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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Nat+Microbiol
2016 ; 2
(ä): 16199
Nephropedia Template TP
gab.com Text
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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
PMID27841852
show ga
The induction by vaccination of broadly neutralizing antibodies (bNAbs) capable
of neutralizing various HIV-1 viral strains 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-electron
microscopy 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.