Functional evidence that the Ser-195 residue of staphylococcal exfoliative toxin A is essential for biological activity.
The substitution of the serine 195 residue of staphylococcal exfoliative toxin A by a cysteine residue led to a biologically inactive protein. This result is consistent with the hypothesis that exfoliative toxin A could be a protease or a lipase. However, no protease or lipase activity was detected with the native toxin.
Prévost
G
G
Institut de Bactériologie, Faculté de Médecine, Strasbourg, France.
Rifai
S
S
Chaix
M L
ML
Piémont
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D005083:Exfoliatins / Q000737:chemistry* / Q000235:genetics; D015870:Gene Expression; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011817:Rabbits; D011994:Recombinant Proteins / Q000096:biosynthesis; D012694:Serine / Q000737:chemistry*; D013206:Staphylococcal Scalded Skin Syndrome / Q000378:metabolism; D013211:Staphylococcus aureus / Q000235:genetics*; D013329:Structure-Activity Relationship
D004269:DNA, Bacterial; D005083:Exfoliatins; D011994:Recombinant Proteins; D012694:Serine