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 membrane protein (MOMP) of P. multocida shared a strong homology with those of homotrimeric nonspecific porins of gram-negative bacteria. The capacity of outer membrane protein (OMP) preparations of P. multocida to bind to respiratory mucosal surface preparations was inhibited significantly by using a polyclonal anti-p35 antiserum in an adhesion ELISA. Anti-p35 antiserum cross-reacted with a 44 kDa (p44) MOMP of P. haemolytica. N-terminal sequencing of MOMP p44 revealed a homology of 81% with the putative porin MOMP p35 of P. multocida.