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HIV-1 subtype C envelope function becomes less sensitive to N-glycosylation deletion during disease progression

dc.contributor.authorLumngwena, Evelyn N.en_ZA
dc.contributor.authorShuping, Liliween_ZA
dc.contributor.authorBernitz, Netanyaen_ZA
dc.contributor.authorWoodman, Zendaen_ZA
dc.date.accessioned2019-06-26T06:34:45Z
dc.date.available2019-06-26T06:34:45Z
dc.date.issued2019-06-17
dc.identifier.citationLumngwena, E. N., et al. 2019. HIV-1 subtype C envelope function becomes less sensitive to N-glycosylation deletion during disease progression. BMC Research Notes, 12:340, doi:10.1186/s13104-019-4375-0
dc.identifier.issn1756-0500 (online)
dc.identifier.otherdoi:10.1186/s13104-019-4375-0
dc.identifier.urihttp://hdl.handle.net/10019.1/106294
dc.descriptionCITATION: Lumngwena, E. N., et al. 2019. HIV-1 subtype C envelope function becomes less sensitive to N-glycosylation deletion during disease progression. BMC Research Notes, 12:340, doi:10.1186/s13104-019-4375-0.
dc.descriptionThe original publication is available at https://bmcresnotes.biomedcentral.com
dc.description.abstractObjective: As part of a larger study to understand how Envelope N-glycosylation influences HIV-1 pathogenesis, we selected a participant infected with a single Subtype C variant and determined whether deletion of specific potential N-glycan sites (PNGs) impacted Envelope function longitudinally. Results: We deleted five PNGs previously linked to HIV-1 transmission of two matched Envelope clones representing variants at 5 and 173 weeks post-infection. The transmitted founder (TF) had significantly better pseudovirus entry efficiency than the chronic infection (CI) variant. Deletion of all PNGs significantly reduced TF entry efficiency, binding to dendritic cell-specific intracellular adhesion molecule 3 grabbing non-integrin (DC-SIGN) receptor and transinfection. However, mutational analysis did not affect the phenotype of the CI Envelope to the same extent. Notably, deletion of the PNGs at N241 and N448 had no effect on CI Envelope function, suggesting that some PNGs might only be important during acute infection. Therefore, vaccines that elicit antibodies against N-glycans important for TF Envelope function could drive the loss of PNGs during immune escape, abrogating viral replication. Conversely, changes in N-glycosylation might have no effect on some variants, reducing vaccine efficacy. This finding highlights the need for further investigation into the role of Envelope N-glycosylation in HIV-1 pathogenesis.
dc.description.urihttps://bmcresnotes.biomedcentral.com/articles/10.1186/s13104-019-4375-0
dc.format.extent6 pages
dc.language.isoen_ZAen_ZA
dc.publisherBMC (part of Springer Nature)
dc.subjectHIV-1
dc.titleHIV-1 subtype C envelope function becomes less sensitive to N-glycosylation deletion during disease progressionen_ZA
dc.typeArticle
dc.date.updated2019-06-25T16:58:41Z
dc.description.versionPublisher's version
dc.rights.holderAuthors retain copyright


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