This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Steichen, C. T.
Right arrow Articles by Turnbough, C. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Steichen, C. T.
Right arrow Articles by Turnbough, C. L., Jr

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2005, p. 5868-5876, Vol. 187, No. 17
0021-9193/05/$08.00+0     doi:10.1128/JB.187.17.5868-5876.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characterization of the Exosporium Basal Layer Protein BxpB of Bacillus anthracis

Christopher T. Steichen, John F. Kearney, and Charles L. Turnbough Jr*

Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294

Received 30 April 2005/ Accepted 3 June 2005

Bacillus anthracis spores, the cause of anthrax, are enclosed by a prominent loose-fitting structure called the exosporium. The exosporium is composed of a basal layer and an external hair-like nap. The filaments of the hair-like nap are apparently formed by a single collagen-like glycoprotein called BclA, whereas several different proteins form or are tightly associated with the basal layer. In this study, we used immunogold electron microscopy to demonstrate that BxpB (also called ExsF) is a component of the exosporium basal layer. Binding to the basal layer by an anti-BxpB monoclonal antibody was greatly increased by the loss of BclA. We found that BxpB and BclA are part of a stable complex that appears to include the putative basal layer protein ExsY and possibly other proteins. Previous results suggested that BxpB was glycosylated; however, our results indicate that it is not a glycoprotein. We showed that {Delta}bxpB spores, which lack BxpB, contain an exosporium devoid of hair-like nap even though the {Delta}bxpB strain produces normal levels of BclA. These results indicated that BxpB is required for the attachment of BclA to the exosporium. Finally, we found that the efficiency of production of {Delta}bxpB spores and their resistance properties were similar to those of wild-type spores. However, {Delta}bxpB spores germinate faster than wild-type spores, indicating that BxpB suppresses germination. This effect did not appear to be related to the absence from {Delta}bxpB spores of a hair-like nap or of enzymes that degrade germinants.

* Corresponding author. Mailing address: UAB 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.

Journal of Bacteriology, September 2005, p. 5868-5876, Vol. 187, No. 17
0021-9193/05/$08.00+0     doi:10.1128/JB.187.17.5868-5876.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Giorno, R., Mallozzi, M., Bozue, J., Moody, K.-S., Slack, A., Qiu, D., Wang, R., Friedlander, A., Welkos, S., Driks, A. (2009). Localization and assembly of proteins comprising the outer structures of the Bacillus anthracis spore. Microbiology 155: 1133-1145 [Abstract] [Full Text]  
  • Chesnokova, O. N., McPherson, S. A., Steichen, C. T., Turnbough, C. L. Jr. (2009). The Spore-Specific Alanine Racemase of Bacillus anthracis and Its Role in Suppressing Germination during Spore Development. J. Bacteriol. 191: 1303-1310 [Abstract] [Full Text]  
  • Lisanby, M. W., Swiecki, M. K., Dizon, B. L. P., Pflughoeft, K. J., Koehler, T. M., Kearney, J. F. (2008). Cathelicidin Administration Protects Mice from Bacillus anthracis Spore Challenge. J. Immunol. 181: 4989-5000 [Abstract] [Full Text]  
  • Liang, L., He, X., Liu, G., Tan, H. (2008). The role of a purine-specific nucleoside hydrolase in spore germination of Bacillus thuringiensis. Microbiology 154: 1333-1340 [Abstract] [Full Text]  
  • Dong, S., McPherson, S. A., Tan, L., Chesnokova, O. N., Turnbough, C. L. Jr., Pritchard, D. G. (2008). Anthrose Biosynthetic Operon of Bacillus anthracis. J. Bacteriol. 190: 2350-2359 [Abstract] [Full Text]  
  • Cote, C. K., Bozue, J., Moody, K. L., DiMezzo, T. L., Chapman, C. E., Welkos, S. L. (2008). Analysis of a novel spore antigen in Bacillus anthracis that contributes to spore opsonization. Microbiology 154: 619-632 [Abstract] [Full Text]  
  • Brahmbhatt, T. N., Darnell, S. C., Carvalho, H. M., Sanz, P., Kang, T. J., Bull, R. L., Rasmussen, S. B., Cross, A. S., O'Brien, A. D. (2007). Recombinant Exosporium Protein BclA of Bacillus anthracis Is Effective as a Booster for Mice Primed with Suboptimal Amounts of Protective Antigen. Infect. Immun. 75: 5240-5247 [Abstract] [Full Text]  
  • Thompson, B. M., Waller, L. N., Fox, K. F., Fox, A., Stewart, G. C. (2007). The BclB Glycoprotein of Bacillus anthracis Is Involved in Exosporium Integrity. J. Bacteriol. 189: 6704-6713 [Abstract] [Full Text]  
  • Bozue, J., Moody, K. L., Cote, C. K., Stiles, B. G., Friedlander, A. M., Welkos, S. L., Hale, M. L. (2007). Bacillus anthracis Spores of the bclA Mutant Exhibit Increased Adherence to Epithelial Cells, Fibroblasts, and Endothelial Cells but Not to Macrophages. Infect. Immun. 75: 4498-4505 [Abstract] [Full Text]  
  • Basu, S., Kang, T. J., Chen, W. H., Fenton, M. J., Baillie, L., Hibbs, S., Cross, A. S. (2007). Role of Bacillus anthracis Spore Structures in Macrophage Cytokine Responses. Infect. Immun. 75: 2351-2358 [Abstract] [Full Text]  
  • Bozue, J., Cote, C. K., Moody, K. L., Welkos, S. L. (2007). Fully Virulent Bacillus anthracis Does Not Require the Immunodominant Protein BclA for Pathogenesis. Infect. Immun. 75: 508-511 [Abstract] [Full Text]  
  • Johnson, M. J., Todd, S. J., Ball, D. A., Shepherd, A. M., Sylvestre, P., Moir, A. (2006). ExsY and CotY Are Required for the Correct Assembly of the Exosporium and Spore Coat of Bacillus cereus. J. Bacteriol. 188: 7905-7913 [Abstract] [Full Text]  
  • Boydston, J. A., Yue, L., Kearney, J. F., Turnbough, C. L. Jr. (2006). The ExsY Protein Is Required for Complete Formation of the Exosporium of Bacillus anthracis. J. Bacteriol. 188: 7440-7448 [Abstract] [Full Text]  
  • Swiecki, M. K., Lisanby, M. W., Shu, F., Turnbough, C. L. Jr, Kearney, J. F. (2006). Monoclonal Antibodies for Bacillus anthracis Spore Detection and Functional Analyses of Spore Germination and Outgrowth. J. Immunol. 176: 6076-6084 [Abstract] [Full Text]  
  • Keim, P., Mock, M., Young, J., Koehler, T. M. (2006). The International Bacillus anthracis, B. cereus, and B. thuringiensis Conference, "Bacillus-ACT05".. J. Bacteriol. 188: 3433-3441 [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»