García-Gómez E, Vaca S, Pérez-Méndez A, Ibarra-Caballero J, Pérez-Márquez V, Tenorio VR, Negrete-Abascal E.
Avian Pathol. 2005 Oct;34(5):426-9.
Carrera de Biología, Facultad de Estudios Superiores Iztacala, UNAM, Av. de los Barrios # 1, Los Reyes Iztacala, Tlalnepantla, Estado de México 54090, México.
Gallibacterium anatis (previously named Pasteurella haemolytica-like) is considered a normal inhabitant of genital and upper respiratory tracts of healthy chickens, but it is also associated with different pathological conditions. Secreted metalloproteases from field and reference G. anatis cultures were obtained by methanol precipitation and were characterized. Proteins of molecular mass higher than 100 kDa showing proteolytic activity were observed in 10% polyacrylamide gels copolymerized with 1% bovine casein. They were active at alkaline pH, and inhibited by ethylenediamine tetraacetic acid. Their activity was stable at 50 degrees C, but partially inhibited at 60 degrees C, and totally inhibited at higher temperatures. Secreted proteins were able to degrade chicken IgG after 24 h of incubation, and cross-reacted with a polyclonal antibody against purified protease from Actinobacillus pleuropneumoniae. Secreted metalloproteases could play a role in infections caused by G. anatis.