Metalloproteases Secreted by <Emphasis Type="Italic">Actinobacillus suis</Emphasis> |
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| Authors: | Erasmo Negrete-Abascal Sergio Vaca Pacheco Gloria L Paniagua Alma Pérez Méndez Jorge Ibarra Caballero Víctor M Pérez Márquez Víctor R Tenorio |
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| Institution: | (1) Carrera De Biología, Facultad de Estudios Superiores Iztacala, UNAM, Av. de los Barrios # 1, Los Reyes Iztacala, Tlalnepantla, Estado de México, 54090, Mexico;(2) Biotecnología Veterinaria S.A. de C.V. Tehuacan, Puebla, 75760, Mexico;(3) CENID-Microbiología, Carr. México-Toluca Km. 15.5, Cuajimalpa, México D.F. 05110, Mexico |
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| Abstract: | Actinobacillus suis secretes metalloproteases into its medium. These secreted proteins, when concentrated by precipitation with 70% (NH4)2SO4 or methanol, displayed proteolytic activity at >200 kDa molecular mass bands in 10% polyacrylamide gels copolymerized with bovine casein (1%). They showed activity in a broad pH range (from pH 5 to pH 10) and were inhibited by 20 mM EDTA or EGTA, but could be reactivated by calcium. They were found heat stable at 40°C, 50°C, 60°C, and 70°C, but their activity diminished at 80°C or higher. They degraded pig and bovine IgG and cross-reacted with a polyclonal serum against a high molecular mass secreted protease from A. pleuropneumoniae. Extracellular proteases could play a role in diseases caused by A. suis. |
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