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

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

Research output: Contribution to journalArticle

87 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2009-2013
Number of pages5
JournalJournal of Infectious Diseases
Volume180
Issue number6
DOIs
Publication statusPublished - 1999
Externally publishedYes

Fingerprint

Pulmonary Surfactant-Associated Protein A
Respiratory Syncytial Viruses
Collectins
Virion
Glycoproteins
Pulmonary Surfactant-Associated Protein D
Mannose-Binding Lectin
Pulmonary Surfactant-Associated Proteins
Calcium
Respiratory Syncytial Virus Infections
Membrane Glycoproteins
Edetic Acid
Blood Proteins

Cite this

Ghildyal, R ; Hartley, C ; Varrasso, A ; Meanger, J ; Voelker, D R ; Anders, E M ; Mills, J. / Surfactant protein A binds to the fusion glycoprotein of respiratory syncytial virus and neutralizes virion infectivity. In: Journal of Infectious Diseases. 1999 ; Vol. 180, No. 6. pp. 2009-2013.
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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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Surfactant protein A binds to the fusion glycoprotein of respiratory syncytial virus and neutralizes virion infectivity. / Ghildyal, R; Hartley, C; Varrasso, A; Meanger, J; Voelker, D R; Anders, E M; Mills, J.

In: Journal of Infectious Diseases, Vol. 180, No. 6, 1999, p. 2009-2013.

Research output: Contribution to journalArticle

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T1 - Surfactant protein A binds to the fusion glycoprotein of respiratory syncytial virus and neutralizes virion infectivity

AU - Ghildyal, R

AU - Hartley, C

AU - Varrasso, A

AU - Meanger, J

AU - Voelker, D R

AU - Anders, E M

AU - Mills, J

PY - 1999

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N2 - 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.

AB - 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.

KW - Animals

KW - Carrier Proteins

KW - Collectins

KW - Glycoproteins

KW - HN Protein

KW - Humans

KW - Neutralization Tests

KW - Proteolipids

KW - Pulmonary Surfactant-Associated Protein A

KW - Pulmonary Surfactant-Associated Protein D

KW - Pulmonary Surfactant-Associated Proteins

KW - Pulmonary Surfactants

KW - Rabbits

KW - Respiratory Syncytial Viruses

KW - Tumor Cells, Cultured

KW - Viral Envelope Proteins

KW - Viral Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

KW - Research Support, U.S. Gov't, P.H.S.

U2 - 10.1086/315134

DO - 10.1086/315134

M3 - Article

VL - 180

SP - 2009

EP - 2013

JO - Journal of Infectious Diseases

JF - Journal of Infectious Diseases

SN - 0022-1899

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