爱泼斯坦-巴尔病毒的BNLF-1膜蛋白LMP1在鼠B细胞系中诱导由CD11a/CD18介导的同型黏附，模拟佛波酯的作用。
The Epstein-Barr virus BNLF-1 membrane protein LMP1 induces homotypic adhesion mediated by CD11a/CD18 in a murine B-cell line, mimicking the action of phorbol ester.
作者信息
Salcedo R, Fuerstenberg S M, Patarroyo M, Winberg G
机构信息
Department of Immunology, Karolinska Institutet, Stockholm, Sweden.
出版信息
J Virol. 1991 Oct;65(10):5558-63. doi: 10.1128/JVI.65.10.5558-5563.1991.
Abstract
Expression of the Epstein-Barr virus BNLF1 gene (LMP1) or treatment with 4B-phorbol-12,13-dibutyrate in the murine pro-B-cell line A/J-95 leads to a five- to sevenfold enhancement of homotypic adhesion without significant changes in adhesion molecule expression. Antibody to CD11a inhibits aggregation, indicating that CD11a/CD18-mediated adhesion is a common target for both agents.
摘要
在小鼠前B细胞系A/J - 95中，爱泼斯坦-巴尔病毒BNLF1基因（LMP1）的表达或用4β-佛波醇-12,13-二丁酸酯处理会导致同型黏附增强5至7倍，而黏附分子的表达没有显著变化。抗CD11a抗体可抑制聚集，这表明CD11a/CD18介导的黏附是这两种因子的共同作用靶点。
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