ISSN: 0973-7510

E-ISSN: 2581-690X

Ciamak Ghazaei
1Department of Microbiology,Faculty of Agriculture and Natural Resources of Moghan, University of Mohaghegh Ardabili, Ardabil,P .O. Box 179, Iran.
J Pure Appl Microbiol. 2013;7(2):1447-1450
© The Author(s). 2013
Received: 25/09/2012 | Accepted: 11/11/2012 | Published: 30/06/2013

The factor of virulence has become inherent among a multitude of bacterial populations surviving on pathogenic mode of life. To this end, ‘Neuraminidase’ is an important enzyme reported to execute the virulence mechanism. It accomplishes this task by acting on glycosidic linkages of terminal sialic acid residues in glycoconjugates and synthetic substrates. Exo and endo-a-neuraminidases are the two types identified so far based on the neuraminidase led glycosidic cleavage of sialic acid. The key mandatory event for the commencement of virulence is the bacterial acquisition of sialic acid through scavenger pathway by neuraminidases. As virulent factor, neuraminidase contributes to a variety of perturbations like high viscosity of blood, thrombocytopenia, hemolytic anemia, loss of circulating factors, increased immune complex, auto immune conditions, deficiency of mucus viscoelasticity etc. The existence of neuraminidase in several functional forms of ‘Nan’ and its contribution to ‘biofilm formation’ appears to influence the evolving mechanisms and survival rates of pathogenic bacteria. With this, neuraminidase involvement in many diseases has shed much light and increased research attention has further widened its exploration as virulent factor in bacteria.


Neuraminidase,Virulence, Enzyme, Sialic acid

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