Classes and crossreactivity of proteinases in the excretory-secretory products of Caenorhabditis elegans.
Abstract: Proteinases released during the in vitro maintenance of asynchronous cultures of the free-living nematode Caenorhabditis elegans were characterized on the basis of subunit composition, fluorogenic substrate specificity, inhibitor sensitivity and pH optima. Cysteine proteinases are present in the excretory-secretory products (ESP) as indicated by the hydrolysis of cathepsin fluorogenic substrates and confirmed by immunoblotting. Serine proteinases were predominant as indicated by substrate gel analysis and inhibitor studies. The presence of metallo-proteinases was also indicated by inhibitor studies. The optimal pH value for cysteine proteinases was 5.5, while serine proteinases were optimal at pH 8.0. As a control, cultures of Escherichia coli, the diet of C. elegans, were extracted separately and gave no evidence of overlap with C. elegans ESP. Cross reactivity between the ESP of C. elegans and antibodies raised against the ESP of the equine parasite Strongylus vulgaris indicated antigenic relatedness of a proteic epitope. This is the first study to characterize the ESP of C. elegans and to display its relatedness with that of S. vulgaris.
Publication Date: 2007-03-27 PubMed ID: 17381874DOI: 10.1017/S0022149X0724725XGoogle Scholar: Lookup
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- Journal Article
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Summary
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The research examines the proteinases released by the nematode Caenorhabditis elegans during in vitro culture, noting types like cysteine, serine, and metallo-proteinases present and their optimal pH. There’s also a observed cross-reactivity between the proteins of C. elegans and those of the parasite Strongylus vulgaris.
Proteinase Characterisation in Caenorhabditis Elegans
- The featured study investigates proteinases secreted during the non-synchronized in vitro culture of the free-living nematode, Caenorhabditis elegans. Through detailed characterization based on subunit composition, sensitivity to inhibitors, optimal pH, and specific reactivity with fluorogenic substrates, the researchers were able to identify the types of proteinases contained in the excretory-secretory products (ESP).
- The presence of cysteine proteinases in the ESP was determined through cathepsin fluorogenic substrate hydrolysis, while its characterization was further supported with immunoblotting.
- Serine proteinases were predominant, as shown by substrate gel analysis and inhibitor susceptibility. Similarly, the presence of metallo-proteinases was also revealed through inhibitor studies.
- The optimal pH for each type of proteinase was also identified: 5.5 for cysteine proteinases and 8.0 for serine proteinases.
Eliminating Diet Influence and Antigenic Relatedness
- As a control, researchers extracted cultures of Escherichia coli, the diet for C. elegans, separately to avoid confusion or overlap in results caused by dietary contribution to the worm’s ESPs. No overlapping evidence was found between E. coli and C. elegans ESPs.
- Finally, researchers observed an antigenic crossreactivity or relatedness between the ESP of C. elegans and antibodies created against the ESP of the equine parasite, Strongylus vulgaris. This suggests a shared proteic epitope between the two differing species, paving the way for further studies on relatedness and potential parasite control strategies.
- This research serves as an inaugural study into the characterization of Caenorhabditis elegans’ ESP and its antigenic relatedness with that of Strongylus vulgaris.
Cite This Article
APA
Nic An Ultaigh S, Ryan MF.
(2007).
Classes and crossreactivity of proteinases in the excretory-secretory products of Caenorhabditis elegans.
J Helminthol, 81(1), 93-99.
https://doi.org/10.1017/S0022149X0724725X Publication
Researcher Affiliations
- School of Biology and Environmental Science, University College Dublin, Belfield, Dublin 4, Ireland.
MeSH Terms
- Animals
- Caenorhabditis elegans
- Caenorhabditis elegans Proteins / analysis
- Immunologic Techniques
- Peptide Hydrolases / analysis
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