Influenza Virus Neuraminidase Structure and Functions.
Julie L. McAuley,Brad Gilbertson,Sanja Trifkovic,Sanja Trifkovic,Lorena E. Brown,Jennifer L. McKimm-Breschkin +5 more
TL;DR: The various structural features of NA are investigated, linking these with functional outcomes in viral replication and the contribution of evolving NA activity to viral attachment, entry and release of virions from infected cells, and maintenance of functional balance with the viral hemagglutinin are discussed.
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Abstract: 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 maintenance of functional balance with the viral hemagglutinin are also discussed. Greater insight into the role of this important antiviral drug target is warranted.
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References
Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases
Joseph N. Varghese,Peter M. Colman,A. Van Donkelaar,Tony J. Blick,Anjali Sahasrabudhe,J.L. McKimm-Breschkin +5 more
TL;DR: The x-ray structure of a complex of sialic acid (Neu5Ac) with neuraminidase N9 subtype from A/tern/Australia/G70C/75 influenza virus at 4 degrees C has revealed the location of a second Neu5 Ac binding site on the surface of the enzyme, indicating that it has some as-yet-unknown biological function in birds.
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Airway mucus: its components and function
Erik P. Lillehoj,K. Chul Kim +1 more
TL;DR: The fact that mucins are tightly associated with various macromolecules present in ASL seems to suggest that the defensive role of ASL is determined not only by these individual components but rather by a combination of these components.
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Human H3N2 Influenza Viruses Isolated from 1968 To 2012 Show Varying Preference for Receptor Substructures with No Apparent Consequences for Disease or Spread.
Shelly Gulati,David F. Smith,Richard D. Cummings,Robert B. Couch,Sara B. Griesemer,Kirsten St. George,Robert G. Webster,Gillian M. Air +7 more
TL;DR: It is concluded that the year-to-year variation in receptor binding specificity is a consequence of amino acid sequence changes driven by antigenic drift, and that viruses with quite different binding specificity and avidity are equally fit to infect and transmit in the human population.
A Beneficiary Role for Neuraminidase in Influenza Virus Penetration through the Respiratory Mucus
Xiaoyun Yang,Lennert Steukers,Katrien Forier,Ranhua Xiong,Kevin Braeckmans,Kristien Van Reeth,Hans Nauwynck +6 more
TL;DR: Findings clearly show that the neuraminidase helps SIV move through the mucus, which is important for the virus to reach and infect epithelial cells and eventually become shed into the lumen of the respiratory tract.
Site-directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism.
TL;DR: The properties of the mutant enzymes suggest a possible mechanism of neuraminidase action, and 12 of the 14 mutant proteins were correctly folded and were transported to the cell surface in a manner identical with that of the wild type.
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