Cross-neutralizing human monoclonal anti-HIV-1 antibody 2F5:: Preparation and crystallographic analysis of the free and epitope-complexed forms of its Fab′ fragment

被引：11

作者：

Bryson, S

Cunningham, A

Ho, J

Hynes, RC

Isenman, DE

Barber, BH

Kunert, R

Katinger, H

Klein, M

Pai, EF

机构：

[1] Univ Toronto, Ctr Excellence, Dept Biochem, Toronto, ON M5S 1A8, Canada

[2] Univ Toronto, Ctr Excellence, Dept Immunol, Toronto, ON M5S 1A8, Canada

[3] Univ Toronto, Ctr Excellence, Dept Med Biophys, Toronto, ON M5S 1A8, Canada

[4] Univ Toronto, Ctr Excellence, Dept Mol & Med Genet, Toronto, ON M5S 1A8, Canada

[5] Univ Toronto, Ctr Excellence, Prot Engn Network, Toronto, ON M5S 1A8, Canada

[6] Princess Margaret Hosp, Ontario Canc Inst, Div Mol & Struct Biol, Toronto, ON M5G 2M9, Canada

[7] Agr Univ Vienna, Inst Appl Microbiol, A-1190 Vienna, Austria

[8] Aventis Pasteur, Res & Dev, F-69280 Marcy Letoile, France

来源：

PROTEIN AND PEPTIDE LETTERS | 2001年 / 8卷 / 05期

关键词：

D O I：

10.2174/0929866013409201

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：413 / 418

页数：6

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