions to this default pathway are common and lead to the presence of oligomannose-type glycan structures on the virion surface. In one extreme example, HIV-1 utilises a high density of glycans to limit host antibody recognition of protein. However, the high density limits glycan processing and the resulting oligomannose structures can be recognised by broadly neutralising antibodies isolated from HIV-1 infected patients. Here we discuss how divergence from host-cell glycosylation can be targeted for vaccine design.
63-69
Crispin, Matthew
cd980957-0943-4b89-b2b2-710f01f33bc9
Doores, Katie J.
52d36150-7a62-4f9d-8348-c83a789d52e6
6 March 2015
Crispin, Matthew
cd980957-0943-4b89-b2b2-710f01f33bc9
Doores, Katie J.
52d36150-7a62-4f9d-8348-c83a789d52e6
Crispin, Matthew and Doores, Katie J.
(2015)
Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design.
Current Opinion in Virology, 11, .
(doi:10.1016/j.coviro.2015.02.002).
Abstract
The surface of enveloped viruses can be extensively glycosylated. Unlike the glycans coating pathogens such as bacteria and fungi, glycans on viruses are added and processed by the host-cell during biosynthesis. Glycoproteins are typically subjected to α-mannosidase processing and Golgi-mediated glycosyltransferase extension to form complex-type glycans. In envelope viruses, exceptions to this default pathway are common and lead to the presence of oligomannose-type glycan structures on the virion surface. In one extreme example, HIV-1 utilises a high density of glycans to limit host antibody recognition of protein. However, the high density limits glycan processing and the resulting oligomannose structures can be recognised by broadly neutralising antibodies isolated from HIV-1 infected patients. Here we discuss how divergence from host-cell glycosylation can be targeted for vaccine design.
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Published date: 6 March 2015
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Local EPrints ID: 414289
URI: http://eprints.soton.ac.uk/id/eprint/414289
ISSN: 1879-6257
PURE UUID: 12d87ede-dc75-4b59-947c-4b6e822da31c
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Date deposited: 25 Sep 2017 16:31
Last modified: 16 Mar 2024 04:30
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Author:
Katie J. Doores
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