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Infection and Immunity, March 2003, p. 1075-1082, Vol. 71, No. 3
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.3.1075-1082.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Production of the Type IV Secretion System Differs among Brucella Species as Revealed with VirB5- and VirB8-Specific Antisera

Bruno Rouot,1* Maria-Teresa Alvarez-Martinez,1 Carine Marius,1 Pierrette Menanteau,2 Laurence Guilloteau,2 Rose-Anne Boigegrain,1 Robert Zumbihl,1,{dagger} David O'Callaghan,1 Natalie Domke,3 and Christian Baron3,4

INSERM U431, Université de Montpellier 2, 34095 Montpellier Cedex 05,1 Laboratoire de Pathologie Infectieuse et Immunologie, INRA, Nouzilly, France,2 Ludwig-Maximilians-Universität, Department Biologie I, Bereich Mikrobiologie, D-80638 Munich, Germany,3 Department of Biology, McMaster University, Hamilton, Ontario LS8 4K1, Canada4

Received 7 August 2002/ Returned for modification 24 September 2002/ Accepted 25 November 2002

Expression of the virB operon, encoding the type IV secretion system required for Brucella suis virulence, occurred in the acidic phagocytic vacuoles of macrophages and could be induced in minimal medium at acidic pH values. To analyze the production of VirB proteins, polyclonal antisera against B. suis VirB5 and VirB8 were generated. Western blot analysis revealed that VirB5 and VirB8 were detected after 3 h in acidic minimal medium and that the amounts increased after prolonged incubation. Unlike what occurs in the related organism Agrobacterium tumefaciens, the periplasmic sugar binding protein ChvE did not contribute to VirB protein production, and B. suis from which chvE was deleted was fully virulent in a mouse model. Comparative analyses of various Brucella species revealed that in all of them VirB protein production increased under acidic conditions. However, in rich medium at neutral pH, Brucella canis and B. suis, as well as the Brucella abortus- and Brucella melitensis-derived vaccine strains S19, RB51, and Rev.1, produced no VirB proteins or only small amounts of VirB proteins, whereas the parental B. abortus and B. melitensis strains constitutively produced VirB5 and VirB8. Thus, the vaccine strains were still able to induce virB expression under acidic conditions, but the VirB protein production was markedly different from that in the wild-type strains at pH 7. Taken together, the data indicate that VirB protein production and probably expression of the virB operon are not uniformly regulated in different Brucella species. Since VirB proteins were shown to modulate Brucella phagocytosis and intracellular trafficking, the differential regulation of the production of these proteins reported here may provide a clue to explain their role(s) during the infection process.

* Corresponding author. Mailing address: CNRS UMR 5539, Université Montpellier 2, CC 107, 34095 Montpellier Cedex 05, France. Phone: 33 467 144 726. Fax: 33 467 144 927. E-mail: rouot{at}crit.univ-montp2.fr.

Editor: D. L. Burns

{dagger} Present address: R.Z., EMIP, Unit INRA 1133, CC101, Université Montpellier 2, Montpellier Cedex, France.

Infection and Immunity, March 2003, p. 1075-1082, Vol. 71, No. 3
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.3.1075-1082.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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