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Ixodes dammini: salivary anaphylatoxin inactivating activity.
Experimental Parasitology
|October 1, 1986
Summary
Tick saliva from Ixodes dammini contains a carboxypeptidase that inactivates anaphylatoxin and bradykinin. This enzyme may prevent inflammatory responses at the tick bite site.
Area of Science:
- Parasitology
- Biochemistry
- Immunology
Background:
- Anaphylatoxins and bradykinin are potent mediators of inflammation.
- Tick saliva components can modulate host responses during blood feeding.
Purpose of the Study:
- To investigate the biochemical activity of Ixodes dammini tick saliva.
- To determine the effect of tick saliva on anaphylatoxin and bradykinin.
Main Methods:
- Testing tick saliva's effect on guinea pig ileum preparations stimulated with histamine.
- Assessing the impact of saliva on intradermal anaphylatoxin-induced edema in guinea pigs.
- Evaluating saliva's influence on polymorphonuclear leukocyte aggregation.
- Measuring the inactivation of various peptides including bradykinin, angiotensin I, angiotensin II, and substance P.
Main Results:
- Tick saliva abolished anaphylatoxin's effects on guinea pig ileum and local edema.
- Saliva did not affect anaphylatoxin-induced polymorphonuclear leukocyte aggregation.
- Bradykinin and lysil-bradykinin were inactivated by saliva.
- Angiotensin I, angiotensin II, and substance P remained unaffected.
- Amino acid release patterns suggested a carboxypeptidase with specificity for terminal basic amino acids.
Conclusions:
- Ixodes dammini saliva possesses a carboxypeptidase activity.
- This enzyme likely inactivates anaphylatoxin and bradykinin at the tick attachment site.
- This mechanism may contribute to successful tick feeding by modulating host inflammatory responses.