Characterization of a region involved in binding of measles virus H protein and its receptor SLAM (CD150)

被引:20
作者
Hu, CL [1 ]
Zhang, P [1 ]
Liu, X [1 ]
Qi, YP [1 ]
Zou, TT [1 ]
Xu, Q [1 ]
机构
[1] Wuhan Univ, Inst Virol, Coll Life Sci, Wuhan 430072, Peoples R China
基金
中国国家自然科学基金;
关键词
measles virus; hemagglutinin protein; signaling lymphocyte activation molecule; phage display peptide library; receptor; peptide;
D O I
10.1016/j.bbrc.2004.02.106
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
Signaling lymphocyte activation molecule (SLAM; also known as CD150) is a newly identified cellular receptor for measles virus (MV). MV Hemagglutinin protein (H) mediates MV entry into host cells by specifically binding to SLAM. Amino acid 27-135 of SLAM was previously shown to be the functional domain to interact with H and used to screen a 10-mer phage display peptide library in this study. After four rounds of screening and sequence analysis, the deduced amino acid sequence of screened peptides SGFDPLITHA and SDWDPLFTHK showed to be highly homologous with amino acid 429-438 of MV H (SGFGPLITHG). Peptides SGFDPLITHA and SDWDPLFTHK specifically inhibited binding of H to SLAM and further inhibition of MV infection suggests that these peptides can be developed to MV blocking reagents and amino acid 429-438 in H protein is functionally involved in receptor binding and may constitute part of the receptor-binding determinants on H protein. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:698 / 704
页数:7
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