Structural Analysis of the Unmutated Ancestor of the HIV-1 Envelope V2 Region Antibody CH58 Isolated from an RV144 Vaccine Efficacy Trial Vaccinee

Nicely N, et al., 20;2(7):713-22, EBioMedicine, 2015

In this article, the authors are reporting the structural and biophysical characterization of an ancestral HIV-1 envelope V2 region human monoclonal antibody known as CH58 (CH58-UA). This antibody was isolated from an RV144-vaccine efficacy trial vaccinee. The crystal structures of CH58-UA antibody with or without V2 peptide allowed understanding of how V2 responses are developed. The epitope mapping experiments carried out on a BIAcore 4000 SPR instrument served as the basis for Ala scanning experiments. A Pall ForteBio Octet RED96 instrument equipped with Streptavidin biosensors allowed identification of binding partners via affinity maturation. Biotinylated gp120165-182 peptides captured by the Streptavidin biosensors were screened against CH58-UA and mature CH58 Fabs.

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