AI Article Synopsis
- Enzymatic digestion of extracellular matrix proteins by proteinases in promastigotes is important for potential vaccine and therapy development against related diseases.
- The study conducted at the University of Tehran used gelatin zymography to analyze proteases, revealing significant findings related to metalloproteinases, including a 63-kDa glycoprotein (GP63), which plays a crucial role in virulence.
- The results demonstrated the presence of various metalloproteases, serine proteases, and cathepsins in promastigote exosomes and lysate, suggesting their potential for immunodiagnostic applications.
Article Abstract
Background: Enzymatic digestion of extra cellular matrix proteins by proteinases of promastigotes is a complex process. Hence, studies on functional proteomics of these enzymes can help select these enzymes as possible vaccine candidates or selecting candidates for chemotherapy and immunotherapy. Several proteolytic enzymes are involved in virulence of spp. These enzymes are mostly serine, cysteine and metalloproteases. We aimed to detect proteases in promastigote exosomes.
Methods: Serine, cysteine and metalloproteases were investigated in exosomes and lysate of promastigote using gelatin zymography. The study was carried out in the Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran, in 2021.
Results: Zymography findings of metalloproteinases showed transparent bands, including a 63-kDa glycoprotein (GP63). This glycoprotein is a major surface metalloproteinase. In addition, transparent bands belonged to serin proteases and cathepsin were demonstrated in gels associated to promastigote lysate and exosomes.
Conclusion: Several metalloproteases, serin proteases and cathepsins were shown in promastigote lysate and exosomes of , which could purified and used as fractions for immunodiagnostic.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10758077 | PMC |
| http://dx.doi.org/10.18502/ijpa.v18i4.14263 | DOI Listing |
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