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鉴定麻疹病毒血凝素(MVH)与其人类细胞受体(信号淋巴细胞激活分子,SLAM)相互作用中涉及的氨基酸残基。

Identification of amino acid residues involved in the interaction between measles virus Haemagglutin (MVH) and its human cell receptor (signaling lymphocyte activation molecule, SLAM).

作者信息

Xu Qin, Zhang Peng, Hu Chunling, Liu Xin, Qi Yipeng, Liu Yingle

机构信息

State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, P. R. China.

出版信息

J Biochem Mol Biol. 2006 Jul 31;39(4):406-11. doi: 10.5483/bmbrep.2006.39.4.406.

Abstract

Signaling lymphocyte activation molecule (SLAM; also known as CD150) is a newly identified cellular receptor for measles virus (MV). The interaction between MV Haemagglutin (MVH) and SLAM is an initial step for MV entry. We have identified several novel SLAM binding sites at residues S429, T436 and H437 of MVH protein and MVH mutants in these residues dramatically decrease the ability to interaction with the cell surface SLAM and fail to coprecipitation with SLAM in vivo as well as malfunction in syncytium formation. At the same time, K58, S59 and H61 of SLAM was also identified to be critical for MVH and SLAM binding. Further, these residues may be useful targets for the development of measles therapy.

摘要

信号淋巴细胞激活分子(SLAM;也称为CD150)是一种新发现的麻疹病毒(MV)细胞受体。MV血凝素(MVH)与SLAM之间的相互作用是MV进入细胞的起始步骤。我们在MVH蛋白的S429、T436和H437残基处鉴定出了几个新的SLAM结合位点,这些残基处的MVH突变体显著降低了与细胞表面SLAM相互作用的能力,在体内无法与SLAM共沉淀,并且在合胞体形成中功能异常。同时,SLAM的K58、S59和H61也被确定对MVH与SLAM的结合至关重要。此外,这些残基可能是麻疹治疗药物开发的有用靶点。

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