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Infection and Immunity, July 2000, p. 3956-3964, Vol. 68, No. 7
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Molecular Characterization of the Mycoplasma gallisepticum pvpA Gene Which Encodes a Putative Variable Cytadhesin Protein

S. Boguslavsky,1 D. Menaker,1 I. Lysnyansky,1 T. Liu,2 S. Levisohn,3 R. Rosengarten,4 M. García,2 and D. Yogev1,*

Department of Membrane and Ultrastructure Research, The Hebrew University-Hadassah Medical School, Jerusalem 91120,1 and Division of Avian and Aquatic Diseases, Kimron Veterinary Institute, Bet Dagan 50250,3 Israel; Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, Georgia 306022; and Institute for Bacteriology, Mycology and Hygiene, Vienna University of Veterinary Medicine, A-1210 Vienna, Austria4

Received 24 January 2000/Returned for modification 13 March 2000/Accepted 24 April 2000

A putative cytadhesin-related protein (PvpA) undergoing variation in its expression was identified in the avian pathogen Mycoplasma gallisepticum. The pvpA gene was cloned, expressed in Escherichia coli, and sequenced. It exhibits 54 and 52% homology with the P30 and P32 cytadhesin proteins of the human pathogens Mycoplasma pneumoniae and Mycoplasma genitalium, respectively. In addition, 50% homology was found with the MGC2 cytadhesin of M. gallisepticum and 49% homology was found with a stretch of 205 amino acids of the cytadherence accessory protein HMW3 of M. pneumoniae. The PvpA molecule possesses a proline-rich carboxy-terminal region (28%) containing two identical directly repeated sequences of 52 amino acids and a tetrapeptide motif (Pro-Arg-Pro-X) which is repeated 14 times. Genetic analysis of several clonal isolates representing different expression states of the PvpA product ruled out chromosomal rearrangement as the mechanism for PvpA phase variation. The molecular basis of PvpA variation was revealed in a short tract of repeated GAA codons, encoding five successive glutamate resides, located in the N-terminal region and subject to frequent mutation generating an in-frame UAA stop codon. Size variation of the PvpA protein was observed among M. gallisepticum strains, ranging from 48 to 55 kDa and caused by several types of deletions occurring at the PvpA C-terminal end and within the two directly repeated sequences. By immunoelectron microscopy, the PvpA protein was localized on the mycoplasma cell surface, in particular on the terminal tip structure. Collectively, these findings suggest that PvpA is a newly identified variable surface cytadhesin protein of M. gallisepticum.

* Corresponding author. Mailing address: Department of Membrane and Ultrastructure Research, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel. Phone: 972-2-6758176. Fax: 972-2-6784010. E-mail: yogev{at}cc.huji.ac.il.

Infection and Immunity, July 2000, p. 3956-3964, Vol. 68, No. 7
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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