Author/Authors :
De la Mora، نويسنده , , Alfonso and Trigo، نويسنده , , Francisco and Jaramillo، نويسنده , , Laura and Garfias، نويسنده , , Yonathan and Solَrzano، نويسنده , , Carlos and Agundis، نويسنده , , Concepciَn and Pereyra، نويسنده , , Ali and Lascurain، نويسنده , , Ricardo and Zenteno، نويسنده , , Edgar and Suلrez-Güemes، نويسنده , , Francisco، نويسنده ,
Abstract :
In this work we identified specific bovine leukocytes that were bound by the Mannheimia haemolytica adhesin molecule (MhA) and the biological effect on the leukocytes. Histochemical staining and flow cytometry showed that MhA bind neutrophils (90%) and monocytes (5%). MhA induced an oxidative response in purified neutrophils; this effect was 1.5-fold higher than the effect observed with control cells activated with Zymosan. Cellular binding by MhA was inhibited with GlcNAc and its oligomers, as well as by glycoproteins containing tri- and tetra-antennary N-glycosydically linked glycans. MhA-induced oxidative burst was significantly inhibited by GlcNAc, iodoacetamide, superoxide dismutase, and piroxicam (p < 0.05). Our findings suggest that among bovine leukocytes, neutrophils are the main target for MhA, inducing production of oxidative radicals by non-opsonic mechanism that seem to play an important role in tissue damage during mannheimiosis.
Keywords :
Mannheimia haemolytica , adhesin , GlcNAc-specificity , Bovine , Neutrophils oxidative burst , Mannheimiosis