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.
Lübke
A
A
Institut für Mikrobiologie und Tierseuchen, Fachbereich Veterinärmedizin, Freie Universität Berlin, Berlin-Dahlem, Germany.
Hartmann
L
L
Schröder
W
W
Hellmann
E
E
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D004797:Enzyme-Linked Immunosorbent Assay; D016978:Mannheimia haemolytica / Q000737:chemistry*; D008969:Molecular Sequence Data; D016979:Pasteurella multocida / Q000737:chemistry*
D001425:Bacterial Outer Membrane Proteins