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

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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-weightpolymer consisting of the pentasaccharide repeating unit 4)-[ $alpha$ -D-NeupNAc-(2 $right-arrow$ 3)- $beta$ -D-Galp-(1 $right-arrow$ 4)- $beta$ -D-GlcpNAc-(1 $right-arrow$ 3)]- $beta$ -D-Galp-(1 $right-arrow$ 4)- $beta$ -D-Glcp-(1.Here, cloning, sequencing, and transcription of the type Ia-specificcapsular polysaccharide synthesis (cps) genes and functional analysisof these gene products are described. A 26-kb DNA fragment containing18 complete open reading frames (ORFs) was cloned. These ORFswere designated cpsIaA to cpsIaL, neu (neuraminic acid synthesisgene) A to D, orf1 and ung (uracil DNA glycosylase). The cps geneproducts of S. agalactiae type Ia were homologous to proteinsinvolved in CP synthesis of S. agalactiae type III and S. pneumoniaeserotype 14. Unlike the cps gene cluster of S. pneumoniae serotype14, transcription of this operon may start from cpsIaA, cpsIaE,and orf1 because putative promoter sequences were found in frontof these genes. Northern hybridization, reverse transcription-PCR,and primer extension analyses supported this hypothesis. DNA sequenceanalysis showed that there were two transcriptional terminatorsin the 3' end of this operon (downstream of orf1 and ung). Thefunctions of CpsIaE, CpsIaG, CpsIaI, and CpsIaJ were examinedby glycosyltransferase assay by using the gene products expressedin Escherichia coli JM109 harboring plasmids containing variousS. agalactiae type Ia cps gene fragments. Enzyme assays suggestedthat the gene products of cpsIaE, cpsIaG, cpsIaI, and cpsIaJ areputative 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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