Elicitation of Neutralizing Antibodies Targeting the V2 Apex of the HIV Envelope Trimer in a Wild-Type Animal Model
Year: 2018
Type: article
Abstract: (Cell Reports 21, 222–235; October 3, 2017) In the originally published version of this article, a statement in the discussion was not updated to reflect the data finally presented in Figure 1. The original publication contained the following statement: (3) “Differing V2-apex iP reactivity. The most effective immunogens, C108 and CRF250, bind all of the PG9, CH01, and CAP256 prototype iPs, while WITO and MGRM8 are neutralized by only two of these antibodies. Further, WITO and MGRM8 SOSIPs showed the poorest binding to iP/UCA antibodies by BLI, suggesting there are potentially fewer ways for them to trigger naive BCRs.” This statement has now been replaced by the following revision: (3) “Differing V2-apex iP reactivity. One of the more effective immunogens, CRF250, binds all of the PG9, CH01, and CAP256 precursor antibodies, suggesting there are potentially multiple ways for this trimer specifically to engage V2-apex-directed naive BCRs and giving it a potential advantage with regard to nAb elicitation.” The authors apologize for this error. Elicitation of Neutralizing Antibodies Targeting the V2 Apex of the HIV Envelope Trimer in a Wild-Type Animal ModelVoss et al.Cell ReportsOctober 03, 2017In BriefVoss et al. show that select V2-apex-focusing immunogens derived from bnAb precursor neutralization-sensitive HIV isolates can reproducibly elicit autologous neutralizing responses to components of the bnAb epitope, including K169/K171 and N156, in a wild-type animal model. Full-Text PDF Open Access
Source: Cell Reports
Language: English
Topic: HIV Research and Treatment
Subfield: Virology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $5,620
OpenAlex ID: W4239873003