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

Simple item page
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.date.updated2019-06-25T16:58:41Z
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.en_ZA
dc.description.urihttps://bmcresnotes.biomedcentral.com/articles/10.1186/s13104-019-4375-0
dc.description.versionPublisher's version
dc.format.extent6 pagesen_ZA
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.language.isoen_ZAen_ZA
dc.publisherBMC (part of Springer Nature)en_ZA
dc.rights.holderAuthors retain copyrighten_ZA
dc.subjectHIV-1en_ZA
dc.subjectGlycosylationen_ZA
dc.subjectDisease managementen_ZA
dc.subjectPathogenic bacteriaen_ZA
dc.titleHIV-1 subtype C envelope function becomes less sensitive to N-glycosylation deletion during disease progressionen_ZA
dc.typeArticleen_ZA
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
lumngwena_hiv_2019.pdf
Size:
1.01 MB
Format:
Adobe Portable Document Format
Description:
Download article
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
0 B
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Research Articles (Molecular Biology and Human Genetics)