Purification of the receptor for the N-acetyl-d-glucosamine specific adhesin of Mannheimia haemolytica from bovine neutrophils


Por: De la Mora A., Suárez-Güemes F., Trigo F., Gorocica P., Solórzano C., Slomianny M.-C., Agundis C., Pereyra M.A., Zenteno E.

Publicada: 1 ene 2007
Resumen:
The GlcNAc-specific adhesin from Mannheimia haemolytica (MhA) has been shown to participate in pathogenicity of mannheimiosis due to its capacity to adhere to tracheal epithelial cells and activate the oxidative burst of bovine neutrophils. In this work, we purified the MhA receptor from bovine neutrophils (MhAr) by affinity chromatography on MhA-Sepharose. The MhAr, which corresponded to approximately 2% of the protein from cell lysate, is a glycoprotein mainly composed of Glu, Ala, Ser, Gly, and Asp, without cysteine. The glycan portion, which corresponds to 20% by weight, is composed of GalNAc, GlcNAc, Man, Gal, and NeuAc. The receptor is a 165-kDa glycoprotein, as determined by molecular sieve chromatography under native conditions; SDS-PAGE analysis shows a heterodimer of 83 and 80 kDa subunits. This work suggests that the GlcNAc-containing receptor plays a relevant role by activating bovine neutrophils through non-opsonic mechanisms. © 2007 Elsevier B.V. All rights reserved.

Filiaciones:
De la Mora A.:
 Laboratorio de Patología, Instituto de Investigaciones en Ciencias Veterinarias, Universidad Autónoma de Baja California, Mexicali, BC, Mexico

Suárez-Güemes F.:
 Facultad de Medicina Veterinaria y Zootecnia, Universidad Nacional Autónoma de México, Mexico

Trigo F.:
 Facultad de Medicina Veterinaria y Zootecnia, Universidad Nacional Autónoma de México, Mexico

Gorocica P.:
 Departamento de Bioquímica, Instituto Nacional de Enfermedades Respiratorias, Secretaría de Salud, Mexico

Solórzano C.:
 Laboratoire de Chimie Biologique, la Université des Sciences et Technologies de Lille, UMR, Villeneuve d'Ascq, 59655 Cedex, France

Slomianny M.-C.:
 Laboratoire de Chimie Biologique, la Université des Sciences et Technologies de Lille, UMR, Villeneuve d'Ascq, 59655 Cedex, France

Agundis C.:
 Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, P. O. Box 70159, 04510 México, D.F., Mexico

Pereyra M.A.:
 Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, P. O. Box 70159, 04510 México, D.F., Mexico

Zenteno E.:
 Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, P. O. Box 70159, 04510 México, D.F., Mexico
ISSN: 03044165
Editorial
ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS, Países Bajos
Tipo de documento: Article
Volumen: 1770 Número: 10
Páginas: 1483-1489
WOS Id: 000250187600007
ID de PubMed: 17707591

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