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Updated: Jan 21, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Published on: September 14, 2014
Variability OF HIV-1 V2 env domain for integrin binding: Clinical correlates
Claudia Fabrizio1, Davide F Bavaro2, Luigia Scudeller3
1Clinic of Infectious Diseases, University of Bari, University Hospital Policlinico, Piazza Giulio Cesare n. 11, 70124, Bari, Italy; Malattie Infettive e Tropicali Ospedale Oncologico San Giuseppe Moscati, Taranto, Italy.
Abstract:
The HIV V2179-181 (HXB2 numbering) tripeptide mediates binding to α4β7 integrin, which is responsible for GALT homing. Our study aimed to assess V2 variability in naive HIV-1 infected patients and its association with clinical and viro-immunological features. Gp120 sequences were obtained from 322 subjects; length, potential N-linked glycosylation sites (PNGs), net-charge (NC) and 179-181tripeptide α4β7-binding-motif of V2 were evaluated. At multivariate analysis, lower V2 length and higher NC correlated with low CD4 cells; no association was found with PNGs. A greater variability pertained positions 162-163, 164-167, 169, 175-179, 187, 194 and 195 in B sequences, and 163 and 177 in X4 tropic viruses. LDV was the most common tripeptide. Asp180 was highly conserved; Leu179 was more frequently observed in non-B and in recent infections compared to others, while Val181 was found in recent infections and in MSM. Further studies to deeply explore the clinical significance of these associations are warranted.
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