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Respiratory Virus Infection: Recent Advances

Review ARTICLE Provisionally accepted The full-text will be published soon. Notify me

Front. Microbiol. | doi: 10.3389/fmicb.2019.00039

Influenza virus neuraminidase structure and functions.

  • 1The University of Melbourne, Australia
  • 2St. Jude Children's Research Hospital, United States

With the constant threat of emergence of a novel influenza virus pandemic, there must be continued evaluation of the molecular mechanisms that contribute to virulence. Although the influenza A virus surface glycoprotein neuraminidase (NA) has been studied mainly in the context of its role in viral release from cells, accumulating evidence suggests it plays an important, multifunctional role in virus infection and fitness. This review investigates the various structural features of NA, linking these with functional outcomes in viral replication. The contribution of evolving NA activity to viral attachment, entry and release of virions from infected cells and to maintenance of functional balance with the viral haemagglutinin is also discussed. Greater insight into the role of this important antiviral drug target is warranted.

Keywords: influenza, Neuraminidase, hemagglutinin, sialic acid, Infection, HA:NA balance, Na

Received: 25 Oct 2018; Accepted: 10 Jan 2019.

Edited by:

Ville Peltola, Turku University Hospital, Finland

Reviewed by:

Takashi Irie, Hiroshima University, Japan
Kirsty R. Short, The University of Queensland, Australia  

Copyright: © 2019 McAuley, Gilbertson, Trifkovic, Brown and McKimm-Breschkin. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

* Correspondence: Dr. Julie McAuley, The University of Melbourne, Melbourne, Australia, jmcauley@unimelb.edu.au