Kilpatrick D R, Lipton H L
Department of Neurology, University of Colorado Health Sciences Center, Denver 80262.
J Virol. 1991 Oct;65(10):5244-9. doi: 10.1128/JVI.65.10.5244-5249.1991.
Western immunoblots of BHK-21 cell lysates probed with the highly virulent GDVII and the less virulent BeAn strains of Theiler's murine encephalomyelitis virus (TMEV) revealed predominant binding to a 34-kDa membrane protein and much lower levels of binding to 100- and 18-kDa membrane proteins. Complete inhibition of virus binding to both the 34- and 18-kDa membrane species by excess unlabeled TMEV demonstrated specificity of binding. Virus binding was also blocked by wheat germ agglutinin, which specifically binds to sialic acid residues and blocks TMEV binding to whole BHK-21 cells. Radiolabeled TMEV also bound to 100-, 34-, and 18-kDa membrane proteins expressed on other TMEV permissive cell lines but not on the nonpermissive cell lines tested. These data suggest that a 34-kDa cellular protein may be the primary determinant of susceptibility to TMEV infection by mediating the binding of GDVII and BeAn viruses to susceptible cells.
用高致病性的Theiler氏鼠脑脊髓炎病毒（TMEV）的GDVII株和低致病性的BeAn株对BHK - 21细胞裂解物进行蛋白质免疫印迹分析，结果显示主要与一种34 kDa的膜蛋白结合，而与100 kDa和18 kDa的膜蛋白的结合水平低得多。过量未标记的TMEV完全抑制病毒与34 kDa和18 kDa膜蛋白种类的结合，证明了结合的特异性。小麦胚芽凝集素也能阻断病毒结合，它特异性结合唾液酸残基并阻断TMEV与整个BHK - 21细胞的结合。放射性标记的TMEV也与其他TMEV允许的细胞系上表达的100 kDa、34 kDa和18 kDa膜蛋白结合，但不与所测试的非允许细胞系结合。这些数据表明，一种34 kDa的细胞蛋白可能是通过介导GDVII和BeAn病毒与易感细胞的结合来决定对TMEV感染易感性的主要因素。
