INTERACTION OF MOUSE HEPATITIS-VIRUS (MHV) SPIKE GLYCOPROTEIN WITH RECEPTOR GLYCOPROTEIN MHVR IS REQUIRED FOR INFECTION WITH AN MHV STRAIN THAT EXPRESSES THE HEMAGGLUTININ-ESTERASE GLYCOPROTEIN
INTERACTION OF MOUSE HEPATITIS-VIRUS (MHV) SPIKE GLYCOPROTEIN WITH RECEPTOR GLYCOPROTEIN MHVR IS REQUIRED FOR INFECTION WITH AN MHV STRAIN THAT EXPRESSES THE HEMAGGLUTININ-ESTERASE GLYCOPROTEIN
复制标题
DOI：
10.1128/jvi.69.2.889-895.1995
复制
发表时间：
1995-02-01
影响因子：
5.4
通讯作者：
HOLMES, KV
中科院分区：
文献类型：
--
作者：
GAGNETEN, S;GOUT, O;HOLMES, KV
除了与宿主细胞膜上的癌胚抗原相关受体结合的刺突（S）糖蛋白外，一些小鼠冠状病毒（小鼠肝炎病毒[MHV]）毒株还表达具有血凝和乙酰酯酶活性的血凝素酯酶（HE）糖蛋白。不表达HE的毒株的病毒粒子，如MHV-A59，可以在体外感染小鼠成纤维细胞，表明HE糖蛋白不是感染这些细胞所必需的。本工作是为了研究在S糖蛋白与其受体糖蛋白MKVR没有相互作用的情况下，HE糖蛋白与碳水化合物部分的相互作用是否会导致病毒进入和感染。MHV的DVIM株表达大量的HE糖蛋白，如血细胞吸附、乙酰酯酶活性和与针对牛冠状病毒的HE糖蛋白的抗体的免疫反应性所示。单克隆抗MHVR抗体MAb-CC 1阻断病毒S糖蛋白与MHVR的结合，并阻断不表达HE的MHV毒株的感染。MAb-CC 1还防止小鼠DBT细胞和原代小鼠神经胶质细胞培养物的MHV-DVIM感染。尽管MDCK-I细胞在其质膜上表达O-乙酰化唾液酸残基，但这些犬细胞对MHV-A59和MHV-DVIM感染具有抗性。用MHVR cDNA转染MDCK-1细胞，使其对MHV-A59和MHV-DVIM感染敏感。因此，MHV株的HE糖蛋白不会导致培养的鼠神经细胞或表达HE糖蛋白的碳水化合物配体的非鼠细胞的感染。因此，MHV的刺突糖蛋白与其癌胚抗原相关受体糖蛋白的相互作用是MHV株的感染性所必需的，无论它们是否表达HE糖蛋白。
In addition to the spike (S) glycoprotein that binds to carcinoembryonic antigen-related receptors on the host cell membrane, some strains of mouse coronavirus (mouse hepatitis virus [MHV]) express a hemagglutinin esterase (HE) glycoprotein with hemagglutinating and acetylesterase activity. Virions of strains that do not express HE, such as MHV-A59, can infect mouse fibroblasts in vitro, showing that the HE glycoprotein is not required for infection of these cells. The present work was done to study whether interaction of the HE glycoprotein with carbohydrate moieties could lead to virus entry and infection in the absence of interaction of the S glycoprotein with its receptor glycoprotein, MKVR. The DVIM strain of MHV expresses large amounts of HE glycoprotein, as shown by hemadsorption, acetylesterase activity, and immunoreactivity with antibodies directed against the HE glycoprotein of bovine coronavirus. A monoclonal anti-MHVR antibody, MAb-CC1, blocks binding of virus S glycoprotein to MHVR and blocks infection of MHV strains that do not express HE. MAb-CC1 also prevented MHV-DVIM infection of mouse DBT cells and primary mouse glial cell cultures. Although MDCK-I cells express O-acetylated sialic acid residues on their plasma membranes, these canine cells were resistant to infection with MHV-A59 and MHV-DVIM. Transfection of MDCK-I cells,vith MHVR cDNA made them susceptible to infection with MHV-A59 and MHV-DVIM. Thus, the HE glycoprotein of an MHV strain did not lead to infection of cultured murine neural cells or of nonmurine cells that express the carbohydrate ligand of the HE glycoprotein. Therefore, interaction of the spike glycoprotein of MHV with its carcinoembryonic antigen-related receptor glycoprotein is required for infectivity of MHV strains whether or not they express the HE glycoprotein.