This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow An erratum has been published
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Johnson, C.
Right arrow Articles by Baseman, J. B.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Johnson, C.
Right arrow Articles by Baseman, J. B.

 Previous Article  |  Next Article 

Infection and Immunity, October 2009, p. 4362-4370, Vol. 77, No. 10
0019-9567/09/$08.00+0     doi:10.1128/IAI.00044-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Characterization of a Unique ADP-Ribosyltransferase of Mycoplasma penetrans{triangledown}

Coreen Johnson, T. R. Kannan, and Joel B. Baseman*

Department of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, MC 7758, San Antonio, Texas 78229-3900

Received 13 January 2009/ Returned for modification 22 February 2009/ Accepted 25 July 2009

Mycoplasma penetrans is a urogenital tract pathogen implicated in the deterioration of the immune system in human immunodeficiency virus-infected AIDS patients. Here, we describe a 78-kDa protein from M. penetrans, designated MYPE9110, that exhibits sequence similarity to known ADP-ribosyltransferases (ADPRTs) such as Bordetella pertussis pertussis toxin and Mycoplasma pneumoniae community-acquired respiratory distress syndrome toxin. MYPE9110 possesses key amino acid residues found in all ADPRTs that are essential for ADPRT activity. Several mammalian cell proteins are ADP-ribosylated by MYPE9110, and the full-length recombinant protein exhibits a strong auto-ADP-ribosylating activity. In the absence of target proteins, MYPE9110 demonstrates a NAD-glycohydrolase activity by hydrolyzing NAD. Furthermore, this toxin elicits cytopathology in HeLa cells by inducing cytoplasmic vacuolization in the presence of ammonium chloride. The deletion of the C-terminal region of MYPE9110 significantly diminishes its binding to host cells while still exhibiting an ADPRT activity, suggesting that MYPE9110 is a member of the family of A-B ADPRT toxins.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, MC 7758, San Antonio, TX 78229-3900. Phone: (210) 567-3939. Fax: (210) 567-6491. E-mail: baseman{at}uthsca.edu

{triangledown} Published ahead of print on 3 August 2009.

Editor: S. R. Blanke

Infection and Immunity, October 2009, p. 4362-4370, Vol. 77, No. 10
0019-9567/09/$08.00+0     doi:10.1128/IAI.00044-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»