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Six Isolates of Mycoplasma bovocull from cattle herds with Infectious bovine keratoconjunctivitis were analyzed by gel electrophoresis and immunoblotting techniques. All six strains showed similarity in their protein profiles although no two patterns were Identical. A monoclonal antibody, hyperimmune rabbit serum, and post-exposure sera from three mycoplasma-free calves experimentally infected with one strain were used for immunoblotting analysis. Monoclonal antibody recognized a band of 94,000 molecular-weight designated p94 common to all strains. This p94 was recognized by post-exposure antisera from all three calves. Hyper­ immune rabbit serum detected antigenic differences between these strains ranging from 15k-136k. Trypsin treatment of intact mycoplasma cells re­ sulted in the removal of p94 when tested with monoclonal antibody and calf sera. Trypsin treated cells reacted with hyperimmune rabbit serum revealed the presence of strain-specific and conserved antigens between these strains. These studies identify the presence of a conserved trypsin-sensitive surface protein (p94) of M. bovoculi involved in eliciting antibody response in the infected host.

Comparison between Mycoplasma bovoculi strains by electrophoretic and immunoblotting techniques: identification of membrane proteins involved in adherence