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 gly...
| Auteurs principaux: | , |
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| Format: | Journal article |
| Langue: | English |
| Publié: |
Elsevier
2015
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| _version_ | 1826293690232995840 |
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| author | Crispin, M Doores, K |
| author_facet | Crispin, M Doores, K |
| author_sort | Crispin, M |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T03:34:02Z |
| format | Journal article |
| id | oxford-uuid:bbb0682d-cb3b-410a-83e0-71d25e963de8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:34:02Z |
| publishDate | 2015 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:bbb0682d-cb3b-410a-83e0-71d25e963de82022-03-27T05:18:48ZTargeting host-derived glycans on enveloped viruses for antibody-based vaccine designJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:bbb0682d-cb3b-410a-83e0-71d25e963de8EnglishSymplectic Elements at OxfordElsevier2015Crispin, MDoores, KThe 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. |
| spellingShingle | Crispin, M Doores, K Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design |
| title | Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design |
| title_full | Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design |
| title_fullStr | Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design |
| title_full_unstemmed | Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design |
| title_short | Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design |
| title_sort | targeting host derived glycans on enveloped viruses for antibody based vaccine design |
| work_keys_str_mv | AT crispinm targetinghostderivedglycansonenvelopedvirusesforantibodybasedvaccinedesign AT dooresk targetinghostderivedglycansonenvelopedvirusesforantibodybasedvaccinedesign |