ArticleJournal of virology1994
Evidence for a functional interaction between the V1/V2 and C4 domains of human immunodeficiency virus type 1 envelope glycoprotein gp120.
Article in Journal of virology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
98 citing papers in PubMed, 131 citations in OpenAlex.
- Natural variations at the E433 site in Env-gp120 β20-β21 cooperate with V2 and gp41 mutations to modulate HIV-1 infectivity.Frontiers in microbiology · 2026Article
- Rab11-FIP1C Is Dispensable for HIV-1 Replication in Primary CD4Journal of virology · 2022Article
- Elucidating the Basis for Permissivity of the MT-4 T-Cell Line to Replication of an HIV-1 Mutant Lacking the gp41 Cytoplasmic Tail.Journal of virology · 2020Article
- The viral protein U (Vpu)-interacting host protein ATP6V0C down-regulates cell-surface expression of tetherin and thereby contributes to HIV-1 release.The Journal of biological chemistry · 2020Article
- Authentication Analysis of MT-4 Cells Distributed by the National Institutes of Health AIDS Reagent Program.Journal of virology · 2019Article
- Genomic tagging of endogenous human ESCRT-I complex preserves ESCRT-mediated membrane-remodeling functions.The Journal of biological chemistry · 2019Article
- Mutations in the HIV-1 envelope glycoprotein can broadly rescue blocks at multiple steps in the virus replication cycle.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The KT Jeang Retrovirology prize 2018: Eric Freed.Retrovirology · 2018Article
- Experimental Estimation of the Effects of All Amino-Acid Mutations to HIV's Envelope Protein on Viral Replication in Cell Culture.PLoS pathogens · 2016Article
- Structure-Activity Relationships of the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PF-46396.Journal of virology · 2016Article
- In Vivo Analysis of Infectivity, Fusogenicity, and Incorporation of a Mutagenic Viral Glycoprotein Library Reveals Determinants for Virus Incorporation.Journal of virology · 2016Article
- Structural and Molecular Determinants of Membrane Binding by the HIV-1 Matrix Protein.Journal of molecular biology · 2016Article
- The Vpu-interacting Protein SGTA Regulates Expression of a Non-glycosylated Tetherin Species.Scientific reports · 2016Article
- Elucidation of the Molecular Mechanism Driving Duplication of the HIV-1 PTAP Late Domain.Journal of virology · 2016Article
- Envelope gene evolution and HIV-1 neuropathogenesis.Journal of neuroinfectious diseases · 2015Article
- Multifunctional RNA nanoparticles.Nano letters · 2014Article
- Partial rescue of V1V2 mutant infectivity by HIV-1 cell-cell transmission supports the domain's exceptional capacity for sequence variation.Retrovirology · 2014Article
- In COS cells Vpu can both stabilize tetherin expression and counteract its antiviral activity.PloS one · 2014Article
- Dual-acting stapled peptides target both HIV-1 entry and assembly.Retrovirology · 2013Article
- HIV-1 variable loop 2 and its importance in HIV-1 infection and vaccine development.Current HIV research · 2013Article
38 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The domains of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein that are required for envelope function have been partially characterized. Little is known, however, about the nature of the interactions between these domains. To identify regions of the HIV-1 envelope glycoprotein that are involved in interactions necessary for proper envelope function, we constructed a series of 14 envelope recombinants between the env genes of two HIV-1 isolates. The envelope chimeras were examined for their ability to induce syncytia, to be proteolytically processed, and to function during a spreading viral infection. Our results demonstrate that the exchange between the two isolates of the first and second hypervariable regions (V1/V2) of gp120 results in defects in envelope glycoprotein processing, syncytium formation, and infectivity. Long-term passage of cultures infected with virus bearing a V1/V2 chimeric envelope glycoprotein leads to the emergence of a revertant virus with replication characteristics comparable to those of the wild type. Analysis of the revertant indicated that an Ile-->Met change in the C4 region of gp120 (between hypervariable regions V4 and V5) is responsible for the revertant phenotype. This single amino acid change restores infectivity without significantly affecting gp160 processing, CD4 binding, or the levels of virion-associated gp120. While the Ile-->Met change in C4 greatly enhances the fusogenic potential of the V1/V2 chimeric envelope glycoprotein, it has a detrimental effect on syncytium formation when analyzed in the context of the wild-type envelope. These results suggest that an interaction required for proper envelope glycoprotein function occurs between the V1/V2 and C4 regions of gp120.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.