Gallibacterium anatis-secreted metalloproteases degrade chicken IgG
| Autor: | Erasmo Negrete-Abascal, E. García-Gómez, J. Ibarra-Caballero, Sergio Vaca, V. Pérez-Márquez, A. Pérez-Méndez, V. R. Tenorio |
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| Rok vydání: | 2005 |
| Předmět: |
medicine.medical_treatment
Immunoglobulin G Microbiology Food Animals Bacterial Proteins medicine Animals Pasteurella Actinobacillus pleuropneumoniae Anatis Protease General Immunology and Microbiology biology Molecular mass Temperature Hydrogen-Ion Concentration biology.organism_classification Secretory protein Biochemistry Polyclonal antibodies biology.protein Metalloproteases Animal Science and Zoology Pasteurellaceae Chickens |
| Zdroj: | Avian pathology : journal of the W.V.P.A. 34(5) |
| ISSN: | 0307-9457 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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