一种抗HIV-1蛋白酶抗体与HIV-2蛋白酶肽之间交叉反应复合物的晶体结构。

Crystal structure of a cross-reaction complex between an anti-HIV-1 protease antibody and an HIV-2 protease peptide.

作者信息

Rezacova Pavlina, Brynda Jiri, Lescar Julien, Fabry Milan, Horejsi Magda, Sieglova Irena, Sedlacek Juraj, Bentley Graham A

机构信息

Department of Recombinant Expression and Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Flemingovo nam. 2, 166 37 Prague 6, Czech Republic.

出版信息

J Struct Biol. 2005 Mar;149(3):332-7. doi: 10.1016/j.jsb.2004.11.009.

DOI:10.1016/j.jsb.2004.11.009

PMID:15721587

Abstract

The monoclonal antibody 1696, elicited by HIV-1 protease, inhibits the activity of both HIV-1 and HIV-2 proteases with inhibition constants in the low nanomolar range. The antibody cross-reacts with peptides derived from the N-terminal region of both proteases. The crystal structure of the recombinant single-chain Fv fragment of 1696 complexed with an N-terminal peptide from the HIV-2 protease has been determined at 1.88A resolution. Interactions of the peptide with scFv1696 are compared with the previously reported structure of scFv1696 in complex with the corresponding peptide from HIV-1 protease. The origin of cross-reactivity of mAb1696 with HIV proteases is discussed.

摘要

由HIV-1蛋白酶引发的单克隆抗体1696可抑制HIV-1和HIV-2蛋白酶的活性，其抑制常数处于低纳摩尔范围。该抗体与两种蛋白酶N端区域衍生的肽发生交叉反应。已在1.88埃分辨率下测定了与HIV-2蛋白酶N端肽复合的重组单链Fv片段1696的晶体结构。将该肽与scFv1696的相互作用与先前报道的scFv1696与HIV-1蛋白酶相应肽复合的结构进行了比较。讨论了单克隆抗体1696与HIV蛋白酶交叉反应的起源。