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Journal of Bacteriology, February 2003, p. 1443-1454, Vol. 185, No. 4
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.4.1443-1454.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Proteomic Analysis of the Spore Coats of Bacillus subtilis and Bacillus anthracis

Erh-Min Lai,1,{dagger} Nikhil D. Phadke,1,{ddagger} Maureen T. Kachman,2 Rebecca Giorno,3 Santiago Vazquez,2 Jenny A. Vazquez,2 Janine R. Maddock,1* and Adam Driks3

Department of Molecular, Cellular and Developmental Biology, University of Michigan,1 Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109 ,2 Department of Microbiology and Immunology, Loyola University Medical Center, Maywood, Illinois 601533

Received 9 August 2002/ Accepted 21 November 2002

The outermost proteinaceous layer of bacterial spores, called the coat, is critical for spore survival, germination, and, for pathogenic spores, disease. To identify novel spore coat proteins, we have carried out a preliminary proteomic analysis of Bacillus subtilis and Bacillus anthracis spores, using a combination of standard sodium dodecyl sulfate-polyacrylamide gel electrophoresis separation and improved two-dimensional electrophoretic separations, followed by matrix-assisted laser desorption ionization-time of flight and/or dual mass spectrometry. We identified 38 B. subtilis spore proteins, 12 of which are known coat proteins. We propose that, of the novel proteins, YtaA, YvdP, and YnzH are bona fide coat proteins, and we have renamed them CotI, CotQ, and CotU, respectively. In addition, we initiated a study of coat proteins in B. anthracis and identified 11 spore proteins, 6 of which are candidate coat or exosporium proteins. We also queried the unfinished B. anthracis genome for potential coat proteins. Our analysis suggests that the B. subtilis and B. anthracis coats have roughly similar numbers of proteins and that a core group of coat protein species is shared between these organisms, including the major morphogenetic proteins. Nonetheless, a significant number of coat proteins are probably unique to each species. These results should accelerate efforts to develop B. anthracis detection methods and understand the ecological role of the coat.

* Corresponding author. Mailing address: Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109. Phone: (734) 936-8068. Fax: (734) 647-0884. E-mail: maddock{at}umich.edu.

{dagger} Present address: Institute of Botany, Academia Sinica, Nankang, Taipei, Taiwan 115.

{ddagger} Present address: Handylab Inc., Ann Arbor, MI 48108.

Journal of Bacteriology, February 2003, p. 1443-1454, Vol. 185, No. 4
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.4.1443-1454.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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