ArticlePloS one2011
HIV-1 gp41 core with exposed membrane-proximal external region inducing broad HIV-1 neutralizing antibodies.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Immune Correlate-Guided HIV Vaccine Design.Cell host & microbe · 2018Review
- The development of HIV vaccines targeting gp41 membrane-proximal external region (MPER): challenges and prospects.Protein & cell · 2018Review
- Article
- The Membrane-Proximal Region of C-C Chemokine Receptor Type 5 Participates in the Infection of HIV-1.Frontiers in immunology · 2017Article
- Immunogenic properties of a trimeric gp41-based immunogen containing an exposed membrane-proximal external region.Virology · 2015Article
- Sample-free quantification of blood biomarkers via laser-treated skin.Biomaterials · 2015Article
- Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.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
- A fusion intermediate gp41 immunogen elicits neutralizing antibodies to HIV-1.The Journal of biological chemistry · 2014Article
- Development and immunological assessment of VLP-based immunogens exposing the membrane-proximal region of the HIV-1 gp41 protein.Journal of biomedical science · 2014Article
- Immunization with hybrid proteins containing the membrane proximal external region of HIV-1.AIDS research and human retroviruses · 2014Article
- Article
- Novel neutralising antibodies targeting the N-terminal helical region of the transmembrane envelope protein p15E of the porcine endogenous retrovirus (PERV).Immunologic research · 2014Article
- Article
- Immunisation with foamy virus Bet fusion proteins as novel strategy for HIV-1 epitope delivery.Immunologic research · 2013Article
- Designing a soluble near full-length HIV-1 gp41 trimer.The Journal of biological chemistry · 2013Article
- Chimeric rhinoviruses displaying MPER epitopes elicit anti-HIV neutralizing responses.PloS one · 2013Article
- Neutralizing antibodies and control of HIV: moves and countermoves.Current HIV/AIDS reports · 2012Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The membrane-proximal external region (MPER) of the HIV-1 gp41 consists of epitopes for the broadly cross-neutralizing monoclonal antibodies 2F5 and 4E10. However, antigens containing the linear sequence of these epitopes are unable to elicit potent and broad neutralizing antibody responses in vaccinated hosts, possibly because of inappropriate conformation of these epitopes. Here we designed a recombinant antigen, designated NCM, which comprises the N- and C-terminal heptad repeats that can form a six-helix bundle (6HB) core and the MPER domain of gp41. Two mutations (T569A and I675V) previously reported to expose the neutralization epitopes were introduced into NCM to generate mutants named NCM(TA), NCM(IV), and NCM(TAIV). Our results showed that NCM and its mutants could react with antibodies specific for 6HB and MPER of gp41, suggesting that these antigens are in the form of a trimer of heterodimer (i.e., 6HB) with three exposed MPER tails. Antigen with double mutations, NCM(TAIV), elicited much stronger antibody response in rabbits than immunogens with single mutation, NCM(TA) and NCM(IV), or no mutation, NCM. The purified MPER-specific antibodies induced by NCM(TAIV) exhibited broad neutralizing activity, while the purified 6HB-specific antibodies showed no detectable neutralizing activity. Our recombinant antigen design supported by an investigation of its underlying molecular mechanisms provides a strong scientific platform for the discovery of a gp41 MPER-based AIDS vaccine.
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