Neuraminidase role

The role of the viral neuraminidase, conversely, seems to be to facilitate the release of progeny virions from infected cells by cleaving sialic acid... 

An overview of the role of the virus-associated glycoprotein sialidase (neuraminidase) and some of the most recent developments towards the discovery of anti-influenza drugs based on the inhibition of influenza virus sialidase is provided in this chapter. 

The influenza virus possesses a neuraminidase that plays a key role in elution of newly synthesized progeny from infected cells. If this process is inhibited, spread of the vims is markedly diminished. Inhibitors of this enzyme are now available for use in treating patients with influenza. 

Refer to Exhibits 3.7 and 4.2 for an explanation of the roles of hemagglutinin and neuraminidase, followed by the nomenclature for classifying influenza virus and the procedure that the FDA and WFIO recommend for the preparation of multivalent vaccines. 

Liu C, Eichelberger MC, Compans RW, Air GM. Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J Virol 1995 69 1099-1106. 

Studies on the activity of rabbit sperm acrosomal enzymes have indicated that gossypol at 12-76 pM could significantly inactivate azocoll proteinase, acrosin, neuraminidase, and arylsulfatase. Hyaluronidase, p-glucuronidase, and acid phosphatase were also inhibited at a higher concentration of gossypol (380 pM) (Yuan et al., 1995). Since acrosomal enzymes play important roles in the fertilization process, the inhibition of... 

Sialidases are enzymes that catalyze the removal of terminal sialic acids from sialosides (56, 57). Human sialidases play pivotal roles in sialic acid metabolism (58). They relate to a number of disease states such as sialidosis (59-62) and cancer (63-65). Bacterial and viral play significant roles in the pathogenesis and pathology of bacterial and viral infections (66, 67). Viral sialidases such as neuraminidases of influenza virus catalyze the removal of sialic acid from the surface of infected host cells to release the newly formed progeny virus (68). 

Gaffney (Gl) suggested that N-acetylneuraminic acid plays an important role in maintaining the stability of the multicomponent system of the human enzyme. Such an hypothesis could be readily verified with the subunit butyrylcholinesterase found in pooled rabbit sera. LaMotta et al. (L12) found that the relative molecular masses of neuraminidase-treated human isoenzymes are essentially the same as those of the untreated isoenzymes (see Table 16). This implies that the sialic acid residues which have been split off do not play a significant role in determining the state of molecular aggregation of human isoenzymes. 

T. cruzi-infected mice correlates with the degree of parasitemia. Further studies revealed that neuraminidase also removes sialic acid from the surfaee of myoeardial and endothelial cells, indicating that this molecule may play a critical role in the pathology of Chagas disease (15). 

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