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By introducing a series of six different substitutions at and around position 9, we investigated the structural requirements of the amino-terminal region of the S1 subunit of pertussis toxin for both enzyme activity and immunoreactivity. All mutant S1 analogs with a substitution at this location exhibited severely decreased ADP-ribosyltransferase activity (range, 400- to 2,500-fold). In contrast, alteration of arginine 58 had considerably less effect. The reactivity of the mutant molecules with monoclonal antibody 1B7 varied with the nature of the substitution. These findings indicate an absolute requirement for the presence of an arginine residue at position 9 for the maintenance of efficient ADP-ribosyltransferase activity and illustrate the specific participation of vicinal residues in the formation of the protective epitope.
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
March 2000,
Infection and immunity,
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
February 1994,
Biochemistry,
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
February 1986,
Journal of general microbiology,
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
October 1990,
The Journal of biological chemistry,
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
March 2002,
Infection and immunity,
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
January 2001,
Cellular microbiology,
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
May 1990,
Journal of immunology (Baltimore, Md. : 1950),
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
March 1989,
Infection and immunity,
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
October 1988,
Proceedings of the National Academy of Sciences of the United States of America,
Y Lobet, and
W Cieplak, and
S G Smith, and
J M Keith
October 1988,
Science (New York, N.Y.),
