Identification, purification, and characterization of the type 4 fimbriae of Pasteurella multocida

• Published in: Infection and Immunity 1997, Vol.65 (1), p.339-343
• Main Authors: RUFFOLO, C. G, TENNENT, J. M, MICHALSKI, W. P, ADLER, B
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - immunology; Bacteriology; Biological and medical sciences; Cross Reactions; Dichelobacter nodosus; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - immunology; Fimbriae Proteins; Fimbriae, Bacterial - chemistry; Fimbriae, Bacterial - classification; Fundamental and applied biological sciences. Psychology; Microbiology; Molecular Sequence Data; Moraxella bovis; Pasteurella multocida; Pasteurella multocida - chemistry; Pasteurella multocida - classification; Pasteurella multocida - immunology; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Sequence Analysis; Sequence Homology; Serotyping
• ISSN: 0019-9567; 1098-5522
• DOI: 10.1128/iai.65.1.339-343.1997

The presence of fimbriae on Pasteurella multocida has been reported, but there have been no prior studies aimed at conclusively characterizing these structures. We now report on the identification and characterization of type 4 fimbriae on serogroup A, B, and D strains of P. multocida. Under microaerophilic conditions P. multocida showed an increased expression of the fimbriae, which were observed to form bundles. Fimbriae purified by high-performance reverse-phase liquid chromatography constituted a single 18-kDa subunit, the first 21 amino acids of which shared very high similarity with the N-terminal amino acid sequence of other type 4 fimbrial subunits. Antiserum against the P. multocida 18-kDa protein immunostained the type 4 fimbrial subunit of Moraxella bovis and Dichelobacter nodosus. Based on these observations we conclude that P. multocida possesses type 4 fimbriae and have designated the P. multocida fimbrial subunit PtfA.