ArticleProtein science : a publication of the Protein Society2007
The disulfide loop of gp41 is critical to the furin recognition site of HIV gp160.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 21 citations in OpenAlex.
- HIV-1 envelope facilitates the development of protease inhibitor resistance through acquiring mutations associated with viral entry and immune escape.Frontiers in microbiology · 2024Article
- Peptide Triazole Thiol Irreversibly Inactivates Metastable HIV-1 Env by Accessing Conformational Triggers Intrinsic to Virus-Cell Entry.Microorganisms · 2021Article
- The CH1α domain of mucosal gp41 IgA contributes to antibody specificity and antiviral functions in HIV-1 highly exposed Sero-Negative individuals.PLoS pathogens · 2020Article
- Oocyte-specific deletion of furin leads to female infertility by causing early secondary follicle arrest in mice.Cell death & disease · 2017Article
- Molecular and Physicochemical Factors Governing Solubility of the HIV gp41 Ectodomain.Biophysical journal · 2016Article
- Furin Cleavage of L2 during Papillomavirus Infection: Minimal Dependence on Cyclophilins.Journal of virology · 2016Article
- Inhibition of HIV Entry by Targeting the Envelope Transmembrane Subunit gp41.Current HIV research · 2016Review
- Synthesis, antiviral activity and resistance of a novel small molecule HIV-1 entry inhibitor.Bioorganic & medicinal chemistry · 2015Article
- Epitope target structures of Fc-mediated effector function during HIV-1 acquisition.Current opinion in HIV and AIDS · 2014Review
- Review
- Viral envelope protein folding and membrane hemifusion are enhanced by the conserved loop region of HIV-1 gp41.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- Secreted antiviral entry inhibitory (SAVE) peptides for gene therapy of HIV infection.Molecular therapy : the journal of the American Society of Gene Therapy · 2011Article
- HIV envelope: challenges and opportunities for development of entry inhibitors.Trends in microbiology · 2011Review
- A low-molecular-weight entry inhibitor of both CCR5- and CXCR4-tropic strains of human immunodeficiency virus type 1 targets a novel site on gp41.Journal of virology · 2010Article
- Short communication: Simultaneous substitutions of V38M and N43T-N44K in the gp41 heptad repeat 1 (HR1) disrupt HIV type 1 gPr160 endoproteolytic cleavage (*).AIDS research and human retroviruses · 2010Article
- Article
- Role of the HIV gp120 conserved domain 1 in processing and viral entry.The Journal of biological chemistry · 2008Article
- Peptide mimic of the HIV envelope gp120-gp41 interface.Journal of molecular biology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The importance of the HIV gp41 conserved disulfide loop to envelope function has been examined by mutational and functional analyses. Based on a luciferase-reporter entry assay, mutants gp41-CC/AA (C598A/C604A) and gp41-Delta (deletion of residues 596-606) result in a nonfunctional envelope protein. Western blot analysis shows both mutants to be properly expressed but not processed to form gp120 and gp41, which explains their nonfunctionality. The presence of mutant gp160 on the cell surface, as well as their ability to bind to sCD4, suggests that the mutations have disrupted processing at the furin recognition site encoded within the gp120 conserved domain 5, without resulting in an overall misfolding of the protein. With respect to the furin recognition site, the mutations are sequentially distant, which implies that the gp41 disulfide loop is interacting with gp120 C5 in gp160. In addition, we have modeled the gp120-gp41 interaction in unprocessed precursor gp160 using structural data available for gp120 and gp41 domains in isolation, supplemented by mutagenesis data. We suggest that the mutations have altered the interaction between gp120 C5 and the gp41 disulfide loop, resulting in decreased accessibility of the furin recognition site and implying that the interaction between the gp120 C5 and gp41 loop is a conformational requirement for gp160 processing. The sensitivity of this interaction could be exploited in future antivirals designed to disrupt HIV pathogenesis by disrupting gp160 processing.
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Registered trials
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.