GapA and CrmA coexpression is essential for Mycoplasma gallisepticum cytadherence and virulence

L. Papazisi, S. Frasca, M. Gladd, X. Liao, D. Yogev, S. J. Geary*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

84 Scopus citations

Abstract

It was previously demonstrated that avirulent Mycoplasma gallisepticum strain Rhigh (passage 164) is lacking three proteins that are expressed in its virulent progenitor, strain Rlow (passage 15). These proteins were identified as the cytadhesin molecule GapA, the putative cytadhesin-related molecule CrmA, and a component of a high-affinity transporter system, HatA. Complementation of Rhigh with wild-type gapA restored expression in the transformant (GT5) but did not restore the cytadherence phenotype and maintained avirulence in chickens. These results suggested that CrmA might play an essential role in the M. gallisepticum cytadherence process. CrmA is encoded by the second gene in the gapA operon and shares significant sequence homology to the ORF6 gene of Mycoplasma pneumoniae, which has been shown to play an accessory role in the cytadherence process. Complementation of Rhigh with wild-type crmA resulted in the transformant (SDCA) that lacked the cytadherence and virulence phenotype comparable to that found in Rhigh and GT5. In contrast, complementation of Rhigh with the entire wild-type gapA operon resulted in the transformant (GCA1) that restored cytadherence to the level found in wild-type Rlow. In vivo pathogenesis trials revealed that GCA1 had regained virulence, causing airsacculitis in chickens. These results demonstrate that both GapA and CrmA are required for M. gallisepticum cytadherence and pathogenesis.

Original languageAmerican English
Pages (from-to)6839-6845
Number of pages7
JournalInfection and Immunity
Volume70
Issue number12
DOIs
StatePublished - Dec 2002

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