Influenza A surface glycosylation and vaccine design

We have shown that glycosylation of influenza A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus survival. However, it is not known whether the glycosylation of HA and the other two major IAV surface glycoproteins, neuraminidase (NA) and M2 ion channel...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 114; no. 2; pp. 280 - 285
Main Authors Wu, Chung-Yi, Lin, Chih-Wei, Tsai, Tsung-I, Lee, Chang-Chun David, Chuang, Hong-Yang, Chen, Jhih-Bin, Tsai, Ming-Hung, Chen, Bo-Rui, Lo, Pei-Wen, Liu, Chiu-Ping, Shivatare, Vidya S., Wong, Chi-Huey
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 10.01.2017
Subjects
Biological Sciences
Glycoproteins
Glycosylation
Immune response
Influenza
Influenza A virus
Orthomyxoviridae
Physical Sciences
T cell receptors
Vaccines
Viruses
glycosylation
vaccine design
influenza A virus
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Abstract We have shown that glycosylation of influenza A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus survival. However, it is not known whether the glycosylation of HA and the other two major IAV surface glycoproteins, neuraminidase (NA) and M2 ion channel, is essential for the replication of IAV. Here, we show that glycosylation of HA at N-142 modulates virus infectivity and host immune response. Glycosylation of NA in the stalk region affects its structure, activity, and specificity, thereby modulating virus release and virulence, and glycosylation at the catalytic domain affects its thermostability; however, glycosylation of M2 had no effect on its function. In addition, using IAV without the stalk and catalytic domains of NA as a live attenuated vaccine was shown to confer a strong IAV-specific CD8⁺ T-cell response and a strong cross-strain as well as cross-subtype protection against various virus strains.
AbstractList Influenza A virus (IAV) is a major threat to global public health, and so understanding the biology of IAV is essential to develop antiflu vaccines and therapeutics. Here, we show the links between viral surface glycosylation and IAV function. The glycosylation of HA modulates virus infectivity, and host immune response; the glycosylation of NA affects its structure, activity, specificity, and thermostability to regulate virus release and virulence. In addition, using live attenuated IAV without the stalk and catalytic domains of NA as vaccine can strongly induce IAV-specific CD8 + T-cell responses to various virus strains. Therefore, our findings have clarified the role of glycosylation in IAV and provided a new direction for the development of universal flu vaccines. We have shown that glycosylation of influenza A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus survival. However, it is not known whether the glycosylation of HA and the other two major IAV surface glycoproteins, neuraminidase (NA) and M2 ion channel, is essential for the replication of IAV. Here, we show that glycosylation of HA at N-142 modulates virus infectivity and host immune response. Glycosylation of NA in the stalk region affects its structure, activity, and specificity, thereby modulating virus release and virulence, and glycosylation at the catalytic domain affects its thermostability; however, glycosylation of M2 had no effect on its function. In addition, using IAV without the stalk and catalytic domains of NA as a live attenuated vaccine was shown to confer a strong IAV-specific CD8 + T-cell response and a strong cross-strain as well as cross-subtype protection against various virus strains.
We have shown that glycosylation of influenza A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus survival. However, it is not known whether the glycosylation of HA and the other two major IAV surface glycoproteins, neuraminidase (NA) and M2 ion channel, is essential for the replication of IAV. Here, we show that glycosylation of HA at N-142 modulates virus infectivity and host immune response. Glycosylation of NA in the stalk region affects its structure, activity, and specificity, thereby modulating virus release and virulence, and glycosylation at the catalytic domain affects its thermostability; however, glycosylation of M2 had no effect on its function. In addition, using IAV without the stalk and catalytic domains of NA as a live attenuated vaccine was shown to confer a strong IAV-specific CD8 T-cell response and a strong cross-strain as well as cross-subtype protection against various virus strains.
We have shown that glycosylation of influenza A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus survival. However, it is not known whether the glycosylation of HA and the other two major IAV surface glycoproteins, neuraminidase (NA) and M2 ion channel, is essential for the replication of IAV. Here, we show that glycosylation of HA at N-142 modulates virus infectivity and host immune response. Glycosylation of NA in the stalk region affects its structure, activity, and specificity, thereby modulating virus release and virulence, and glycosylation at the catalytic domain affects its thermostability; however, glycosylation of M2 had no effect on its function. In addition, using IAV without the stalk and catalytic domains of NA as a live attenuated vaccine was shown to confer a strong IAV-specific CD8⁺ T-cell response and a strong cross-strain as well as cross-subtype protection against various virus strains.
