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

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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.

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Ghildyal, R., Hartley, C., Varrasso, A., Meanger, J., Voelker, D. R., Anders, E. M., & Mills, J. (1999). Surfactant protein A binds to the fusion glycoprotein of respiratory syncytial virus and neutralizes virion infectivity. Journal of Infectious Diseases, 180(6), 2009–2013. https://doi.org/10.1086/315134

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