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Infection and Immunity, May 2000, p. 2954-2961, Vol. 68, No. 5
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Characterization of Heat, Oxidative, and Acid Stress Responses in Brucella melitensis

Ana P. Teixeira-Gomes,* Axel Cloeckaert, and Michel S. Zygmunt

Laboratoire de Pathologie Infectieuse et Immunologie, Institut National de la Recherche Agronomique, Centre de Recherches de Tours, 37380 Nouzilly, France

Received 17 September 1999/Returned for modification 17 November 1999/Accepted 20 January 2000

Brucella melitensis is a facultative intracellular pathogen which is able to survive and replicate within phagocytic cells. Therefore, it has to adapt to a range of different hostile environments. In order to understand the mechanisms of intracellular survival employed by virulent B. melitensis 16M, an initial approach consisting of analysis of the differences in patterns of protein synthesis in response to heat, oxidative, and acid pH stresses by two-dimensional (2-D) polyacrylamide gel electrophoresis was used. Depending on the stress, this involved about 6.4 to 12% of the 676 protein spots detected in 2-D gel electrophoresis. On the basis of N-terminal sequence analysis and database searching, 19 proteins whose level of synthesis was up- or down-regulated by stress conditions were identified. Some of them were previously reported for Brucella, such as BvrR, DnaK, GroEL, and Cu-Zn superoxide dismutase (SOD). Eight other proteins closely matched proteins found in other bacteria: AapJ, alpha-ETF, ClpP, Fe and/or Mn SOD, malate dehydrogenase, IalB, 30S ribosomal protein S1, and pyruvate dehydrogenase E1 component beta subunit. Results indicated that B. melitensis could bring specific regulatory mechanisms into play in response to stress conditions. For example, the ribosome releasing factor in B. melitensis appeared to be a heat shock protein, whereas the ClpP protein, described as a heat shock protein for Escherichia coli, was strongly down-regulated in B. melitensis in response to heat stress. Some of the identified proteins and their potential specific regulation could be required for the adaptation of B. melitensis to environmental stresses encountered in phagocytic cells and possibly for bacterial virulence.

* Corresponding author. Mailing address: Laboratoire de Pathologie Infectieuse et Immunologie, INRA, Centre de Recherches de Tours, 37380 Nouzilly, France. Phone: (33) 2 47 42 78 67. Fax: (33) 2 47 42 77 79. E-mail: Ana-Paula.Teixeira{at}tours.inra.fr.

Infection and Immunity, May 2000, p. 2954-2961, Vol. 68, No. 5
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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