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Journal of Bacteriology, November 2007, p. 7896-7910, Vol. 189, No. 21
0021-9193/07/$08.00+0     doi:10.1128/JB.00726-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Antigen 84, an Effector of Pleiomorphism in Mycobacterium smegmatis{triangledown}

Liem Nguyen,1,2,3 Nicole Scherr,2 John Gatfield,2 Anne Walburger,2 Jean Pieters,2* and Charles J. Thompson2,3*

Department of Molecular Biology and Microbiology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106,1 Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland,2 Life Sciences Centre, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia V6T 1Z3, Canada3

Received 9 May 2007/ Accepted 23 August 2007

While in most rod-shaped bacteria, morphology is based on MreB-like proteins that form an actin-like cytoskeletal scaffold for cell wall biosynthesis, the factors that determine the more flexible rod-like shape in actinobacteria such as Mycobacterium species are unknown. Here we show that a Mycobacterium smegmatis protein homologous to eubacterial DivIVA-like proteins, including M. tuberculosis antigen 84 (Ag84), localized symmetrically to centers of peptidoglycan biosynthesis at the poles and septa. Controlled gene disruption experiments indicated that the gene encoding Ag84, wag31, was essential; when overexpressed, cells became longer and wider, with Ag84 asymmetrically distributed at one pole. Many became grossly enlarged, bowling-pin-shaped cells having up to 80-fold-increased volume. In these cells, Ag84 accumulated predominantly at a bulbous pole that was apparently generated by uncontrolled cell wall expansion. In some cells, Ag84 was associated with exceptional sites of cell wall expansion (buds) that evolved into branches. M. bovis BCG Ag84 was able to form oligomers in vitro, perhaps reflecting its superstructure in vivo. These data suggested a role for Ag84 in cell division and modulating cell shape in pleiomorphic actinobacteria.

* Corresponding author. Mailing address for Charles J. Thompson: Department of Microbiology and Immunology, Life Sciences Centre, University of British Columbia, 2350 Health Sciences Mall, Vancouver, B.C., Canada V6T 1Z3. Phone: 604-822-2501. Fax: 604-822-6041. E-mail: charles.thompson{at}ubc.ca. Mailing address for Jean Pieters: Department of Biochemistry, Biozentrum, University of Basel, 50-70 Klingelbergstrasse, Basel, Switzerland CH4056. Phone: 41 61 267 2151. Fax: 41 61 267 2148. E-mail: Jean.Pieters{at}unibas.ch

{triangledown} Published ahead of print on 31 August 2007.

Journal of Bacteriology, November 2007, p. 7896-7910, Vol. 189, No. 21
0021-9193/07/$08.00+0     doi:10.1128/JB.00726-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hempel, A. M., Wang, S.-b., Letek, M., Gil, J. A., Flardh, K. (2008). Assemblies of DivIVA Mark Sites for Hyphal Branching and Can Establish New Zones of Cell Wall Growth in Streptomyces coelicolor. J. Bacteriol. 190: 7579-7583 [Abstract] [Full Text]  
  • Mistry, B. V., Del Sol, R., Wright, C., Findlay, K., Dyson, P. (2008). FtsW Is a Dispensable Cell Division Protein Required for Z-Ring Stabilization during Sporulation Septation in Streptomyces coelicolor. J. Bacteriol. 190: 5555-5566 [Abstract] [Full Text]  
  • Letek, M., Ordonez, E., Vaquera, J., Margolin, W., Flardh, K., Mateos, L. M., Gil, J. A. (2008). DivIVA Is Required for Polar Growth in the MreB-Lacking Rod-Shaped Actinomycete Corynebacterium glutamicum. J. Bacteriol. 190: 3283-3292 [Abstract] [Full Text]  


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