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

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

Journal Name: Protein & Peptide Letters

Volume 8 , Issue 5 , 2001

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.

Keywords: CROSS-NEUTRALIZING, CRYSTALLOGRAPHIC ANALYSIS, peptide complex

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Article Details

VOLUME: 8
ISSUE: 5
Year: 2001
Page: [413 - 418]
Pages: 6
DOI: 10.2174/0929866013409201
Price: $58

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