Strongyloides spp.: demonstration and partial characterization of acidic collagenolytic activity from infective larvae.
Infective larvae of Strongyloides spp. have been shown to contain azocollytic enzymes which may aid in host skin penetration. Attempts to demonstrate classical, neutral pH-active collagenase activity in Strongyloides ratti were unsuccessful. In the current study, we investigated the presence of acidic collagenolytic activity in the infective larvae of Strongyloides ransomi, S. ratti, and S. stercoralis. All three species demonstrated collagenolytic activity in acidic homogenates as well as in neutral freeze-thaw fractions. Biochemical characterization of this collagenolytic activity from S. ratti and S. ransomi indicated that it was active over an acidic pH range, although it was stable at a neutral pH. This, along with molecular weight estimates and inhibitor susceptibilities, suggested that the collagenolytic activity was similar to vertebrate acidic cysteinyl proteinases. These studies also indicated that this activity is similar to the acidic cysteinyl proteinases in extracts of S. ransomi.
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Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030.
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D000818:Animals; D003094:Collagen / Q000378:metabolism; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007814:Larva; D003012:Microbial Collagenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D013321:Strongyloides / Q000201:enzymology*; D013552:Swine
D003094:Collagen; D003012:Microbial Collagenase