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Infection and Immunity, November 2001, p. 6987-6998, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.6987-6998.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

A 60-Kilodalton Immunodominant Glycoprotein Is Essential for Cell Wall Integrity and the Maintenance of Cell Shape in Streptococcus mutans

Jean-San Chia,1,* Lan Yi Chang,1 Chia-Tung Shun,2 Ying-Ying Chang,3 and Jen-Yang Chen1

Graduate Institute of Microbiology, College of Medicine National Taiwan University,1 and Department of Forensic Medicine2 and Department of Pathology,3 National Taiwan University Hospital, Taipei, Taiwan, Republic of China

Received 30 April 2001/Returned for modification 3 July 2001/Accepted 12 July 2001

We have demonstrated previously by Western blotting that in naturally sensitized humans, the serum or salivary antibody response to Streptococcus mutans was directed predominantly to a protein antigen with a size of approximately 60-kDa. To identify this immunodominant antigen, specific serum antibodies were eluted from immunoblots and five positive clones with inserts ranging in length from 3 to 8 kb from identical chromosomal loci were obtained by screening a genomic expression library of Streptococcus mutans GS-5. Amino acid sequencing established the identity of this immunodominant antigen, a 60-kDa immunodominant glycoprotein (IDG-60), to be a cell wall-associated general stress protein GSP-781, which was originally predicted to have a molecular mass of approximately 45 kDa based on the derived nucleotide sequence. Discrepancy in the molecular mass was also observed in recombinant his-tagged IDG-60 (rIDG-60) expressed from Escherichia coli. Glycosylation, consisting of sialic acid, mannose galactose, and N-acetylgalactosamine, was detected by lectin binding to IDG-60 in cell wall extracts from S. mutans and rIDG-60 expressed in vivo or translated in vitro. Despite the presence of multiple Asn or Ser or Thr glycosylation sites, IDG-60 was resistant to the effect of N-glycosidase F and multiple O-glycosidase molecules but not to beta -galactosidase. Insertional inactivation of the gene encoding IDG-60, sagA, resulted in a retarded growth rate, destabilization of the cell wall, and pleiomorphic cell shape with multifold ingrowth of cell wall. In addition, distinct from the parental GS-5 strain, the isogenic mutant GS-51 was unable to survive the challenge of low pH and high osmotic pressure or high temperature. Expression of the wild-type gene in trans within GS-51 from plasmid pDL277 complemented the growth defect and restored normal cell shape. These results suggested that IDG-60 is essential for maintaining the integrity of the cell wall and the uniformity of cell shape, both of which are indispensable for bacteria survival under stress conditions.

* Corresponding author. Mailing address: No. 1, Jen Ai Road 1st Section, Room 713, Graduate Institute of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan. Phone: 886-2-23123456, ext. 8222. Fax: 886-2-23915293. E-mail: chiajs{at}ha.mc.ntu.edu.tw.

Infection and Immunity, November 2001, p. 6987-6998, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.6987-6998.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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