Whole cell proteins of eight bovine mycoplasmas (M, bovoculi, M, bovis, M.
dispar, M. bovirhinis, M. arginini, M. verecundum, M. canadense, M. alkales
cens) were separated by SDS-PAGE and transferred to nitrocellulose paper. R
abbit anti-hi bovoculi serum was found to react with immunoblots of all myc
oplasma species tested. These cross-reactive proteins were in the range of
35,000-100,000 molecular weight. Monoclonal antibody MA25.5 developed again
st a M. bovoculi 94 kDa surface protein cross-reacted with a band of 62 kDa
from M. dispar and three bands of 89, 85 and 74 kDa from M. arginini only
while MA18.13 that recognized a band of 57 kDa from M. bovoculi did not rea
ct with the other species. The role of MA25.5 monoclonal antibody in inhibi
ting the growth of hi, bovoculi, ill. dispar and M. arginini was tested usi
ng the metabolic-inhibition (MI) test. Monoclonal antibody MA25.5 inhibited
the growth of M. bovoculi and also inhibited ill dispar growth but at lowe
r MI titers, while it showed no effect on the growth of M. arginini. (C) 20
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