Haemophilus ducreyi contains a major outer membrane protein (MOMP) whose apparent molecular weight is 39,000 to 42,000 for all strains tested. Two monoclonal antibodies (MAbs), designated 9D12 and 2C7, bound to the MOMP for all strains of H. ducreyi tested. As reported previously, MAb 9D12 was H. ducreyi specific (E. J. Hansen and T. A. Loftus, Infect. Immun. 44:196-198, 1984). MAb 2C7 bound to all members of the family Pasteurellaceae tested, suggesting that the MAbs bound to distinct epitopes on the MOMP. The MOMP was purified by extraction of whole cells with Zwittergent and ion-exchange chromatography. A peak eluted from a cation-exchange column contained three bands. All three species bound both MAbs, and the fraction yielded a single N-terminal amino acid sequence, suggesting that the bands represented different conformations of the MOMP. The MOMP was heat modifiable, contained two cysteine residues, and was cationic at pH 8.0, features not usually associated with classical porin proteins. The N-terminal amino acid sequence and total amino acid content of the MOMP were homologous to the OmpA proteins of members of the family Enterobacteriaceae and the OmpA-like protein of Actinobacillus actinomycetemcomitans. An OmpA-specific polyclonal serum bound to the MOMP, and MAb 2C7 bound to Haemophilus influenzae protein 5, an OmpA- like protein, indicating that the MOMP was antigenically related to OmpA. These data indicated that the most abundant protein in the outer membrane of H. ducreyi was not a classical porin and belonged to the OmpA family of proteins.
|Original language||English (US)|
|Number of pages||6|
|Journal||Infection and immunity|
|State||Published - Jan 1 1993|
ASJC Scopus subject areas
- Infectious Diseases