crystal structure and size-dependent neutralization properties of hk20, a human monoclonal antibody binding to the highly conserved heptad repeat 1 of gp41晶体结构和尺度依赖的中和hk20的性质,人类单克隆抗体绑定到高度保守的七个重复gp41 1.pdf

Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41 1. 2.¤ 1. 3 1 1 Charles Sabin , Davide Corti , Victor Buzon , Mike S. Seaman , David Lutje Hulsik , Andreas Hinz , 4 4 2 5 5 2 Fabrizia Vanzetta , Gloria Agatic , Chiara Silacci , Lara Mainetti , Gabriella Scarlatti , Federica Sallusto , 6 2,7 1 Robin Weiss , Antonio Lanzavecchia , Winfried Weissenhorn * ´ 1 Unit of Virus Host Cell Interactions (UVHCI) UMI 3265, Universite Joseph Fourier-EMBL-CNRS, Grenoble, France, 2 Institute for Research in Biomedicine, Bellinzona, Switzerland, 3 Division of Viral Pathogenesis, Beth Israel Deaconess Medical Center, Boston, Massachusetts, United States of America, 4 Humabs SAGL, Bellinzona, Switzerland, 5 Viral Evolution and Transmission Unit, Division of Immunology, Transplant and Infectious Diseases, San Raffaele Scientific Institute, Milan, Ita ly, 6 Division of Infection and Immunity, University College London, London, United Kingdom, 7 Institute of Microbiology, Swiss Federal Institute of Technology, Zurich, Switzerland Abstract The human monoclonal antibody (mAb) HK20 neutralizes a broad spectrum of primary HIV-1 isolates by targeting the highly conserved heptad repeat 1 (HR1) of gp41, which is transiently exposed during HIV-1 entry. Here we pr