Specific peptides of casein pancreatic digestion enhance the production of tetanus toxin.
Casein pancreatic digest is the basic bacterial growth medium used for diphtheria, botulinum and tetanus toxin vaccine production. It is known that the variation in the peptide content of the casein digest directly affects final toxin yields. In this study, the identification and sequences of eight peptides, four to eight amino acids in length, of casein pancreatic digestion, which seem to be involved in the enhancement of tetanus toxin production, are described. They all contain one or two residues of proline/molecule and a predominance of hydrophobic amino acid residues. The most active peptides show a general structure of Pro-aromatic-Pro, and this pattern resembled the motif displayed by bradykinin-potentiating peptides found in snake venoms. By analogy with the mechanism of bradykinin potentiation through inhibition of the proteolytic degradation of bradykinin, it is suggested that the six peptides identified here could protect the tetanus toxin from proteolysis, once secreted by the bacteria.
Porfírio
Z
Z
Biochemistry and Biophysics Laboratory, Instituto Butantan, São Paulo, Brazil.
Prado
S M
SM
Vancetto
M D
MD
Fratelli
F
F
Alves
E W
EW
Raw
I
I
Fernandes
B L
BL
Camargo
A C
AC
Lebrun
I
I
D000818:Animals; D002364:Caseins / Q000494:pharmacology*; D005260:Female; D008297:Male; D051379:Mice; D010446:Peptide Fragments / Q000494:pharmacology*; D013744:Tetanus Toxin / Q000096:biosynthesis*
D002364:Caseins; D010446:Peptide Fragments; D013744:Tetanus Toxin