Recombinant protein of heptad-repeat HR212, a stable fusion inhibitor with potent anti-HIV action in vitro
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چکیده
منابع مشابه
Membrane-Anchored HIV-1 N-Heptad Repeat Peptides Are Highly Potent Cell Fusion Inhibitors via an Altered Mode of Action
Peptide inhibitors derived from HIV-gp41 envelope protein play a pivotal role in deciphering the molecular mechanism of HIV-cell fusion. According to accepted models, N-heptad repeat (NHR) peptides can bind two targets in an intermediate fusion conformation, thereby inhibiting progression of the fusion process. In both cases the orientation towards the endogenous intermediate conformation shoul...
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During HIV-1 fusion to the host cell membrane, the N-terminal heptad repeat (NHR) and the C-terminal heptad repeat (CHR) of the envelope subunit gp41 become transiently exposed and accessible to fusion inhibitors or Abs. In this process, the NHR region adopts a trimeric coiled-coil conformation that can be a target for therapeutic intervention. Here, we present an approach to rationally design ...
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Peptides derived from N-terminal heptad repeat (NHR) of the HIV-1 gp41 are generally poor inhibitors of HIV-1 entry because these peptides tend to aggregate and do not form a trimeric coiled coil. In this study, we have fused portions of gp41 NHR, e.g., N36 or N28, to the T4 fibritin trimerization domain, Foldon (Fd), thus constructing novel NHR-trimers, designated N36Fd or N28Fd, which could b...
متن کاملMutations in the fusion peptide and heptad repeat regions of the Newcastle disease virus fusion protein block fusion.
Nonconservative mutations were introduced by site-specific mutagenesis into the fusion peptide and the adjacent heptad repeat region of the fusion protein of Newcastle disease virus in order to determine the role of both regions in the fusion activity of the protein. Mutations in both regions that allowed for proper folding and intracellular transport of the protein blocked the fusion activity ...
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ژورنال
عنوان ژورنال: Virology
سال: 2008
ISSN: 0042-6822
DOI: 10.1016/j.virol.2008.04.013