Cross-Neutralizing Human Monoclonal Anti-HIV-1 Antibody 2F5: Preparation and Crystallographic Analysis of the Free and Epitope-Complexed Forms of its F ab Fragment

Title: Cross-Neutralizing Human Monoclonal Anti-HIV-1 Antibody 2F5: Preparation and Crystallographic Analysis of the Free and Epitope-Complexed Forms of its F ab Fragment

Volume: 8 Issue: 5

Author(s): Steve Bryson, Annie Cunningham, Jason Ho, Rosemary C. Hynes, David E. Isenman, Brian H. Barber, Renate Kunert, Hermann Katinger, Michel Klein and Emil F. Pai

Affiliation:

Keywords: CROSS-NEUTRALIZING, CRYSTALLOGRAPHIC ANALYSIS, peptide complex

Abstract: The human monoclonal antibody 2F5 is a potent neutralizer of most clades of HIV-1 and possesses protective effects against viral transmission. It recognizes the linear epitope ELDKWAS of the viral envelope protein gp41. As structural information about epitope recognition may help to develop an HIV-1 vaccine we initiated crystallographic analyses of mAb 2F5 and its epitope complex. We now report the preparation of the corresponding Fab fragments, complexation with the epitope peptide, and crystallization of free mAb 2F5 Fab as well as the peptide complex. Both crystal forms are well suited for high-resolution structural analysis.

Cite this article as:

Bryson Steve, Cunningham Annie, Ho Jason, Hynes C. Rosemary, Isenman E. David, Barber H. Brian, Kunert Renate, Katinger Hermann, Klein Michel and Pai F. Emil, Cross-Neutralizing Human Monoclonal Anti-HIV-1 Antibody 2F5: Preparation and Crystallographic Analysis of the Free and Epitope-Complexed Forms of its F ab Fragment, Protein & Peptide Letters 2001; 8 (5) . https://dx.doi.org/10.2174/0929866013409201