PMID: 10802190May 10, 2000

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

FEMS Microbiology Letters
S MakinoT Shirahata


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.


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Mar 8, 2008·Applied Microbiology and Biotechnology·Adilson José da SilvaTeresa Cristina Zangirolami
May 4, 2007·Clinical and Vaccine Immunology : CVI·Ho To, Shinya Nagai


May 1, 1994·Journal of Bacteriology·J Yother, J M White
Mar 1, 1994·Proceedings of the National Academy of Sciences of the United States of America·D W DunneK A Joiner

Related Concepts

Gram-Positive Bacteria
Erysipelothrix Infection
Bacterial cell
Bacterial Proteins
Carboxy-Terminal Amino Acid
Chimeric Proteins, Recombinant
Amino Acids, I.V. solution additive
Proteins, Recombinant DNA
Erysipelothrix rhusiopathiae

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