Surfactant Protein A Binds to the Fusion Glycoprotein of Respiratory Syncytial Virus and Neutralizes Virion Infectivity | Zendy

Reena Ghildyal | Zendy; Carol A. Hartley | Zendy; Annalisa Varrasso | Zendy; Jayesh Meanger | Zendy; Dennis R. Voelker | Zendy; E M Anders | Zendy; John Mills | Zendy

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Surfactant Protein A Binds to the Fusion Glycoprotein of Respiratory Syncytial Virus and Neutralizes Virion Infectivity

Author(s) -

Reena Ghildyal,

Carol A. Hartley,

Annalisa Varrasso,

Jayesh Meanger,

Dennis R. Voelker,

E M Anders,

John Mills

Publication year - 1999

Publication title -

the journal of infectious diseases

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.69

H-Index - 252

eISSN - 1537-6613

pISSN - 0022-1899

DOI - 10.1086/315134

Subject(s) - collectin , glycoprotein , surfactant protein d , infectivity , virus , biology , virology , membrane glycoproteins , innate immune system , biochemistry , immune system , immunology

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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