Surface antigen, SpaA, of erysipelothrix rhusiopathiae binds to Gram-positive bacterial cell surfaces.

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 Lett

authors

Makino SI,Yamamoto K,Asakura H,Shirahata T

doi

10.1111/j.1574-6968.2000.tb09123.x

keywords:

subject

Has Abstract

pub_date

2000-05-15 00:00:00

pages

313-7

issue

2

eissn

0378-1097

issn

1574-6968

pii

S0378-1097(00)00164-6

journal_volume

186

pub_type

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