Cao W, Henry M D, Borrow P, Yamada H, Elder J H, Ravkov E V, Nichol S T, Compans R W, Campbell K P, Oldstone M B
Division of Virology, Department of Neuropharmacology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Science. 1998 Dec 11;282(5396):2079-81. doi: 10.1126/science.282.5396.2079.
A peripheral membrane protein that is interactive with lymphocytic choriomeningitis virus (LCMV) was purified from cells permissive to infection. Tryptic peptides from this protein were determined to be alpha-dystroglycan (alpha-DG). Several strains of LCMV and other arenaviruses, including Lassa fever virus (LFV), Oliveros, and Mobala, bound to purified alpha-DG protein. Soluble alpha-DG blocked both LCMV and LFV infection. Cells bearing a null mutation of the gene encoding DG were resistant to LCMV infection, and reconstitution of DG expression in null mutant cells restored susceptibility to LCMV infection. Thus, alpha-DG is a cellular receptor for both LCMV and LFV.
从允许感染的细胞中纯化出一种与淋巴细胞性脉络丛脑膜炎病毒(LCMV)相互作用的外周膜蛋白。该蛋白的胰蛋白酶肽段被确定为α- dystroglycan(α-DG)。几种LCMV毒株和其他沙粒病毒,包括拉沙热病毒(LFV)、奥利韦罗斯病毒和莫巴拉病毒,都与纯化的α-DG蛋白结合。可溶性α-DG可阻断LCMV和LFV感染。携带编码DG基因无效突变的细胞对LCMV感染具有抗性,在无效突变细胞中重建DG表达可恢复对LCMV感染的易感性。因此,α-DG是LCMV和LFV的细胞受体。