Serological and biochemical properties of the major outer membrane protein within strains of the genus Actinobacillus.
Sarcosyl-extracted outer membrane preparations of organisms of the genus Actinobacillus were investigated with regard to heat-modifiable and serological properties as well as N-terminal amino acid sequencing of the isolated major outer membrane protein (Omp). The major Omp of Actinobacillus lignieresii was recognized by a monoclonal antibody with specificity towards Proteus mirabilis OmpA. Moreover, N-terminal amino acid sequencing revealed strong homology to OmpA of enterobacteriaceae, on the contrary, no reaction of the Proteus mirabilis OmpA monoclonal antibody was detectable when investigating the outer membrane preparations of Actinobacillus suis and Actinobacillus equuli in Western blot analyses. N-terminal amino acid sequencing of the major Omp of these two species showed homologies to OmpC or OmpF of the enterobacteriaceae. In accordance with these results, a polyclonal antibody with specificity for the major Omp of Pasteurella multocida cross-reacted with the major Omps of Actinobacillus suis and Actinobacillus equuli. The relationship of the major Omp of Pasteurella multocida and OmpC and OmpF had been verified in recent studies.
Hartmann
L
L
Institut für Mikrobiologie und Tierseuchen, Freie Universität Berlin, Germany.
Schröder
W
W
Lübke-Becker
A
A
D000188:Actinobacillus / Q000378:metabolism*; D000595:Amino Acid Sequence; D000942:Antigens, Bacterial / Q000737:chemistry*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006361:Heating; D015151:Immunoblotting; D008623:Mercaptoethanol / Q000737:chemistry; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D012967:Sodium Dodecyl Sulfate; D008623:Mercaptoethanol