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ProGlyProt ID
Organism Information
Organism Name
Bacillus anthracis str. Ames (Sterne 7702)
Family: Bacillaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI)
Genome Sequence(s)
Organism Additional Information
Bacillus anthracis is a Gram-positive bacterium that forms spores, the causal agent of anthrax. This lethal infection involves both toxaemia and septicaemia.
Gene Information
Gene Name
bclA (BA_1222)
Protein Information
Protein Name
BclA (collagen-like protein)
UniProtKB/SwissProt ID
UniProtKB Sequence
Sequence length
382 AA
Subcellular Location
It is the major glycoprotein of exosporium and also the immunodominant protein of the spore surface. Exosporium is a loose fitting layer enclosing the spore. BclA forms the filaments of the external hair-like nap of the exosporium.
Protein Structure
Glycosylation Status
Glycosylation Type
Information currently not available with us.
Technique(s) used for Glycosylation Detection
ECL Glycoprotein detection kit and chemical deglycosylation using trifluoromethanesulfonic acid (TFMS).
Glycan Information
Glycan Annotation
The protein is extensively O-glycosylated with a 715-Da tetrasaccharide and a 324-Da disaccharide. The tetrasaccharide contains three rhamnose residues and an unusual terminal sugar, 2-O-methyl-4- (3-hydroxy-3-methylbutanamido)-4,6-dideoxy-D-glucopyranose, named anthrose (Ant). The tetrasaccharide has the structure: β-Ant-(1→3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→2)-L-Rhap. Oligosaccharide is attached to the BclA through a GalNAc linker. In its absence, GlcNAc can serve as a substitute linker.
1) Oberli, M.A., Tamborrini, M., Tsai, Y.H., Werz, D.B., Horlacher, T., Adibekian, A., Gauss, D., Moller, H.M., Pluschke, G. and Seeberger, P.H. (2010) Molecular analysis of carbohydrate-antibody interactions: case study using a Bacillus anthracis tetrasaccharide. J Am Chem Soc, 132, 10239-10241. [PubMed: 20614885]
2) Tamborrini, M., Holzer, M., Seeberger, P.H., Schurch, N. and Pluschke, G. (2010) Anthrax spore detection by a luminex assay based on monoclonal antibodies that recognize anthrose-containing oligosaccharides. Clin Vaccine Immunol, 17, 1446-1451. [PubMed: 20660139]
3) Dong, S., Chesnokova, O.N., Turnbough, C.L., Jr. and 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. [PubMed: 19749053]
4) Saksena, R., Adamo, R. and Kovac, P. (2006) Synthesis of the tetrasaccharide side chain of the major glycoprotein of the Bacillus anthracis exosporium. Bioorg Med Chem Lett, 16, 615-617. [PubMed: 16275067]
5) Adamo, R., Saksena, R. and Kovac, P. (2005) Synthesis of the beta anomer of the spacer-equipped tetrasaccharide side chain of the major glycoprotein of the Bacillus anthracis exosporium. Carbohydr Res, 340, 2579-2582. [PubMed: 16216230]
6) Daubenspeck, J.M., Zeng, H., Chen, P., Dong, S., Steichen, C.T., Krishna, N.R., Pritchard, D.G. and Turnbough, C.L., Jr. (2004) Novel oligosaccharide side chains of the collagen-like region of BclA, the major glycoprotein of the Bacillus anthracis exosporium. J Biol Chem, 279, 30945-30953. [PubMed: 15152001]
7) Sylvestre, P., Couture-Tosi, E. and Mock, M. (2002) A collagen-like surface glycoprotein is a structural component of the Bacillus anthracis exosporium. Mol Microbiol, 45, 169-178. [PubMed: 12100557]
Additional Comments
Owing to its absence in related strains of bacteria, anthrose has been regarded as a potential biomarker for anthrax detection.
A hydrophilic collagen-like region (CLR) from 41–250 residue consists of 70 triplet repeats (GXX) including 54 GPT triplet
Year of Identification
Copyright @ 2011 IMTECH
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