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Journal of Bacteriology, December 2006, p. 8627-8637, Vol. 188, No. 24
0021-9193/06/$08.00+0     doi:10.1128/JB.00978-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Mycoplasma genitalium P140 and P110 Cytadhesins Are Reciprocally Stabilized and Required for Cell Adhesion and Terminal-Organelle Development{triangledown}

Raul Burgos,1 Oscar Q. Pich,1 Mario Ferrer-Navarro,1 Joel B. Baseman,2 Enrique Querol,1 and Jaume Piñol1*

Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain,1 Department of Microbiology and Immunology, The University of Texas Health Science Center at San Antonio, MC 7758, 7703 Floyd Curl Dr., San Antonio, Texas 78229-39002

Received 5 July 2006/ Accepted 26 September 2006

Mycoplasma genitalium is a human pathogen that mediates cell adhesion by a complex structure known as the attachment organelle. This structure is composed of cytadhesins and cytadherence-associated proteins, but few data are available about the specific role of these proteins in M. genitalium cytadherence. We have deleted by homologous recombination the mg191 and mg192 genes from the MgPa operon encoding the P140 and P110 cytadhesins. Molecular characterization of these mutants has revealed a reciprocal posttranslational stabilization between the two proteins. Loss of either P140 or P110 yields a hemadsorption-negative phenotype and correlates with decreased or increased levels of cytoskeleton-related proteins MG386 and DnaK, respectively. Scanning electron microscopy analysis reveals the absolute requirement of P140 and P110 for the proper development of the attachment organelle. The phenotype described for these mutants resembles that of the spontaneous class I and class II cytadherence-negative mutants [G. R. Mernaugh, S. F. Dallo, S. C. Holt, and J. B. Baseman, Clin. Infect. Dis. 17(Suppl. 1):S69-S78, 1993], whose genetic basis remained undetermined until now. Complementation assays and sequencing analysis demonstrate that class I and class II mutants are the consequence of large deletions affecting the mg192 and mg191-mg192 genes, respectively. These deletions originated from single-recombination events involving sequences of the MgPa operon and the MgPa island located immediately downstream. We also demonstrate the translocation of MgPa sequences to a particular MgPa island by double-crossover events. Based on these observations, we propose that in addition to being a source of antigenic variation, MgPa islands could be also involved in a general phase variation mechanism switching on and off, in a reversible or irreversible way, the adhesion properties of M. genitalium.

* Corresponding author. Mailing address: Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain. Phone: 34-93-5811278. Fax: 34-93-5812011. E-mail: jaume.pinyol{at}uab.es.

{triangledown} Published ahead of print on 6 October 2006.

Journal of Bacteriology, December 2006, p. 8627-8637, Vol. 188, No. 24
0021-9193/06/$08.00+0     doi:10.1128/JB.00978-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Sluijter, M., Spuesens, E. B. M., Hartwig, N. G., van Rossum, A. M. C., Vink, C. (2009). The Mycoplasma pneumoniae MPN490 and Mycoplasma genitalium MG339 Genes Encode RecA Homologs That Promote Homologous DNA Strand Exchange. Infect. Immun. 77: 4905-4911 [Abstract] [Full Text]  
  • Pich, O. Q., Burgos, R., Ferrer-Navarro, M., Querol, E., Pinol, J. (2008). Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence. Microbiology 154: 3188-3198 [Abstract] [Full Text]  
  • Burgos, R., Pich, O. Q., Querol, E., Pinol, J. (2007). Functional Analysis of the Mycoplasma genitalium MG312 Protein Reveals a Specific Requirement of the MG312 N-Terminal Domain for Gliding Motility. J. Bacteriol. 189: 7014-7023 [Abstract] [Full Text]  


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