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Structure-based Vaccine Design in HIV: Blind Men and the Elephant?

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Traditional vaccine approaches have failed for HIV and novel strategies are now being sought to develop immunogens designed to elicit specific activity against known broad neutralization epitopes. Structure-based vaccine design has great potential but, so far, remains a largely unproven concept. Further structural information for the envelope (Env) glycoproteins, gp120 and gp41, would be extremely beneficial, particularly for understanding trimer-specific antibodies and their epitopes and to clarify the atomic details of the structural elements responsible for masking crucial epitopes and for mediating the conformational rearrangements undertaken during the process of receptor-binding and membrane fusion.

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Keywords: B cell; CD4 binding site; CD4-induced; Gly-Ala-Gly; HIV; HIV-1 envelope; HIV-1 trimer; HIV-1 vaccine; HJ16; High-Mannose Glycan Cluster; Hyperglycosylation; SIV mac239 trimers; T cell; T-lymphotropic virus; VRC01; Vaccine; Z13e1; anti-retroviral therapy; antibodies; broadly neutralizing antibodies; cryoelectron tomography; ebola virus; glycoproteins; glycosylation; gp120; gp41; human respiratory syncytial virus; immunogen; influenza virus; leukemia; monoclonal antibodies; neutralization; visna virus

Document Type: Research Article

Publication date: November 1, 2010

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  • Current Pharmaceutical Design publishes timely in-depth reviews covering all aspects of current research in rational drug design. Each issue is devoted to a single major therapeutic area. A Guest Editor who is an acknowledged authority in a therapeutic field has solicits for each issue comprehensive and timely reviews from leading researchers in the pharmaceutical industry and academia.

    Each thematic issue of Current Pharmaceutical Design covers all subject areas of major importance to modern drug design, including: medicinal chemistry, pharmacology, drug targets and disease mechanism.
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