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
Authors: Steve Bryson1; Annie Cunningham1; Jason Ho1; Rosemary C. Hynes1; David E. Isenman1; Brian H. Barber1; Renate Kunert1; Hermann Katinger1; Michel Klein1; Emil F. Pai1
Source: Protein and Peptide Letters, Volume 8, Number 5, October 2001 , pp. 413-418(6)
Publisher: Bentham Science Publishers
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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
Document Type: Review article
DOI: 10.2174/0929866013409201
Affiliations: 1: Departments of Biochemistry, Immunology, Medical Biophysics and Molecular and Medical Genetics and Protein Engineering Network - Centres of Excellence, University of Toronto,Canada
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