Abstract:
:In a previous study, we isolated the spaA gene encoding the surface protective antigen A, SpaA, of Erysipelothrix rhusiopathiae, and found that the N-terminal region of SpaA was responsible for protective immunity against erysipelas and that the C-terminal region contained eight repeat units consisting of 20 amino acids comprising the binding domain on the Erysipelothrix cell surface. In this study, using recombinant SpaA proteins, we showed that the repeat region bound to the cell surfaces of various Gram-positive bacterial cells, SpaA was a membrane-associated protein, this association depended on the interaction with choline residues in teichoic acid, and SpaA bound to lipoteichoic acid (LTA) of Bacillus subtilis and Staphylococcus aureus. These results showed that LTA was required for the surface association of SpaA in E. rhusiopathiae and that such an association might be common among Gram-positive bacterial cells. We suggested that an LTA-SpaA complex might have an important role in the E. rhusiopathiae infection process.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Makino SI,Yamamoto K,Asakura H,Shirahata Tdoi
10.1111/j.1574-6968.2000.tb09123.xkeywords:
subject
Has Abstractpub_date
2000-05-15 00:00:00pages
313-7issue
2eissn
0378-1097issn
1574-6968pii
S0378-1097(00)00164-6journal_volume
186pub_type
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