Playing hide and seek : how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection

Seasonal influenza A viruses (IAV) originate from pandemic IAV and have undergone changes in antigenic structure, including addition of glycans to the hemagglutinin (HA) glycoprotein. The viral HA is the major target recognized by neutralizing antibodies and glycans have been proposed to shield anti...

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Main Authors: Tate, Michelle D., Job, Emma R., Deng, Yi-Mo, Gunalan, Vithiagaran, Maurer-Stroh, Sebastian, Reading, Patrick C.
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2014
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Online Access:https://hdl.handle.net/10356/104013
http://hdl.handle.net/10220/19496
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-1040132023-02-28T16:56:18Z Playing hide and seek : how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection Tate, Michelle D. Job, Emma R. Deng, Yi-Mo Gunalan, Vithiagaran Maurer-Stroh, Sebastian Reading, Patrick C. School of Biological Sciences DRNTU::Science::Biological sciences Seasonal influenza A viruses (IAV) originate from pandemic IAV and have undergone changes in antigenic structure, including addition of glycans to the hemagglutinin (HA) glycoprotein. The viral HA is the major target recognized by neutralizing antibodies and glycans have been proposed to shield antigenic sites on HA, thereby promoting virus survival in the face of widespread vaccination and/or infection. However, addition of glycans can also interfere with the receptor binding properties of HA and this must be compensated for by additional mutations, creating a fitness barrier to accumulation of glycosylation sites. In addition, glycans on HA are also recognized by phylogenetically ancient lectins of the innate immune system and the benefit provided by evasion of humoral immunity is balanced by attenuation of infection. Therefore, a fine balance must exist regarding the optimal pattern of HA glycosylation to offset competing pressures associated with recognition by innate defenses, evasion of humoral immunity and maintenance of virus fitness. In this review, we examine HA glycosylation patterns of IAV associated with pandemic and seasonal influenza and discuss recent advancements in our understanding of interactions between IAV glycans and components of innate and adaptive immunity. Published version 2014-06-02T03:59:33Z 2019-12-06T21:24:33Z 2014-06-02T03:59:33Z 2019-12-06T21:24:33Z 2014 2014 Journal Article Tate, M., Job, E., Deng, Y.-M., Gunalan, V., Maurer-Stroh, S., & Reading, P. (2014). Playing Hide and Seek: How Glycosylation of the Influenza Virus Hemagglutinin Can Modulate the Immune Response to Infection. Viruses, 6(3), 1294-1316. 1999-4915 https://hdl.handle.net/10356/104013 http://hdl.handle.net/10220/19496 10.3390/v6031294 24638204 en Viruses © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science::Biological sciences
spellingShingle DRNTU::Science::Biological sciences
Tate, Michelle D.
Job, Emma R.
Deng, Yi-Mo
Gunalan, Vithiagaran
Maurer-Stroh, Sebastian
Reading, Patrick C.
Playing hide and seek : how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection
description Seasonal influenza A viruses (IAV) originate from pandemic IAV and have undergone changes in antigenic structure, including addition of glycans to the hemagglutinin (HA) glycoprotein. The viral HA is the major target recognized by neutralizing antibodies and glycans have been proposed to shield antigenic sites on HA, thereby promoting virus survival in the face of widespread vaccination and/or infection. However, addition of glycans can also interfere with the receptor binding properties of HA and this must be compensated for by additional mutations, creating a fitness barrier to accumulation of glycosylation sites. In addition, glycans on HA are also recognized by phylogenetically ancient lectins of the innate immune system and the benefit provided by evasion of humoral immunity is balanced by attenuation of infection. Therefore, a fine balance must exist regarding the optimal pattern of HA glycosylation to offset competing pressures associated with recognition by innate defenses, evasion of humoral immunity and maintenance of virus fitness. In this review, we examine HA glycosylation patterns of IAV associated with pandemic and seasonal influenza and discuss recent advancements in our understanding of interactions between IAV glycans and components of innate and adaptive immunity.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Tate, Michelle D.
Job, Emma R.
Deng, Yi-Mo
Gunalan, Vithiagaran
Maurer-Stroh, Sebastian
Reading, Patrick C.
format Article
author Tate, Michelle D.
Job, Emma R.
Deng, Yi-Mo
Gunalan, Vithiagaran
Maurer-Stroh, Sebastian
Reading, Patrick C.
author_sort Tate, Michelle D.
title Playing hide and seek : how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection
title_short Playing hide and seek : how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection
title_full Playing hide and seek : how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection
title_fullStr Playing hide and seek : how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection
title_full_unstemmed Playing hide and seek : how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection
title_sort playing hide and seek : how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection
publishDate 2014
url https://hdl.handle.net/10356/104013
http://hdl.handle.net/10220/19496
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