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GP120 Mass Spectrometry Data to Analyse N-Glycosylation

ABSTRACT: Analysis of gp120 N-glycosylation. N-linked glycosylation sites of gp120 were interrogated for the presence of 55 glycoforms from chronic vs acute HIV virions.

INSTRUMENT(S):

ORGANISM(S): Human Immunodeficiency Virus 1

TISSUE(S): Microglial Cell

DISEASE(S): Disease Free

SUBMITTER: Carole Creuzenet

LAB HEAD: Carole Creuzenet

PROVIDER: PXD067311 | Pride | 2026-04-13

REPOSITORIES: Pride

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			Action	DRS
	20230324_UVPD_CDS_CreuzenetC_B4-1A.mzML	Mzml
	20230324_UVPD_CDS_CreuzenetC_B4-1A.raw	Raw
	20230324_UVPD_CDS_CreuzenetC_B4-1Ab.raw	Raw
	20230324_UVPD_CDS_CreuzenetC_B4-1B.mzML	Mzml
	20230324_UVPD_CDS_CreuzenetC_B4-1B.raw	Raw

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Publications

Comprehensive analysis of gp120 glycosylation to explore differences between transmitter/founder and chronic HIV-1 isolates.

Temesy Stephen S Haly Jordan J Sun Yingxue Y Patel Mukti M Zebian Najwa N Saha Repon R Galappaththi Sashini Loku SL Zhang Yiying Y Twells Nick N Mahal Lara K LK Arts Eric J EJ Creuzenet Carole C

Glycobiology 20260301 5

The extraordinary genetic diversity of HIV variants and their differences in glycosylation of surface protein gp120 have hindered developing a universal vaccine. Via lectin-mediated interactions, the gp120 glycans may trap viruses at the mucosal interface, enhance trans-infection of CD4+ T cells, or enhance HIV uptake for antigen presentation while limiting such presentation by inhibiting gp120 proteolysis. Also, variations in numbers and location of glycosylation sites may allow escape from eme ...[more]

PMID: 41885535

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Variability in the Glycosylation Patterns of gp120 Proteins from Different Human Immunodeficiency Virus Type 1 Isolates Expressed in Different Host Cells

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