ISOLATION AND PARTIAL CHARACTERIZATION OF THE MAJOR PROTEIN OF THE OUTER-MEMBRANE OF PASTEURELLA-HAEMOLYTICA AND PASTEURELLA-MULTOCIDA

The N-terminal amino acid sequence of the 35 kDa (p35) major outer mem brane protein (MOMP) of P. multocida shared a strong homology with tho se of homotrimeric nonspecific porins of gram-negative bacteria. The c apacity of outer membrane protein (OMP) preparations of P. multocida t o bind to respiratory mucosal surface preparations was inhibited signi ficantly by using a polyclonal anti-p35 antiserum in an adhesion ELISA . Anti-p35 antiserum cross-reacted with a 44 kDa (p44) MOMP of P. haem olytica. N-terminal sequencing of MOMP p44 revealed a homology of 81% with the putative porin MOMP p35 of P. multocida.