Infect Immun, July 1998, p. 3480-3484, Vol. 66, No. 7
Department of Pathology, Case Western Reserve
University, Cleveland, Ohio 44106,1 and
Rocky Mountain Laboratories, NIAID, National Institutes of
Health, Hamilton, Montana 598402
Received 7 November 1997/Returned for modification 23 December
1997/Accepted 24 March 1998
Escherichia coli heat-labile enterotoxin (LT) and
cholera toxin (CT) were found to inhibit intracellular antigen
processing. Processing was not inhibited by mutant LT with attenuated
ADP-ribosyltransferase activity, CT B or LT B subunit, which enhanced
presentation of preexisting cell surface peptide-class II major
histocompatibility complex complexes. Inhibition of antigen processing
correlated with A subunit ADP-ribosyltransferase activity.
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Inhibition of Class II Major Histocompatibility
Complex Antigen Processing by Escherichia coli Heat-Labile
Enterotoxin Requires an Enzymatically Active A Subunit
and
*
Corresponding author. Mailing address: Institute of
Pathology, Case Western Reserve University, 2085 Adelbert Rd.,
Cleveland, OH 44106. Phone: (216) 368-4711. Fax: (216) 368-0495. E-mail: cvh3{at}po.cwru.edu.
Present address: Antigen Discovery and Evaluation, RIBI Immunochem
Research, Hamilton, MT 59840.
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