ArticleThe Journal of biological chemistry2010
Structural characterization of HIV gp41 with the membrane-proximal external region.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Article
- Neutralizing Antibodies Targeting HIV-1 gp41.Viruses · 2020Review
- NMR Structure of the FIV gp36 C-Terminal Heptad Repeat and Membrane-Proximal External Region.International journal of molecular sciences · 2020Article
- Structure of the membrane proximal external region of HIV-1 envelope glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.Biochemistry · 2018Article
- Article
- Modulating immunogenic properties of HIV-1 gp41 membrane-proximal external region by destabilizing six-helix bundle structure.Virology · 2016Article
- Immunogenic properties of a trimeric gp41-based immunogen containing an exposed membrane-proximal external region.Virology · 2015Article
- The membrane proximal external regions of gp41 from HIV-1 strains HXB2 and JRFL have different sensitivities to alanine mutation.Biochemistry · 2015Article
- Article
- Article
- Recombinant expression, purification, and biophysical characterization of the transmembrane and membrane proximal domains of HIV-1 gp41.Protein science : a publication of the Protein Society · 2014Article
- Article
- Mutations in the feline immunodeficiency virus envelope glycoprotein confer resistance to a dominant-negative fragment of Tsg101 by enhancing infectivity and cell-to-cell virus transmission.Biochimica et biophysica acta · 2014Article
- Carbohydrate-functionalized nanovaccines preserve HIV-1 antigen stability and activate antigen presenting cells.Journal of biomaterials science. Polymer edition · 2014Article
- Synchrotron X-ray footprinting on tour.Journal of synchrotron radiation · 2014Article
- Pushing the endogenous envelope.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Review
- Betaretroviral envelope subunits are noncovalently associated and restricted to the mammalian class.Journal of virology · 2013Article
- C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.The Journal of general virology · 2013Review
- Computer-Aided Approaches for Targeting HIVgp41.Biology · 2012Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Human immunodeficiency virus, type 1 (HIV-1) envelope glycoprotein (gp120/gp41) plays a critical role in virus infection and pathogenesis. Three of the six monoclonal antibodies considered to have broadly neutralizing activities (2F5, 4E10, and Z13e1) bind to the membrane-proximal external region (MPER) of gp41. This makes the MPER a desirable template for developing immunogens that can elicit antibodies with properties similar to these monoclonal antibodies, with a long term goal of developing antigens that could serve as novel HIV vaccines. In order to provide a structural basis for rational antigen design, an MPER construct, HR1-54Q, was generated for x-ray crystallographic and x-ray footprinting studies to provide both high resolution atomic coordinates and verification of the solution state of the antigen, respectively. The crystal structure of HR1-54Q reveals a trimeric, coiled-coil six-helical bundle, which probably represents a postfusion form of gp41. The MPER portion extends from HR2 in continuation of a slightly bent long helix and is relatively flexible. The structures observed for the 2F5 and 4E10 epitopes agree well with existing structural data, and enzyme-linked immunosorbent assays indicate that the antigen binds well to antibodies that recognize the above epitopes. Hydroxyl radical-mediated protein footprinting of the antigen in solution reveals specifically protected and accessible regions consistent with the predictions based on the trimeric structure from the crystallographic data. Overall, the HR1-54Q antigen, as characterized by crystallography and footprinting, represents a postfusion, trimeric form of HIV gp41, and its structure provides a rational basis for gp41 antigen design suitable for HIV vaccine development.
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