Pertussis Toxin, A Protomer

Pertussis Toxin, A Protomer is the enzymatic component of the holotoxin. It has both NAD-glycohydrolase and ADP-ribosyltransferase activities. Pertussis Toxin, A Protomer inhibits neutrophil-mediated inflammation through its ADP-ribosylation activity, however, it is unable to infiltrate cells in the absence of the B oligomer.

Références

1. Kaslow, H R., et al., 1989. Alkylation of cysteine 41, but not cysteine 200, decreases the ADP-ribosyltransferase activity of the S1 subunit of pertussis toxin. The Journal of biological chemistry. 264(11): 6386-90. PMID: 2703495
2. Gill, D M., et al., 1988. ADP-ribosylation of membrane proteins by bacterial toxins in the presence of NAD glycohydrolase. Biochimica et biophysica acta. 954(1): 65-72. PMID: 2833927
3. Burns, D L., et al., 1986. Adenine nucleotides promote dissociation of pertussis toxin subunits. The Journal of biological chemistry. 261(9): 4324-7. PMID: 3005329
4. Tamura, M., et al., 1982. Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model. Biochemistry. 21(22): 5516-22. PMID: 6293544
5. Moss, J., et al., 1983. Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (islet-activating protein). The Journal of biological chemistry. 258(19): 11879-82. PMID: 6311827
6. Brito, G A., et al., 1997. Role of pertussis toxin A subunit in neutrophil migration and vascular permeability. Infection and immunity. 65(3): 1114-8. PMID: 9038326