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Infection and Immunity, May 2004, p. 2791-2802, Vol. 72, No. 5
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.5.2791-2802.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Proteolytic Processing of the Mycoplasma hyopneumoniae Cilium Adhesin

Steven P. Djordjevic,1 Stuart J. Cordwell,2 Michael A. Djordjevic,3 Jody Wilton,1 and F. Chris Minion4*

New South Wales Agriculture, Elizabeth Macarthur Agricultural Institute, Camden, New South Wales 2570,1 Australian Proteome Analysis Facility, Macquarie University, New South Wales 2109,2 Genomic Interactions Group, Research School of Biological Sciences, Australian National University, Canberra, Australian Capital Territory 2601, Australia,3 Department of Veterinary Microbiology and Preventive Medicine, Iowa State University, Ames, Iowa 500114

Received 28 August 2003/ Returned for modification 15 October 2003/ Accepted 7 January 2004

Mycoplasma hyopneumoniae is an economically significant swine pathogen that colonizes the respiratory ciliated epithelial cells. Cilium adherence is mediated by P97, a surface protein containing a repeating element (R1) that is responsible for binding. Here, we show that the cilium adhesin is proteolytically processed on the surface. Proteomic analysis of strain J proteins identified cleavage products of 22, 28, 66, and 94 kDa. N-terminal sequencing showed that the 66- and 94-kDa proteins possessed identical N termini and that the 66-kDa variant was generated by cleavage of the 28-kDa product from the C terminus. The 22-kDa product represented the N-terminal 195 amino acids of the cilium adhesin preprotein, confirming that the hydrophobic leader signal sequence is not cleaved during translocation across the membrane. Comparative studies of M. hyopneumoniae strain 232 showed that the major cleavage products of the cilium adhesin are similar, although P22 and P28 appear to be processed further in strain 232. Immunoblotting studies using antisera raised against peptide sequences within P22 and P66/P94 indicate that processing is complex, with cleavage occurring at different frequencies within multiple sites, and is strain specific. Immunogold electron microscopy showed that fragments containing the cilium-binding site remained associated with the cell surface whereas cleavage products not containing the R1 element were located elsewhere. Not all secreted proteins undergo multiple cleavage, however, as evidenced by the analysis of the P102 gene product. The ability of M. hyopneumoniae to selectively cleave its secreted proteins provides this pathogen with a remarkable capacity to alter its surface architecture.

* Corresponding author. Mailing address: Department of Veterinary Microbiology and Preventive Medicine, Iowa State University, Ames, IA 50011. Phone: (515) 294-6347. Fax: (515) 294-1401. E-mail: fcminion{at}iastate.edu.

Editor: J. T. Barbieri

Infection and Immunity, May 2004, p. 2791-2802, Vol. 72, No. 5
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.5.2791-2802.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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