NYMC Faculty Publications

A Monoclonal Antibody Targeting a Highly Conserved Epitope in Influenza B Neuraminidase Provides Protection Against Drug Resistant Strains

Author Type(s)

Faculty

Journal Title

Biochemical and Biophysical Research Communications

First Page

226

Last Page

229

Document Type

Article

Publication Date

11-8-2013

Keywords

Amino Acid Sequence, Animals, Antibodies, Monoclonal, Antibodies, Viral, Conserved Sequence, Dogs, Drug Resistance, Viral, Epitopes, Humans, Influenza B virus, Influenza, Human, Madin Darby Canine Kidney Cells, Models, Molecular, Molecular Sequence Data, Mutation, Neuraminidase

Disciplines

Medicine and Health Sciences

Abstract

All influenza viral neuraminidases (NA) of both type A and B viruses have only one universally conserved sequence located between amino acids 222-230. A monoclonal antibody against this region has been previously reported to provide broad inhibition against all nine subtypes of influenza A NA; yet its inhibitory effect against influenza B viral NA remained unknown. Here, we report that the monoclonal antibody provides a broad inhibition against various strains of influenza B viruses of both Victoria and Yamagata genetic lineage. Moreover, the growth and NA enzymatic activity of two drug resistant influenza B strains (E117D and D197E) are also inhibited by the antibody even though these two mutations are conformationally proximal to the universal epitope. Collectively, these data suggest that this unique, highly-conserved linear sequence in viral NA is exposed sufficiently to allow access by inhibitory antibody during the course of infection; it could represent a potential target for antiviral agents and vaccine-induced immune responses against diverse strains of type B influenza virus.

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