Antibody Epitopes on the Neuraminidase of a Recent H3N2 Influenza Virus (A/Memphis/31/98)

Gulati, Upma; Hwang, Chi-Ching; Venkatramani, Lalitha; Gulati, Shelly; Stray, Stephen J.; Lee, Janis T.; Laver, W.G.; Bochkarev, A.; Zlotnick, Adam; Air, Gillian M.

doi:10.1128/jvi.76.23.12274-12280.2002

Cited by 92 publications

(106 citation statements)

References 43 publications

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“…Mutational studies with monoclonal antibodies identified three regions (A,B,C) in NA N2 that are important for recognition [4,31], of which only the surface residues can be within the epitopes. Regions A and B are usually dominant [31]. Epitope A (residues 383-387, 389-394, 396, 399, 400, 401, 403) presents three point mutations in at residues 385, 399, and 403.…”

Section: Methodsmentioning

confidence: 99%

Epitope analysis for influenza vaccine design

Muñoz

Deem

2005

Vaccine

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Until now, design of the annual influenza vaccine has relied on phylogenetic or whole-sequence comparisons of the viral coat proteins hemagglutinin and neuraminidase, with vaccine effectiveness assumed to correlate monotonically to the vaccine-influenza sequence difference. We use a theory from statistical mechanics to quantify the non-monotonic immune response that results from antigenic drift in the epitopes of the hemagglutinin and neuraminidase proteins. The results explain the ineffectiveness of the 2003-2004 influenza vaccine in the United States and provide an accurate measure by which to optimize the effectiveness of future annual influenza vaccines.

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Section: Methodsmentioning

confidence: 99%

Epitope analysis for influenza vaccine design

Muñoz

Deem

2005

Vaccine

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“…These can be partially mapped by sequence changes in escape mutants selected with monoclonal antibodies. Antibodies can only select escape mutants if they neutralize the parental virus, and for NA this property correlates with the ability of the antibody to inhibit NA activity in an in vitro assay 83,94,95 . The positions of amino acid sequence changes in escape mutants are quite similar in different subtypes of NA, leading to the conclusion that neutralizing anti-NA antibodies bind to epitopes surrounding the enzyme active site Table 1.…”

Section: Na As An Antigenmentioning

confidence: 99%

Influenza neuraminidase

Air

2011

Influenza Resp Viruses

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216

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Influenza neuraminidase is the target of two licensed antivirals that have been very successful, with several more in development. However, neuraminidase has been largely ignored as a vaccine target despite evidence that inclusion of neuraminidase in the subunit vaccine gives increased protection. This article describes current knowledge on the structure, enzyme activity and antigenic significance of neuraminidase.

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“…However, only four escape mutants selected by NC41 were obtained (8). Usually, substitutions were found at one to four positions in escape mutants targeted by one monoclonal antibody (10,12,25).…”

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confidence: 99%

Comparison of Epitope Structures of H3HAs through Protein Modeling of Influenza A Virus Hemagglutinin: Mechanism for Selection of Antigenic Variants in the Presence of a Monoclonal Antibody

Nakajima

Nobusawa

et al. 2007

Microbiology and Immunology

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Starting with nine plaques of influenza A/Kamata/14/91(H3N2) virus, we selected mutants in the presence of monoclonal antibody 203 (mAb203). In total, amino acid substitutions were found at nine positions (77, 80, 131, 135, 141, 142, 143, 144 and 146), which localized in the antigenic site A of the hemagglutinin (HA). The escape mutants differed in the extent to which they had lost binding to mAb203. HA protein with substitutions of some amino acid residues created by site‐directed mutagenesis in the escape mutants retained the ability to bind to mAb203. Changes in the amino acid character affecting charge or hydrophobicity accounted for the binding capacity to the antibody of the HA with most of the substitutions in the escape mutants and binding‐positive mutants. However, the effect of some amino acid substitutions remained unexplained. A three‐dimensional model of the 1991 HA was constructed and used to analyze substituted amino acids in these mutants for the accessible surface hydrophobic and hydrophilic characters. One amino acid substitution in an escape mutant and another amino acid substitution in a binding‐positive mutant seemed to be explained by the changes noted on this model.

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Antibody Epitopes on the Neuraminidase of a Recent H3N2 Influenza Virus (A/Memphis/31/98)

Cited by 92 publications

References 43 publications

Epitope analysis for influenza vaccine design

Epitope analysis for influenza vaccine design

Influenza neuraminidase

Comparison of Epitope Structures of H3HAs through Protein Modeling of Influenza A Virus Hemagglutinin: Mechanism for Selection of Antigenic Variants in the Presence of a Monoclonal Antibody

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