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Journal of Bacteriology, September 1999, p. 5176-5184, Vol. 181, No. 17
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Molecular Characterization of Type-Specific Capsular Polysaccharide Biosynthesis Genes of Streptococcus agalactiae Type Ia

Shin Yamamoto,1 Katsuhide Miyake,1 Yoichi Koike,1 Masaki Watanabe,1 Yuichi Machida,1 Michio Ohta,2 and Shinji Iijima1,*

Department of Biotechnology, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8603,1 and Department of Bacteriology, School of Medicine, Nagoya University, Nagoya, 466-5880,2 Japan

Received 8 March 1999/Accepted 30 June 1999

The type-specific capsular polysaccharide (CP) of a group B streptococcus, Streptococcus agalactiae type Ia, is a high-molecular-weight polymer consisting of the pentasaccharide repeating unit 4)-[alpha -D-NeupNAc-(2right-arrow3)-beta -D-Galp-(1right-arrow4)-beta -D-GlcpNAc-(1right-arrow3)]-beta -D-Galp-(1right-arrow4)-beta -D-Glcp-(1. Here, cloning, sequencing, and transcription of the type Ia-specific capsular polysaccharide synthesis (cps) genes and functional analysis of these gene products are described. A 26-kb DNA fragment containing 18 complete open reading frames (ORFs) was cloned. These ORFs were designated cpsIaA to cpsIaL, neu (neuraminic acid synthesis gene) A to D, orf1 and ung (uracil DNA glycosylase). The cps gene products of S. agalactiae type Ia were homologous to proteins involved in CP synthesis of S. agalactiae type III and S. pneumoniae serotype 14. Unlike the cps gene cluster of S. pneumoniae serotype 14, transcription of this operon may start from cpsIaA, cpsIaE, and orf1 because putative promoter sequences were found in front of these genes. Northern hybridization, reverse transcription-PCR, and primer extension analyses supported this hypothesis. DNA sequence analysis showed that there were two transcriptional terminators in the 3' end of this operon (downstream of orf1 and ung). The functions of CpsIaE, CpsIaG, CpsIaI, and CpsIaJ were examined by glycosyltransferase assay by using the gene products expressed in Escherichia coli JM109 harboring plasmids containing various S. agalactiae type Ia cps gene fragments. Enzyme assays suggested that the gene products of cpsIaE, cpsIaG, cpsIaI, and cpsIaJ are putative glucosyltransferase, beta -1,4-galactosyltransferase, beta -1,3-N-acetylglucosaminyltransferase, and beta -1,4-galactosyltransferase, respectively.

* Corresponding author. Mailing address: Department of Biotechnology, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya, 464-8603, Japan. Phone: 81-52-789-4275. Fax: 81-52-789-3221. E-mail: iijima{at}proc.nubio.nagoya-u.ac.jp.

Journal of Bacteriology, September 1999, p. 5176-5184, Vol. 181, No. 17
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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