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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Carrier Proteins / metabolism
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Collectins
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Glycoproteins / metabolism
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HN Protein*
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Humans
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Neutralization Tests
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Proteolipids / metabolism*
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Pulmonary Surfactant-Associated Protein A
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Pulmonary Surfactant-Associated Protein D
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Pulmonary Surfactant-Associated Proteins
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Pulmonary Surfactants / metabolism*
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Rabbits
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Respiratory Syncytial Viruses / metabolism*
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Respiratory Syncytial Viruses / physiology
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Tumor Cells, Cultured
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Viral Envelope Proteins
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Viral Proteins / metabolism*
Substances
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Carrier Proteins
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Collectins
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Glycoproteins
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HN Protein
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Proteolipids
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Pulmonary Surfactant-Associated Protein A
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Pulmonary Surfactant-Associated Protein D
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Pulmonary Surfactant-Associated Proteins
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Pulmonary Surfactants
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Viral Envelope Proteins
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Viral Proteins
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attachment protein G