Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses.

Members of the pentraxin family, including PTX3 and serum amyloid P component (SAP), have been reported to play a role in innate host defence against a range of microbial pathogens, yet little is known regarding their antiviral activities. In this study, we demonstrate that human SAP binds to human...

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Autores principales:	Emma R Job, Barbara Bottazzi, Brad Gilbertson, Kathryn M Edenborough, Lorena E Brown, Alberto Mantovani, Andrew G Brooks, Patrick C Reading
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7f07531ab19844848008cdb5ee48adb6
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spelling	oai:doaj.org-article:7f07531ab19844848008cdb5ee48adb62021-11-18T07:51:47ZSerum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses.1932-620310.1371/journal.pone.0059623https://doaj.org/article/7f07531ab19844848008cdb5ee48adb62013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23544079/?tool=EBIhttps://doaj.org/toc/1932-6203Members of the pentraxin family, including PTX3 and serum amyloid P component (SAP), have been reported to play a role in innate host defence against a range of microbial pathogens, yet little is known regarding their antiviral activities. In this study, we demonstrate that human SAP binds to human influenza A virus (IAV) strains and mediates a range of antiviral activities, including inhibition of IAV-induced hemagglutination (HA), neutralization of virus infectivity and inhibition of the enzymatic activity of the viral neuraminidase (NA). Characterization of the anti-IAV activity of SAP after periodate or bacterial sialidase treatment demonstrated that α(2,6)-linked sialic acid residues on the glycosidic moiety of SAP are critical for recognition by the HA of susceptible IAV strains. Other proteins of the innate immune system, namely human surfactant protein A and porcine surfactant protein D, have been reported to express sialylated glycans which facilitate inhibition of particular IAV strains, yet the specific viral determinants for recognition of these inhibitors have not been defined. Herein, we have selected virus mutants in the presence of human SAP and identified specific residues in the receptor-binding pocket of the viral HA which are critical for recognition and therefore susceptibility to the antiviral activities of SAP. Given the widespread expression of α(2,6)-linked sialic acid in the human respiratory tract, we propose that SAP may act as an effective receptor mimic to limit IAV infection of airway epithelial cells.Emma R JobBarbara BottazziBrad GilbertsonKathryn M EdenboroughLorena E BrownAlberto MantovaniAndrew G BrooksPatrick C ReadingPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 3, p e59623 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Emma R Job Barbara Bottazzi Brad Gilbertson Kathryn M Edenborough Lorena E Brown Alberto Mantovani Andrew G Brooks Patrick C Reading Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses.
description	Members of the pentraxin family, including PTX3 and serum amyloid P component (SAP), have been reported to play a role in innate host defence against a range of microbial pathogens, yet little is known regarding their antiviral activities. In this study, we demonstrate that human SAP binds to human influenza A virus (IAV) strains and mediates a range of antiviral activities, including inhibition of IAV-induced hemagglutination (HA), neutralization of virus infectivity and inhibition of the enzymatic activity of the viral neuraminidase (NA). Characterization of the anti-IAV activity of SAP after periodate or bacterial sialidase treatment demonstrated that α(2,6)-linked sialic acid residues on the glycosidic moiety of SAP are critical for recognition by the HA of susceptible IAV strains. Other proteins of the innate immune system, namely human surfactant protein A and porcine surfactant protein D, have been reported to express sialylated glycans which facilitate inhibition of particular IAV strains, yet the specific viral determinants for recognition of these inhibitors have not been defined. Herein, we have selected virus mutants in the presence of human SAP and identified specific residues in the receptor-binding pocket of the viral HA which are critical for recognition and therefore susceptibility to the antiviral activities of SAP. Given the widespread expression of α(2,6)-linked sialic acid in the human respiratory tract, we propose that SAP may act as an effective receptor mimic to limit IAV infection of airway epithelial cells.
format	article
author	Emma R Job Barbara Bottazzi Brad Gilbertson Kathryn M Edenborough Lorena E Brown Alberto Mantovani Andrew G Brooks Patrick C Reading
author_facet	Emma R Job Barbara Bottazzi Brad Gilbertson Kathryn M Edenborough Lorena E Brown Alberto Mantovani Andrew G Brooks Patrick C Reading
author_sort	Emma R Job
title	Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses.
title_short	Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses.
title_full	Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses.
title_fullStr	Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses.
title_full_unstemmed	Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses.
title_sort	serum amyloid p is a sialylated glycoprotein inhibitor of influenza a viruses.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/7f07531ab19844848008cdb5ee48adb6
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Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses.

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