表面活性蛋白A与呼吸道合胞病毒的融合糖蛋白结合，并中和病毒体的感染性。

Surfactant protein A binds to the fusion glycoprotein of respiratory syncytial virus and neutralizes virion infectivity.

作者信息

Ghildyal R, Hartley C, Varrasso A, Meanger J, Voelker D R, Anders E M, Mills J

机构信息

Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.

出版信息

J Infect Dis. 1999 Dec;180(6):2009-13. doi: 10.1086/315134.

DOI:10.1086/315134

PMID:10558959

Abstract

Collectins are a family of calcium-dependent collagenous lectins that appear to be important in innate host defense. We investigated the ability of three human collectins, namely, lung surfactant proteins A (SP-A) and D (SP-D) and the serum mannose-binding protein (MBP), to bind to the surface glycoproteins of respiratory syncytial virus (RSV). SP-A was shown to bind to the F (fusion) glycoprotein but not to the viral G (attachment) glycoprotein, and binding was completely abrogated in the presence of EDTA. Neither SP-D nor MBP bound to either glycoprotein. SP-A also neutralized RSV in a calcium dependent fashion. These results support a role for SP-A in the defense of infants against infection with RSV and indicate a possible mechanism for its protective activity.

摘要

凝集素是一类钙依赖性胶原凝集素，在宿主天然防御中似乎起着重要作用。我们研究了三种人类凝集素，即肺表面活性蛋白A（SP-A）和D（SP-D）以及血清甘露糖结合蛋白（MBP）与呼吸道合胞病毒（RSV）表面糖蛋白结合的能力。结果显示，SP-A能与F（融合）糖蛋白结合，但不与病毒G（附着）糖蛋白结合，且在EDTA存在的情况下结合完全被消除。SP-D和MBP均不与这两种糖蛋白结合。SP-A还以钙依赖的方式中和RSV。这些结果支持了SP-A在保护婴儿免受RSV感染方面的作用，并提示了其保护活性的可能机制。