Improvement of Influenza A/Fujian/411/02 (H3N2) Virus Growth in Embryonated Chicken Eggs by Balancing the Hemagglutinin and Neuraminidase Activities, Using Reverse Genetics

Lü, Bin; Zhou, Helen; Ye, Dan; Kemble, George; Jin, Hong

doi:10.1128/jvi.79.11.6763-6771.2005

Cited by 111 publications

(117 citation statements)

References 51 publications

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“…The functional balance between HA and NA is important for influenza virus infection, transmission, and host adaptation (24)(25)(26)(27). The interdependence of NA stalk length and HA glycosylation near the receptor binding site has been illustrated (28).…”

Section: Fig 3 In Vitro Phenotype Of Wt and Mutant H9n2 Influenza Virmentioning

confidence: 99%

Amino Acid 316 of Hemagglutinin and the Neuraminidase Stalk Length Influence Virulence of H9N2 Influenza Virus in Chickens and Mice

Sun

Tan

Wei

et al. 2013

J Virol

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e H9N2 influenza viruses with an A316S substitution in hemagglutinin (HA) and a shorter neuraminidase (NA) stalk have become predominant in China. The A316S was shown to increase HA cleavage efficiency when combined with short stalk NA, and the short stalk NA improved NA enzyme activity and release of virus from erythrocytes. Single mutations or combinations of these mutations strengthened the virulence of H9N2 virus in chickens and mice.

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Section: Fig 3 In Vitro Phenotype Of Wt and Mutant H9n2 Influenza Virmentioning

confidence: 99%

Amino Acid 316 of Hemagglutinin and the Neuraminidase Stalk Length Influence Virulence of H9N2 Influenza Virus in Chickens and Mice

Sun

Tan

Wei

et al. 2013

J Virol

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“…Secondly, some virus strains, especially the recent H3N2 strains, do not grow well in ECE, and others such as the highly pathogenic avian influenza strains, viz., H5N1, could be lethal to embryos, resulting in low titres. [35][36][37] Indeed, this is one of the reasons why seasonal influenza vaccine strains are generated through reassortment with a high yielding strain such as A/PR/8/34. Third, occasional breakdown in sterility during downstream processing could lead to rejection of large volume of vaccine bulk, leading to a need to revisit the long process of planning and execution, or to the lack of availability of vaccine when needed.…”

Section: Introductionmentioning

confidence: 99%

Cell culture-based influenza vaccines: A necessary and indispensable investment for the future

Hegde

2015

Human Vaccines & Immunotherapeutics

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“…In contrast, both the reassortant viruses bearing either the wild-type or DK134 mutant HA of A/Hebei/52/ 94 and A/Beijing/262/95 NA were able to be rescued although at significantly lower titres (256 and 64, respectively). While the role of residue 13 of the NA glycoprotein in the replication of these recombinant viruses is unclear, the functional interaction between the activities of the HA and NA glycoproteins of influenza is well documented (Baigent & McCauley, 2001;Baum & Paulson, 1991;Kaverin et al, 2000;Lu et al, 2005;Wagner et al, 2000).…”

mentioning

confidence: 99%

Antigenic drift in the evolution of H1N1 influenza A viruses resulting from deletion of a single amino acid in the haemagglutinin gene

McDonald

Smith

Cox

2007

Journal of General Virology

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Two genetically distinct lineages of H1N1 influenza A viruses, circulated worldwide before 1994, were antigenically indistinguishable. In 1994, viruses emerged in China, including A/Beijing/262/ 95, with profound antigenic differences from the contemporary circulating H1N1 strains. Haemagglutinin sequence comparisons of either a predecessor virus, A/Hebei/52/94, or one representative of the cocirculating A/Bayern/7/95-like clade, A/Shenzhen/227/95, revealed a deletion of K at position 134 (H3 numbering) in the antigenic variants. The K134 deletion conferred a selective advantage to the Chinese deletion lineage, such that it eventually gave rise to currently circulating H1 viruses. Using reverse genetics to generate viruses with either an insertion or deletion of aa 134, we have confirmed that the K134 deletion, rather than a constellation of sublineage specific amino acid changes, was sufficient for the antigenic difference observed in the Chinese deletion lineage, and reinsertion of K134 revealed the requirement of a compatible neuraminidase surface glycoprotein for viral growth.Approximately 20 % of the world's population is infected by influenza A each year, resulting in significant mortality and morbidity (Stohr, 2002). The high incidence of influenza cases is attributable to the ability of the influenza virus to escape immunity induced by prior infection or vaccination. This escape is potentiated by the accumulation of mutations in the surface glycoproteins haemagglutinin (HA), and to a lesser extent neuraminidase (NA), which confer antigenic change to the virus. This phenomenon, known as antigenic drift, necessitates annual vaccine updates to confer protection against the currently circulating strains.Mutations in the HA molecule are considered to contribute almost entirely to the antigenic drift observed among influenza A viruses (Wilson & Cox, 1990). Those sites at the distal tip of the H1 HA molecule and on the side of the globular head near the receptor-binding pocket appear to be the main targets of the human immune response (Cox & Brokstad, 1999;Raymond et al., 1986;Sato et al., 2004). Influenza A viruses bind to sialic acids on the surface of target cells via a depression in the distal surface of the globular head of the HA molecule (Weis et al., 1988;Wilson et al., 1981). Several residues within this depression are highly conserved across the HA subtypes, including residues 98, 134, 138, 153 and 183 (H3 numbering) (Nobusawa et al., 1991). Amino acid substitutions within the receptor-binding pocket or the 'second shell' residues, including 190, 225 and 158, may alter the specificity toward certain types of galactosidic linkages, namely a2-6Gal or a2-3Gal linkages (Aytay & Schulze, 1991; Matrosovich et al., 2000). Because of its location on the HA threedimensional structure, mutations in the receptor-binding pocket or second shell residues can alter the antigenicity of a virus in addition to, or instead of, modifying receptor specificity or affinity (Daniels et al., 1984).The HA1 domains of the HA g...

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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

Cited by 111 publications

References 51 publications

Amino Acid 316 of Hemagglutinin and the Neuraminidase Stalk Length Influence Virulence of H9N2 Influenza Virus in Chickens and Mice

Amino Acid 316 of Hemagglutinin and the Neuraminidase Stalk Length Influence Virulence of H9N2 Influenza Virus in Chickens and Mice

Cell culture-based influenza vaccines: A necessary and indispensable investment for the future

Antigenic drift in the evolution of H1N1 influenza A viruses resulting from deletion of a single amino acid in the haemagglutinin gene

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