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Infection and Immunity, March 2002, p. 1209-1218, Vol. 70, No. 3
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.3.1209-1218.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of hsa, the Gene Encoding the Sialic Acid-Binding Adhesin of Streptococcus gordonii DL1

Yukihiro Takahashi,1* Kiyoshi Konishi,1 John O. Cisar,2 and Masanosuke Yoshikawa1

Department of Microbiology, The Nippon Dental University School of Dentistry at Tokyo, Chiyoda-ku, Tokyo 102-8159, Japan,1 Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, Bethesda, Maryland 20892-43522

Received 4 September 2001/ Returned for modification 24 October 2001/ Accepted 27 November 2001

Oral colonization by Streptococcus gordonii, an important cause of subacute bacterial endocarditis, involves bacterial recognition of sialic acid-containing host receptors. The sialic acid-binding activity of this microorganism was previously detected by bacterium-mediated hemagglutination and associated with a streptococcal surface component identified as the Hs antigen. The gene for this antigen (hsa) has now been cloned in Escherichia coli, and its expression has been detected by colony immunoblotting with anti-Hs serum. Mutants of S. gordonii containing hsa inactivated by the insertion of an erythromycin resistance gene or deletion from the chromosome were negative for Hs-immunoreactivity, bacterium-mediated hemagglutinating activity, and adhesion to {alpha}2-3-linked sialoglycoconjugates. The deletion in the latter mutants was complemented by plasmid-borne hsa, resulting in Hs antigen production and the restoration of cell surface sialic acid-binding activity. The hsa gene encodes a 203-kDa protein with two serine-rich repetitive regions in its 2,178-amino-acid sequence. The first serine-rich region occurs within the amino-terminal region of the molecule, between different nonrepetitive sequences that may be associated with sialic acid binding. The second serine-rich region, which is much longer than the first, is highly repetitive, containing 113 dodecapeptide repeats with a consensus sequence of SASTSASVSASE. This long repetitive region is followed by a typical gram-positive cell wall anchoring region at the carboxyl-terminal end. Thus, the predicted properties of Hsa, which suggest an amino-terminal receptor-binding domain attached to the cell surface by a molecular stalk, are consistent with the identification of this protein as the sialic acid-binding adhesin of S. gordonii DL1.

* Corresponding author. Mailing address: Department of Microbiology, The Nippon Dental University School of Dentistry at Tokyo, 1-9-20 Fujimi, Chiyoda-ku, Tokyo 102-8159, Japan. Phone: 81-3-3261-8763. Fax: 81-3-3264-8399. E-mail: biseibut{at}tokyo.ndu.ac.jp.

Infection and Immunity, March 2002, p. 1209-1218, Vol. 70, No. 3
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.3.1209-1218.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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