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Infection and Immunity, October 2002, p. 5612-5621, Vol. 70, No. 10
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.10.5612-5621.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Characterization of P40, a Cytadhesin of Mycoplasma agalactiae

Bénédicte Fleury,1 Dominique Bergonier,1 Xavier Berthelot,1 Ernst Peterhans,2 Joachim Frey,3* and Edy M. Vilei3

Unité Mixte de Recherche ENVT-INRA 959, École Nationale Vétérinaire de Toulouse, F-31076 Toulouse Cedex 3, France,1 Institute for Veterinary Virology,2 Institute for Veterinary Bacteriology, University of Berne, CH-3012 Berne, Switzerland3

Received 23 May 2002/ Returned for modification 25 June 2002/ Accepted 8 July 2002

An immunodominant protein, P40, of Mycoplasma agalactiae was analyzed genetically and functionally. The gene encoding P40 was cloned from type strain PG2, sequenced, submitted to point mutagenesis in order to convert mycoplasma-specific TGATrp codon to the universal TGGTrp codon, and subsequently expressed in Escherichia coli. Nucleotide sequence-derived amino acid sequence comparisons revealed a similarity of P40 to the adhesin P50 of Mycoplasma hominis and to protein P89 of Spiroplasma citri, which is expected to be involved in adhesion. The amino acid sequence of P40 revealed a recognition site for a signal peptidase and strong antigenic and hydrophilic motifs in the C-terminal domain. Triton X-114 phase partitioning confirmed that P40 is a membrane protein. Fab fragments of antibodies directed against recombinant purified P40 significantly inhibited adherence of M. agalactiae strains PG2 to lamb joint synovial cells LSM 192. Sera taken sequentially from sheep infected with PG2 revealed that P40 induced a strong and persistent immune response that gave strong signals on immunoblots containing recombinant P40 even 3 months after infection. The gene encoding P40 was present in a single copy in all of the 26 field strains of M. agalactiae analyzed and was not detected in closely related mycoplasma species. P40 was expressed as a protein with an apparent molecular mass of 37 kDa on sodium dodecyl sulfate-acrylamide gels by all M. agalactiae strains except for serotype C strains, which showed nonsense mutations in their p40 genes.

* Corresponding author. Mailing address: Institute for Veterinary Bacteriology, University of Berne, Länggass-Strasse 122, CH-3012 Berne, Switzerland. Phone: 41-31-631-2414. Fax: 41-31-631-2634. E-mail: joachim.frey{at}vbi.unibe.ch.

Editor: J. T. Barbieri

Infection and Immunity, October 2002, p. 5612-5621, Vol. 70, No. 10
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.10.5612-5621.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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