STRUCTURAL AND FUNCTIONAL-ANALYSIS OF THE SURFACE PROTEIN OF HUMAN CORONAVIRUS OC43
STRUCTURAL AND FUNCTIONAL-ANALYSIS OF THE SURFACE PROTEIN OF HUMAN CORONAVIRUS OC43
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DOI：
10.1006/viro.1993.1360
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发表时间：
1993-07-01
期刊：
影响因子：
3.7
通讯作者：
HERRLER, G
中科院分区：
文献类型：
--
作者：
KUNKEL, F;HERRLER, G
从人冠状病毒OC 43（HCV-OC 43）的病毒膜中分离纯化了两种表面糖蛋白S和HE。只有S蛋白能够凝集鸡红细胞，表明该病毒蛋白是HCV-OC 43的主要血凝素。该病毒在红细胞表面识别的受体决定簇是N-乙酰基-9-O-乙酰基神经氨酸（Neu 5，9Ac 2），牛冠状病毒也使用该受体决定簇附着于细胞。通过分析两种连接类型中含有不同量Neu 5，9Ac 2的红细胞，发现两种病毒对9-O-乙酰化唾液酸的亲和力存在细微差异。牛冠状病毒在识别与半乳糖连接的少量Neu 5，9Ac 2 β 2，3方面更有效，而HCV-OC 43在β 2，6连接方面更上级。克隆了HCV-OC 43株S蛋白基因并进行了序列测定。一个大的开放阅读框预测一个非糖基化形式的150 kDa多肽。如果将20个潜在糖基化位点用于连接N-连接寡糖侧链，则预期蛋白质约为190 kDa。这些预测证实了在体外转录和翻译的基因在犬胰腺微粒体膜的存在或不存在。HCV-OC 43与牛冠状病毒的S蛋白序列有很高的同源性。更多菌株的结构和功能分析应有助于确定唾液酸结合位点的位置。
The two surface glycoproteins S and HE of human coronavirus OC43 (HCV-OC43) were isolated from the viral membrane and purified. Only the S protein was able to agglutinate chicken erythrocytes, indicating that this viral protein is the major hemagglutinin of HCV-OC43. The receptor determinant recognized by this virus on the surface of erythrocytes isN-acetyl-9-O-acetylneuraminic acid (Neu5,9Ac2) which is also used by bovine coronavirus for attachment to cells. By analyzing erythrocytes containing different amounts of Neu5,9Ac2in either of two linkage types, it was found that there are subtle differences in the affinity of both viruses for 9-O-acetylated sialic acid. Bovine coronavirus was more efficient in recognizing low amounts of Neu5,9Ac2β2,3 linked to galactose, whereas HCV-OC43 was superior with respect to the β2,6 linkage. The gene coding for the S protein of HCV-OC43 was cloned and sequenced. A large open reading frame predicts a polypeptide of 150 kDa in the unglycosylated form. A protein of about 190 kDa is expected if the 20 potential glycosylation sites are used for attachment of N-linked oligosaccharide side chains. These predictions were confirmed byin vitrotranscription and translation of the gene in the presence or absence of canine pancreatic microsomal membranes. A high degree of sequence homology was found between the S proteins of HCV-OC43 and bovine coronavirus. Structural and functional analyses of more strains should help to identify the location of the sialic acid-binding site.