Activity of Lymphostatin, A Lymphocyte Inhibitory Virulence Factor of Pathogenic Escherichia coli, is Dependent on a Cysteine Protease Motif.

This increase in ED 50 was highly significant across five donors ( P = 0.0097) and was comparable to that seen previously for lymphostatin with a substitution of three alanine residues for a DTD motif in the glycosyltransferase domain (rLifA DTD-AAA ). 12 Our data indicate that the cysteine protease motif is required for the ability of lymphostatin to block mitogen-activated proliferation of bovine T cells, without obvious alteration of its secondary or tertiary structure.

also in 132,142 other papers