Karen A Kirby, Yee Tsuey Ong, Atsuko Hachiya, Thomas G Laughlin, Leslie A Chiang, Yun Pan, Jennifer L Moran, Bruno Marchand, Kamalendra Singh, Fabio Gallazzi, Thomas P Quinn, Kazuhisa Yoshimura, Toshio Murakami, Shuzo Matsushita, Stefan G Sarafianos
Humanized monoclonal antibody KD-247 targets the Gly(312)-Pro(313)-Gly(314)-Arg(315) arch of the third hypervariable (V3) loop of the HIV-1 surface glycoprotein. It potently neutralizes many HIV-1 clade B isolates, but not of other clades. To understand the molecular basis of this specificity, we solved a high-resolution (1.55 Å) crystal structure of the KD-247 antigen binding fragment and examined the potential interactions with various V3 loop targets. Unlike most antibodies, KD-247 appears to interact with its target primarily through light chain residues...
January 2015: FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology