Protective Activity of the Purified Protein Antigen of Erysipelothrix rhusiopathiae in Pigs

Abstract

We purified the protein antigen (P64), which contains 66 and 64 kDa proteins, from the alkaline extract (AE) of whole cells of Erysipelothrix rhusiopathiae strain Agata (serovar 5) to determine the protective activity of the antigen against E. rhusiopathiae infection in pigs. The serum titre of antibody against P64 rapidly increased in pigs immunized with 500 and 100 mg of P64 and reached maximum values at 3 weeks after the first immunization (1 week after the second immunization). However, the serum antibody titres were not increased in pigs immunized with 20 mg of P64 and in nonimmunized pigs. In the pigs immunized with live cell vaccine (acriflavin-fast attenuated strain Koganei 65-0.15), the serum titres of antibody against P64 also increased at 1-2 weeks after immunization. In a pig challenge test performed on immunized and nonimmunized pigs, all nonimmunized pigs showed typical clinical signs of swine erysipelas (fever, erysipeloid, arthritis), while all pigs immunized with 500 and 100 mg of P64 and live cell vaccine showed no clinical signs of this disease. In Western blot analysis, sera from pigs immunized with P64 and live cell vaccine strongly reacted with the 64 kDa protein. In contrast, the serum from nonimmunized pigs did not react with any proteins. From these results, it was suggested that a specific antibody against the 64 kDa protein could be increased in pigs immunized with P64 or live cell vaccine and that this anti-P64 antibody has a strong protective effect against E. rhusiopathiae infection in pigs. U. S.

Role of Surface Protective Antigen A in the Pathogenesis of Erysipelothrix rhusiopathiae Strain C43065

“…Briefly, whole-cell proteins from either the ∆spaA mutant or the wild-type strain C43065 were compared by SDS-PAGE, followed by Coomassie staining and western blotting. Although several nonspecific proteins (14,20,28, and 66 kDa protein bands) were evident in both samples by Coomassie staining, the 64 kDa protein only appeared in samples of the wild-type strain, but not in samples of the mutant strain (Fig. 3C).…”

“…Surface protective antigens of gram-positive bacteria have been implicated in both virulence and protection during bacterial infection [10,27]. Among several cell surface proteins identified in E. rhusiopathiae, SpaA has been shown to be a 64 kDa surface protective antigen associated with the induction of highly protective antibodies against E. rhusiopathiae after infection in both mice and pigs [5,14,17,28]. Structural and sequence analyses have revealed that the C-terminal region of SpaA is very similar to the choline-binding proteins of Streptococcus pneumoniae, which can bind to choline residues of teichoic acid [8].…”

Pathogenic characterization of <i>Erysipelothrix rhusiopathiae</i> Met-203 type SpaA strains from chronic and subacute swine erysipelas in Japan

“…The clinical signs of SE can be divided into three types: acute (septicemia), subacute (urticaria) and chronic (arthritis, lymphadenitis and endocarditis) [ 20 ]. Surface protective antigen (Spa) A is well known as one of the major protective antigens of E. rhusiopathiae [ 7 , 21 ]. The N-terminal half of the hypervariable region of SpaA in particular has been shown to be important for specific immunity to the infection [ 3 , 13 , 17 ].…”