Sialidase pathogenesis

Influenza virus sialidase poses a highly attractive target for antiviral drug design due to its prominent position at the surface of the virion and its profound role in viral pathogenesis. Random screening programs identified a number of... 

A. Buschiazzo, M. F. Amaya, M. L. Cremona, A. C. C. Frasch, and P. M. Alzari, The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis, Mol. Cell,... 

M. G. Risso, T. A. Pitcovsky, R. L. Caccuri, O. Campetella, and M. S. Leguizamon, Immune system pathogenesis is prevented by the neutralization of the systemic tram-sialidase from Trypanosoma cruzi during severe infections, Parasitology, 134 (2007) 503-510. 

C. A. Vercelli, A. M. Hidalgo, S. H. Hyon, and P. F. Argibay, Trypanosoma cruzi tram-sialidase inhibits human lymphocyte proliferation by nonapoptotic mechanisms implications in pathogenesis and transplant immunology, Transplant. Proc., 37 (2005) 4594 1597. 

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). 

A number of pathogens also have sialidases to aid in pathogenesis or nutrition. Orthomyxoviruses (e.g. influenza) and paramyxoviruses (e.g. mumps, parainfluenza, Newcastle disease, Sendai) have sialidases on their surfaces. Surface sialidase activity is also exhibited by parasites such as Trypanosoma cruzi, T. brucei as well as a number of both pathogenic and non-pathogenic bacteria which may also secrete the enzyme. 

Corfield, A. P., 1992, Bacterial sialidases—Roles in pathogenesis and nutrition, Glycobiology 2 509-521. 

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