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Infection and Immunity, April 2000, p. 1787-1795, Vol. 68, No. 4
Research Institute, Division of Structural
Biology and Biochemistry, The Hospital for Sick Children and the
University of Toronto, Toronto, Ontario,
Canada,1 and Connecticut Children's
Medical Center, Division of Digestive Diseases and Nutrition, Hartford,
Connecticut2
Received 9 September 1999/Returned for modification 18 November
1999/Accepted 22 December 1999
Although the Burkholderia cepacia complex consists of
several genomovars, one highly transmissible strain of B. cepacia has been isolated from the sputa of cystic fibrosis (CF)
patients throughout the United Kingdom and Canada. This strain
expresses surface cable (Cbl) pili and is thought to be the major
strain associated with the fatal "cepacia syndrome." In the present
report we characterize the specific 55-kDa buccal epithelial cell (BEC) protein that binds cable pilus-positive B. cepacia.
N-terminal sequences of CNBr-generated internal peptides identified the
protein as cytokeratin 13 (CK13). Western blots of BEC extracts probed with a specific monoclonal antibody to CK13 confirmed the
identification. Mixed epidermal cytokeratins (which contain CK13),
cytokeratin extract from BEC (which consists essentially of CK13 and
CK4), and a polyclonal antibody to mixed cytokeratins inhibited
B. cepacia binding to CK13 blots and to normal human
bronchial epithelial (NHBE) cells. Preabsorption of the antikeratin
antibody with the BEC cytokeratin fraction reversed the inhibitory
effect of the antibody. A cytokeratin mixture lacking CK13 was
ineffective as an inhibitor of binding. Colocalization of CK13 and
B. cepacia by confocal microscopy demonstrated that intact
nonpermeabilized NHBE cells express small amounts of surface CK13 and
bind Cbl-positive B. cepacia in the same location. Binding
to intact NHBE cells was dependent on bacterial concentration and was
saturable, whereas a Cbl-negative isolate exhibited negligible binding.
These findings raise the possibility that surface-accessible CK13 in
respiratory epithelia may be a biologically relevant target for the
binding of cable piliated B. cepacia.
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Cable-Piliated Burkholderia cepacia
Binds to Cytokeratin 13 of Epithelial Cells
*
Corresponding author. Mailing address: Division of
Structural Biology and Biochemistry, The Hospital for Sick Children,
555 University Ave., Toronto, Ontario, Canada M5G 1X8. Phone: (416) 813-5746. Fax: (416) 813-5022. E-mail:
jfforst{at}sickkids.on.ca.
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