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Journal of Bacteriology, April 2008, p. 2350-2359, Vol. 190, No. 7
0021-9193/08/$08.00+0     doi:10.1128/JB.01899-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Anthrose Biosynthetic Operon of Bacillus anthracis{triangledown}

Shengli Dong,1 Sylvia A. McPherson,2 Li Tan,2 Olga N. Chesnokova,2 Charles L. Turnbough Jr.,2* and David G. Pritchard1*

Department of Biochemistry and Molecular Genetics,1 Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294-21702

Received 4 December 2007/ Accepted 17 January 2008

The exosporium of Bacillus anthracis spores consists of a basal layer and an external hair-like nap. The nap is composed primarily of the glycoprotein BclA, which contains a collagen-like region with multiple copies of a pentasaccharide side chain. This oligosaccharide possesses an unusual terminal sugar called anthrose, followed by three rhamnose residues and a protein-bound N-acetylgalactosamine. Based on the structure of anthrose, we proposed an enzymatic pathway for its biosynthesis. Examination of the B. anthracis genome revealed six contiguous genes that could encode the predicted anthrose biosynthetic enzymes. These genes are transcribed in the same direction and appear to form two operons. We introduced mutations into the B. anthracis chromosome that either delete the promoter of the putative upstream, four-gene operon or delete selected genes in both putative operons. Spores produced by strains carrying mutations in the upstream operon completely lacked or contained much less anthrose, indicating that this operon is required for anthrose biosynthesis. In contrast, inactivation of the downstream, two-gene operon did not alter anthrose content. Additional experiments confirmed the organization of the anthrose operon and indicated that it is transcribed from a {sigma}E-specific promoter. Finally, we demonstrated that anthrose biosynthesis is not restricted to B. anthracis as previously suggested.

* Corresponding author. Mailing address for D. G. Pritchard: University of Alabama at Birmingham, Department of Biochemistry and Molecular Genetics, MCLM 552, 1530 3rd Ave. S, Birmingham, AL 35294-2170. Phone: (205) 934-6023. Fax: (205) 934-6022. E-mail: Davidp1{at}uab.edu. Mailing address for C. L. Turnbough, Jr.: University of Alabama at Birmingham, Department of Microbiology, BBRB 409, 1530 3rd Ave. S, Birmingham, AL 35294-2170. Phone: (205) 934-6289. Fax: (205) 975-5479. E-mail: chuckt{at}uab.edu

{triangledown} Published ahead of print on 1 February 2008.

Journal of Bacteriology, April 2008, p. 2350-2359, Vol. 190, No. 7
0021-9193/08/$08.00+0     doi:10.1128/JB.01899-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Dong, S., Chesnokova, O. N., Turnbough, C. L. Jr., Pritchard, D. G. (2009). Identification of the UDP-N-Acetylglucosamine 4-Epimerase Involved in Exosporium Protein Glycosylation in Bacillus anthracis. J. Bacteriol. 191: 7094-7101 [Abstract] [Full Text]  
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