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10.1038/nmicrobiol.2016.199

http://scihub22266oqcxt.onion/10.1038/nmicrobiol.2016.199
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suck abstract from ncbi


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pmid27841852      Nat+Microbiol 2016 ; 2 (ä): 16199
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  • An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability #MMPMID27841852
  • van Gils MJ; van den Kerkhof TL; Ozorowski G; Cottrell CA; Sok D; Pauthner M; Pallesen J; de Val N; Yasmeen A; de Taeye SW; Schorcht A; Gumbs S; Johanna I; Saye-Francisco K; Liang CH; Landais E; Nie X; Pritchard LK; Crispin M; Kelsoe G; Wilson IA; Schuitemaker H; Klasse PJ; Moore JP; Burton DR; Ward AB; Sanders RW
  • Nat Microbiol 2016[Nov]; 2 (ä): 16199 PMID27841852show ga
  • The induction of broadly HIV-1 neutralizing antibodies (bNAbs), capable of neutralizing various viral strains, by vaccination is challenging, but understanding how a subset of HIV-infected individuals develops bNAbs may guide immunization strategies. Here, we describe the isolation and characterization of the bNAb ACS202 from an elite neutralizer that recognizes a new, trimer-specific and cleavage-dependent epitope at the gp120-gp41 interface of the envelope glycoprotein (Env), involving the glycan N88 and the gp41 fusion peptide. In addition, an Env trimer, AMC011 SOSIP.v4.2, based on early virus isolates from the same elite neutralizer, was constructed and its structure by cryo-EM at 6.2 Å resolution reveals a closed, pre-fusion conformation similar to that of the BG505 SOSIP.664 trimer. The availability of a native-like Env trimer and a bNAb from the same elite neutralizer provides the opportunity to design vaccination strategies aimed at generating similar bNAbs against a key functional site on HIV-1.
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