Inhibition of class II major histocompatibility complex antigen processing by Escherichia coli heat-labile enterotoxin requires an enzymatically active A subunit.
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.
Matousek
M P
MP
Department of Pathology, Case Western Reserve University, Cleveland, Ohio 44106, USA.
Nedrud
J G
JG
Cieplak
W
W
Harding
C V
CV
D000818:Animals; D017951:Antigen Presentation / Q000187:drug effects*; D001427:Bacterial Toxins / Q000633:toxicity*; D002772:Cholera Toxin / Q000633:toxicity; D000242:Cyclic AMP / Q000032:analysis; D004768:Enterotoxins / Q000633:toxicity*; D004926:Escherichia coli / Q000472:pathogenicity*; D029968:Escherichia coli Proteins; D000949:Histocompatibility Antigens Class II / Q000378:metabolism*; D051379:Mice; D008808:Mice, Inbred CBA; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism
D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D000949:Histocompatibility Antigens Class II; D002772:Cholera Toxin; C027538:heat-labile enterotoxin, E coli; D000242:Cyclic AMP; D011065:Poly(ADP-ribose) Polymerases