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Journal of Bacteriology, October 2005, p. 6824-6831, Vol. 187, No. 19
0021-9193/05/$08.00+0     doi:10.1128/JB.187.19.6824-6831.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Metabolic Enzyme as a Primary Virulence Factor of Mycoplasma mycoides subsp. mycoides Small Colony

Paola Pilo,1,{dagger} Edy M. Vilei,1 Ernst Peterhans,2 Laetitia Bonvin-Klotz,3 Michael H. Stoffel,3 Dirk Dobbelaere,4 and Joachim Frey1*

Institute of Veterinary Bacteriology,1 Institute of Veterinary Virology,2 Department of Veterinary Anatomy,3 Institute of Animal Pathology, University of Bern, Länggass-Strasse 122, 3001 Bern, Switzerland4

Received 21 April 2005/ Accepted 5 July 2005

During evolution, pathogenic bacteria have developed complex interactions with their hosts. This has frequently involved the acquisition of virulence factors on pathogenicity islands, plasmids, transposons, or prophages, allowing them to colonize, survive, and replicate within the host. In contrast, Mycoplasma species, the smallest self-replicating organisms, have regressively evolved from gram-positive bacteria by reduction of the genome to a minimal size, with the consequence that they have economized their genetic resources. Hence, pathogenic Mycoplasma species lack typical primary virulence factors such as toxins, cytolysins, and invasins. Consequently, little is known how pathogenic Mycoplasma species cause host cell damage, inflammation, and disease. Here we identify a novel primary virulence determinant in Mycoplasma mycoides subsp. mycoides Small Colony (SC), which causes host cell injury. This virulence factor, released in significant amounts in the presence of glycerol in the growth medium, consists of toxic by-products such as H2O2 formed by L-{alpha}-glycerophosphate oxidase (GlpO), a membrane-located enzyme that is involved in the metabolism of glycerol. When embryonic calf nasal epithelial cells are infected with M. mycoides subsp. mycoides SC in the presence of physiological amounts of glycerol, H2O2 is released inside the cells prior to cell death. This process can be inhibited with monospecific anti-GlpO antibodies.

* Corresponding author. Mailing address: Institute of Veterinary Bacteriology, University of Bern, Länggass-Strasse 122, 3001 Bern, Switzerland. Phone: 41 31 631 2414. Fax: 41 31 631 2634. E-mail: joachim.frey{at}vbi.unibe.ch.

{dagger} Present address: Department of Microbiology, Columbia University, 701 West 168th St., New York, NY 10032.

Journal of Bacteriology, October 2005, p. 6824-6831, Vol. 187, No. 19
0021-9193/05/$08.00+0     doi:10.1128/JB.187.19.6824-6831.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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