Biochemical and immunological characterization of cell surface proteins of Pasteurella multocida strains causing atrophic rhinitis in swine

Abstract

we showed that among 34 isolates from swine the membrane protein and lipopolysaccharide (LPS) patterns, as analyzed by sodium dodecyl sulfate-gel electrophoresis, could be classified into three and six patterns, respectively. In all cases a certain LPS pattern was correlated with a certain protein pattern. Certain combinations of types of cell surface proteins and LPSs were correlated with pathogenicity, the latter property being judged by the guinea pig skin test. In the present paper the immunological and biochemical properties of cell surface constituents were analyzed. The reaction between electrophoretically separated cell surface constituents with guinea pig and sow antisera showed that LPS as well as several proteins were immunogenic. Among these is protein H, whose electrophoretic mobility is the main criterium for typing of cell envelope protein patterns. Protein H was the most heavily labeled component when whole cells were iodinated by the Iodo-Gen procedure, showing its accessibility at the cell surface. These properties of protein H make it an attractive vaccine candidate. Further biochemical analyses revealed that protein H shares many properties with pore proteins of members of the family Enterobacteriaceae. One of these properties, association between pore proteins and peptidoglycan, was used as the basis for a simple procedure developed to partially purify protein H.

Purification and characterization of protein H, the major porin of Pasteurella multocida

“…This microorganism is pathogenic for humans and a wide variety of mammals and birds (35) and is often associated with Bordetella bronchiseptica in atrophic rhinitis of swine (46). Lugtenberg et al (30,31) presented evidence for the presence in the envelope of P. multocida of a 37.5-kDa major protein (protein H) which, owing to its high immunogenicity and exposure on the cell surface, is considered an attractive vaccine candidate. This protein has been partially purified and shown to share several properties with porins of enterobacteria, namely, resistance to denaturation by sodium dodecyl sulfate (SDS) and noncovalent association with murein (31).…”

In Process Quality Control Factors Affecting Potency of Fowl Cholera Vaccine

“…Washed culture of P. multocida (bacterial suspension free from LPS and medium component) induced significantly higher antibody titer as compared to the vaccine prepared from purified LPS or whole culture vaccine (p<0.05: Figure-III). Outer membrane proteins (OMPs) of P. multocida have been studied as potential immunogens, which make them potential vaccine candidates (Lugtenberg et al, 1986;Rhoades & Rimler, 1989;Lu et al, 1983;Adler et al, 1996). Purified OMP of P. multocida or whole culture induces antibody response in rabbit and show resistance to challenge infection (Adler et al, 1996).…”

Isolation of the Major Outer‐membrane Protein of Actinobacillus pleuropneumonias and Haemophilus parasuis

“…N-terminal sequencing was performed using the Edman method and the data were analysed using the software Model 610 A Data Analysis Program version 1.2 (ABI). (LUGTENBERG et al, 1986), whereas p40 from A . pleuropneumoniae and p42 from H. parasuzs displayed no heat-modifiability after solubilization at 37 "C, as P. haemolytica had (data not shown).…”

“…The immunoblot results and the N-terminal homologies suggest that p40 and p42 are at least related to porin proteins. Sarcosyl insoluble proteins are known to be OMPs, cell-surface exposed, and therefore accessible to antibodies (LUGTENBERG et al, 1986;LU et al, 1988). In addition to their capability of forming water-filled trans-outer-membrane channels (porins), which permit the passage of small hydrophilic molecules, OMPs, particularly MOMPs, are probably also involved in the infectious process.…”