Journal
MOLECULAR MICROBIOLOGY
Volume 93, Issue 3, Pages 568-581Publisher
WILEY
DOI: 10.1111/mmi.12680
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Funding
- National Institute of Allergy and Infectious Diseases [U19AI070412]
- Kleberg Foundation
- Robert A. Welch Foundation [AQ-1399]
- National Center for Research Resources at the National Institute of Health [RR-15301]
- US Department of Energy, Office of Basic Energy Sciences [W-31-109-ENG-38]
- Cancer Therapy & Research Center (CTRC) Cancer Center Support Grant [NCI P30CA054174]
- UTHSCSA Executive Research Committee
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Community-acquired respiratory distress syndrome (CARDS) toxin from Mycoplasma pneumoniae is a 591-amino-acid virulence factor with ADP-ribosyltransferase (ADPRT) and vacuolating activities. It is expressed at low levels during in vitro growth and at high levels during colonization of the lung. Exposure of experimental animals to purified recombinant CARDS toxin alone is sufficient to recapitulate the cytopathology and inflammatory responses associated with M. pneumoniae infection in humans and animals. Here, by molecular modelling, serial truncations and site-directed mutagenesis, we show that the N-terminal region is essential for ADP-ribosylating activity. Also, by systematic truncation and limited proteolysis experiments we identified a portion of the C-terminal region that mediates toxin binding to mammalian cell surfaces and subsequent internalization. In addition, the C-terminal region alone induces vacuolization in a manner similar to full-length toxin. Together, these data suggest that CARDS toxin has a unique architecture with functionally separable N-terminal and C-terminal domains.
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