The impact of key amino acid substitutions in the hemagglutinin of influenza A (H3N2) viruses on vaccine production and antibody response (Q39713700)

14 September 2017

title

The impact of key amino acid substitutions in the hemagglutinin of influenza A (H3N2) viruses on vaccine production and antibody response (English)

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14 September 2017

3

Hong Jin

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14 September 2017

Zhongying Chen

1

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14 September 2017

Helen Zhou

series ordinal

2

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14 September 2017

language of work or name

English

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publication date

1 May 2010

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14 September 2017

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14 September 2017

volume

28

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14 September 2017

issue

24

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14 September 2017

page(s)

4079-4085

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https://api.crossref.org/works/10.1016%2FJ.VACCINE.2010.03.078

14 September 2017

1 reference

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Influenza vaccine strain selection and recent studies on the global migration of seasonal influenza viruses

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The global circulation of seasonal influenza A (H3N2) viruses

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Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

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Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid

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Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation

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Structural basis of immune recognition of influenza virus hemagglutinin

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Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution

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Hemagglutinin sequence clusters and the antigenic evolution of influenza A virus

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Simultaneous amino acid substitutions at antigenic sites drive influenza A hemagglutinin evolution

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Mapping the antigenic and genetic evolution of influenza virus

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Positive selection on the H3 hemagglutinin gene of human influenza virus A.

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Two residues in the hemagglutinin of A/Fujian/411/02-like influenza viruses are responsible for antigenic drift from A/Panama/2007/99

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Codominant mixtures of viruses in reference strains of influenza virus due to host cell variation

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Host cell-mediated variation in H3N2 influenza viruses

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Influence of host cell-mediated variation on the international surveillance of influenza A (H3N2) viruses

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Multiple amino acid residues confer temperature sensitivity to human influenza virus vaccine strains (FluMist) derived from cold-adapted A/Ann Arbor/6/60.

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Single amino acid substitutions in the hemagglutinin of influenza A/Singapore/21/04 (H3N2) increase virus growth in embryonated chicken eggs

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Improvement of influenza A/Fujian/411/02 (H3N2) virus growth in embryonated chicken eggs by balancing the hemagglutinin and neuraminidase activities, using reverse genetics

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Molecular changes associated with adaptation of human influenza A virus in embryonated chicken eggs

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Hemagglutinin receptor binding avidity drives influenza A virus antigenic drift

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Amino-acid change on the antigenic region B1 of H3 haemagglutinin may be a trigger for the emergence of drift strain of influenza A virus

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Molecular evolution of influenza A (H3N2) viruses circulated in Fujian Province, China during the 1996-2004 period

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Molecular and phylogenetic analysis of haemagglutinin and neuraminidase sequences from recent human influenza type A (H3N2) viral isolates in Southern Greece

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Studies of the binding properties of influenza hemagglutinin receptor-site mutants

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Receptor-binding properties of modern human influenza viruses primarily isolated in Vero and MDCK cells and chicken embryonated eggs

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Influenza H1N1 A/Solomon Island/3/06 virus receptor binding specificity correlates with virus pathogenicity, antigenicity, and immunogenicity in ferrets

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Change in receptor-binding specificity of recent human influenza A viruses (H3N2): a single amino acid change in hemagglutinin altered its recognition of sialyloligosaccharides

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Low growth ability of recent influenza clinical isolates in MDCK cells is due to their low receptor binding affinities

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Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates

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1 reference

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Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity

7 January 2021

1 reference

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Selection of a single amino acid substitution in the hemagglutinin molecule by chicken eggs can render influenza A virus (H3) candidate vaccine ineffective

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.VACCINE.2010.03.078

inferred from DOI database lookup

7 January 2021

based on heuristic

The role of influenza A virus hemagglutinin residues 226 and 228 in receptor specificity and host range restriction

1 reference

https://api.crossref.org/works/10.1016%2FJ.VACCINE.2010.03.078

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/J.VACCINE.2010.03.078

1 reference

14 September 2017

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