Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5543937 | Research in Veterinary Science | 2017 | 7 Pages |
Abstract
This work describes the purification and characterization of PorPV HN protein (isolate PAC1). The specificity of neuraminidase is restricted to sialyl(α2,3)lactose (3SL). HN showed typical Michaelis-Menten kinetics with fetuin as substrate (km = 0.029 μM, Vmax = 522.8 nmol minâ 1 mgâ 1). When 3SL was used as substrate, typical cooperative kinetics were found (S50 = 0.15 μM, Vmax = 154.3 nmol minâ 1 mgâ 1). The influenza inhibitor zanamivir inhibited the PorPV neuraminidase with IC50 of 0.24 μM. PorPV neuraminidase was activated by Ca2 + and inhibited by nucleoside triphosphates with the level of inhibition depending on phosphorylation level. The present results open possibilities to study the role of neuraminidase in the pathogenicity of PorPV infection and its potential inhibitors.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Animal Science and Zoology
Authors
Gerardo Santos-López, MarÃa T. Borraz-Argüello, Luis Márquez-DomÃnguez, Juan Carlos Flores-Alonso, Humberto RamÃrez-Mendoza, Bernard Priem, Sébastien Fort, Verónica Vallejo-Ruiz, Julio Reyes-Leyva, Irma Herrera-Camacho,