Back to Search
Start Over
The Schistosomatium douthitti cercarial elastase is biochemically and structurally distinct from that of Schistosoma mansoni
- Source :
- Molecular and biochemical parasitology. 28(2)
- Publication Year :
- 1988
-
Abstract
- The cercarial acetabular gland proteinase of Schistosomatium douthitti, an agent of ‘swimmer's itch’, has been identified and characterized. Like the corresponding proteinase of Schistosoma mansoni, it has significant elastase activity and can degrade a model of dermal extracellular matrix. However, unlike the S. mansoni enzyme, it has a higher molecular weight (50 000 versus 30 000), is of a different proteinase class (metallo versus serine), and has no significant primary structure homology to the S. mansoni proteinase. While these findings indicate that the failure of S. douthitti to produce chronic schistosomiasis in humans is not due to its lacking, or having a less potent ‘penetration proteinase’ than S. mansoni, the proteolytic enzymes are sufficiently different to support the hypothesis that the Schistosomatium line diverged quite early from the main branch of Schistosoma evolution.
- Subjects :
- medicine.medical_treatment
Schistosomiasis
Microbiology
Serine
chemistry.chemical_compound
Calcium Chloride
Schistosomatidae
parasitic diseases
medicine
Animals
Molecular Biology
Schistosoma
Protease
biology
Pancreatic Elastase
Elastase
Proteolytic enzymes
Nucleic Acid Hybridization
Schistosoma mansoni
Hydrogen-Ion Concentration
biology.organism_classification
medicine.disease
Virology
Extracellular Matrix
chemistry
RNA
Parasitology
PMSF
Subjects
Details
- ISSN :
- 01666851
- Volume :
- 28
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Molecular and biochemical parasitology
- Accession number :
- edsair.doi.dedup.....e3853e3ef8409585821af14684775319