We have shown that glycosylation of influenza A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus survival. However, it is not known whether the glycosylation of HA and the other two major IAV surface glycoproteins, neuraminidase (NA) and M2 ion channel, is essential for the replication of IAV. Here, we show that glycosylation of HA at N-142 modulates virus infectivity and host immune response. Glycosylation of NA in the stalk region affects its structure, activity, and specificity, thereby modulating virus release and virulence, and glycosylation at the catalytic domain affects its thermostability; however, glycosylation of M2 had no effect on its function. In addition, using IAV without the stalk and catalytic domains of NA as a live attenuated vaccine was shown to confer a strong IAV-specific CD8+ T-cell response and a strong cross-strain as well as cross-subtype protection against various virus strains.We have shown that glycosylation of influenza A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus survival. However, it is not known whether the glycosylation of HA and the other two major IAV surface glycoproteins, neuraminidase (NA) and M2 ion channel, is essential for the replication of IAV. Here, we show that glycosylation of HA at N-142 modulates virus infectivity and host immune response. Glycosylation of NA in the stalk region affects its structure, activity, and specificity, thereby modulating virus release and virulence, and glycosylation at the catalytic domain affects its thermostability; however, glycosylation of M2 had no effect on its function. In addition, using IAV without the stalk and catalytic domains of NA as a live attenuated vaccine was shown to confer a strong IAV-specific CD8+ T-cell response and a strong cross-strain as well as cross-subtype protection against various virus strains.
We have shown that glycosylation of influenza A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus survival. However, it is not known whether the glycosylation of HA and the other two major IAV surface glycoproteins, neuraminidase (NA) and M2 ion channel, is essential for the replication of IAV. Here, we show that glycosylation of HA at N-142 modulates virus infectivity and host immune response. Glycosylation of NA in the stalk region affects its structure, activity, and specificity, thereby modulating virus release and virulence, and glycosylation at the catalytic domain affects its thermostability; however, glycosylation of M2 had no effect on its function. In addition, using IAV without the stalk and catalytic domains of NA as a live attenuated vaccine was shown to confer a strong IAV-specific CD8+ T-cell response and a strong cross-strain as well as cross-subtype protection against various virus strains.
Author Lin, Chih-Wei
Chen, Jhih-Bin
Chuang, Hong-Yang
Shivatare, Vidya S.
Tsai, Tsung-I
Liu, Chiu-Ping
Lee, Chang-Chun David
Wong, Chi-Huey
Wu, Chung-Yi
Chen, Bo-Rui
Tsai, Ming-Hung
Lo, Pei-Wen
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  fullname: Lin, Chih-Wei
  organization: Genomics Research Center, Academia Sinica, Taipei 115, Taiwan
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  organization: Genomics Research Center, Academia Sinica, Taipei 115, Taiwan
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  organization: Genomics Research Center, Academia Sinica, Taipei 115, Taiwan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28028222$$D View this record in MEDLINE/PubMed
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influenza A virus
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Author contributions: C.-Y.W. and C.-H.W. designed research; C.-Y.W., C.-W.L., T.-I.T., C.-C.D.L., H.-Y.C., J.-B.C., M.-H.T., B.-R.C., P.-W.L., and C.-P.L. performed research; C.-Y.W. and C.-H.W. analyzed data; and C.-Y.W., V.S.S., and C.-H.W. wrote the paper.
Reviewers: N.L.B.P., Indiana University; and M.v.I., Griffith University.
Contributed by Chi-Huey Wong, November 16, 2016 (sent for review July 12, 2016; reviewed by Nicola L. B. Pohl and Mark von Itzstein)
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Snippet We have shown that glycosylation of influenza A virus (IAV) hemagglutinin (HA), especially at position N-27, is crucial for HA folding and virus survival....
Influenza A virus (IAV) is a major threat to global public health, and so understanding the biology of IAV is essential to develop antiflu vaccines and...
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SubjectTerms Biological Sciences
Glycoproteins
Glycosylation
Immune response
Influenza
Influenza A virus
Orthomyxoviridae
Physical Sciences
T cell receptors
Vaccines
Viruses
Title Influenza A surface glycosylation and vaccine design
URI https://www.jstor.org/stable/26478705
https://www.ncbi.nlm.nih.gov/pubmed/28028222
https://www.proquest.com/docview/1858600417
https://www.proquest.com/docview/1853742174
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https://pubmed.ncbi.nlm.nih.gov/PMC5240703
Volume 114
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