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Jan 29, 2019 · 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.
- Julie L. McAuley, Brad P. Gilbertson, Sanja Trifkovic, Sanja Trifkovic, Lorena E. Brown, Jennifer L....
- 10.3389/fmicb.2019.00039
- 2019
- Front Microbiol. 2019; 10: 39.
Neuraminidase cleaves the sialic acid molecule, thereby freeing the virus to infect other cells in the host organism. Antibodies against neuraminidase that are generated by the host’s immune system following infection bind to a portion of the neuraminidase antigen known as an epitope .
- Kara Rogers
The structure of the influenza virus neuraminidases, the spatial organization of their active site, the mechanism of carbohydrate chains desialylation by neuraminidase, and its role in the influenza virus function at different stages of the viral infectious cycle are considered in this review.
- Y A Shtyrya, L V Mochalova, N V Bovin
- Acta Naturae. 2009 Jul; 1(2): 26-32.
- 2009
- 2009/07
Apr 16, 2019 · Abstract. Influenza A virions possess two surface glycoproteins—the hemagglutinin (HA) and neuraminidase (NA)—which exert opposite functions.
- Ivan Kosik, Jonathan W. Yewdell
- 10.3390/v11040346
- 2019
- Viruses. 2019 Apr; 11(4): 346.
The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. Viral neuraminidase was the first neuraminidase to be identified. It was discovered in 1957 by Alfred Gottschalk at the Walter and Eliza Hall Institute in Melbourne. [1] .
Nov 15, 2021 · Neuraminidase of influenza A and B viruses plays a critical role in the virus life cycle and is an important target of the host immune system. Here, we highlight the current understanding of influenza neuraminidase structure, function, antigenicity, immunogenicity, and immune protective potential.
