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Infect. Immun., 05 1996, 1720-1723, Vol 64, No. 5
Copyright © 1996, American Society for Microbiology

ADP-ribosylation of an approximately 70-kilodalton protein of Klebsiella pneumoniae

U Geipel, I Just and K Aktories
Abteilung Bakteriologie und Hygiene, Institut fur Medizinische Mikrobiologie und Hygiene, Homburg/Saar, Germany

An approximately 70-kDa protein in the culture supernatant of a human pathogenic strain of Klebsiella pneumoniae was labeled in the presence of [32P-adenylate]NAD. Labeling was significantly increased by the addition of dithiothreitol ( > 1 mM) but prevented by treatment of the culture supernatant for 3 min at 56 degrees C. The addition of unlabeled NAD, but not of ADP-ribose, blocked labeling of the approximately 70-kDa protein. The radioactive label was released by formic acid but not by HgCl2 (1 mM) or neutral hydroxylamine (0.5 M). The addition of homogenates of human platelets, human neutrophils, rat brain, rat lung, or rat spleen tissues to the culture supernatant did not induce labeling of eukaryotic proteins. The data indicate that the K. pneumoniae strain produces ADP-ribosyltransferase which modifies an endogenous protein.