天花病毒CrmB蛋白单独合成的肿瘤坏死因子结合域的生物学效应

Biological effects of individually synthesized TNF-binding domain of variola virus CrmB protein.

作者信息

Tsyrendorzhiev D D, Orlovskaya I A, Sennikov S V, Tregubchak T V, Gileva I P, Tsyrendorzhieva M D, Shchelkunov S N

机构信息

Research Institute of Clinical Immunology, Siberian Division of the Russian Academy of Medical Sciences, Novosibirsk, Russia,

出版信息

Bull Exp Biol Med. 2014 Jun;157(2):249-52. doi: 10.1007/s10517-014-2537-6. Epub 2014 Jun 22.

DOI:10.1007/s10517-014-2537-6

PMID:24952494

Abstract

The biological characteristics of a 17-kDa protein synthesized in bacterial cells, a TNF-binding domain (VARV-TNF-BP) of a 47-kDa variola virus CrmB protein (VARV-CrmB) consisting of TNF-binding and chemokine-binding domains, were studied. Removal of the C-terminal chemokine-binding domain from VARV-CrmB protein was inessential for the efficiency of its inhibition of TNF cytotoxicity towards L929 mouse fibroblast culture and for TNF-induced oxidative metabolic activity of mouse blood leukocytes. The results of this study could form the basis for further studies of VARV-TNF-BP mechanisms of activity for prospective use in practical medicine.

摘要

对在细菌细胞中合成的一种17 kDa蛋白（由47 kDa天花病毒CrmB蛋白（VARV-CrmB）的肿瘤坏死因子（TNF）结合域（VARV-TNF-BP）组成，该蛋白包含TNF结合域和趋化因子结合域）的生物学特性进行了研究。从VARV-CrmB蛋白中去除C端趋化因子结合域，对于其抑制TNF对L929小鼠成纤维细胞培养物的细胞毒性效率以及TNF诱导的小鼠血液白细胞氧化代谢活性而言并非必需。本研究结果可为进一步研究VARV-TNF-BP的活性机制奠定基础，以便未来应用于实际医学。