Boat T F, Davis J, Stern R C, Cheng P W
Biochim Biophys Acta. 1978 Apr 19;540(1):127-33. doi: 10.1016/0304-4165(78)90441-5.
We have demonstrated that the inhibitor of influenza B virus hemagglutination in human saliva is inactivated by neuraminidase and is associated with the mucous glycoprotein fraction (blood group substance) of this secretion. Inhibitory activity of saliva was found to be roughly proportional to its sialic acid content (r = 0.456). However, the minimal quantity of salivary sialic acid, neutral sugar, or blood group antigen required to inhibit virus hemagglutination was greater for secretors of A and B than for secretors of H and Lea blood group substances. Removal of terminal galactose from blood group B substance with alpha-galactosidase markedly decreased blood group B activity but increased blood group H and virus hemagglutination inhibitory activities of this glycoprotein. These data suggest that terminal alpha-linked galactose and, probably, N-acetyl-galactosamine interfere with access of influenza virus to binding sites on oligosaccharide chains of the mucous glycoprotein.
我们已经证明,人类唾液中抑制乙型流感病毒血凝的物质会被神经氨酸酶灭活,并且与该分泌物的黏液糖蛋白部分(血型物质)相关。发现唾液的抑制活性大致与其唾液酸含量成正比(r = 0.456)。然而,抑制病毒血凝所需的唾液酸、中性糖或血型抗原的最小量,A和B血型分泌者比H和Lea血型物质分泌者要多。用α-半乳糖苷酶去除B型血型物质末端的半乳糖,会显著降低B型血型活性,但会增加该糖蛋白的H型血型和病毒血凝抑制活性。这些数据表明,末端α-连接的半乳糖,可能还有N-乙酰半乳糖胺,会干扰流感病毒与黏液糖蛋白寡糖链上结合位点的接触。