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Infection and Immunity, March 2006, p. 1777-1785, Vol. 74, No. 3
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.3.1777-1785.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Identification of Fibronectin-Binding Proteins in Mycoplasma gallisepticum Strain R

Meghan May,1,2 Leka Papazisi,3 Timothy S. Gorton,1,2 and Steven J. Geary1,2*

Department of Pathobiology and Veterinary Science,1 Center of Excellence for Vaccine Research, The University of Connecticut, 61 North Eagleville Rd., Storrs, Connecticut 06269,2 The Institute for Genomic Research, 9712 Medical Center Dr., Rockville, Maryland 208503

Received 2 November 2005/ Returned for modification 16 November 2005/ Accepted 19 November 2005

We have determined that virulent Mycoplasma gallisepticum strain Rlow is capable of binding the extracellular matrix protein fibronectin. Fibronectin was found to be present in M. gallisepticum Rlow protein extracts by Western blotting and peptide sequencing. Mycoplasma gallisepticum Rhigh, the attenuated, high-passage derivative of Rlow, is deficient in this ability. MGA_1199, the M. gallisepticum homologue of the cytadherence-associated protein P65 from Mycoplasma pneumoniae, and MGA_0928, the M. gallisepticum homologue of the M. pneumoniae cytoskeletal protein HMW3, were identified as fibronectin-binding proteins. Peptides from the regions of MGA_1199 and MGA_0928 exhibiting the highest degree of homology with known fibronectin-binding proteins were shown to bind the gelatin/heparin-binding domain of fibronectin. MGA_1199 and MGA_0928 were shown to be absent and aberrant, respectively, in Rhigh, explaining its lack of fibronectin-binding capability. Consistent with its M. pneumoniae counterpart, MGA_1199 (renamed PlpA) was demonstrated to be surface exposed, despite a lack of classical membrane-spanning domains. Due to its demonstrated topology and the strength of interaction between its binding peptide and fibronectin, we propose that PlpA functions as a fibronectin-binding protein in vivo and may possess atypical transmembrane domains.

* Corresponding author. Mailing address: Department of Pathobiology and Veterinary Science, University of Connecticut, 61 North Eagleville Rd., Storrs, CT 06269. Phone: (860) 486-0835. Fax: (860) 486-2794. E-mail: geary{at}uconnvm.uconn.edu.

Editor: J. T. Barbieri

Infection and Immunity, March 2006, p. 1777-1785, Vol. 74, No. 3
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.3.1777-1785.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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