Identification of the protease inhibitory domain of Trichinella spiralis novel cystatin (TsCstN)
Issued Date
2024-08-01
Resource Type
eISSN
29826799
Scopus ID
2-s2.0-85203114732
Pubmed ID
39218632
Journal Title
Parasites, hosts and diseases
Volume
62
Issue
3
Start Page
330
End Page
341
Rights Holder(s)
SCOPUS
Bibliographic Citation
Parasites, hosts and diseases Vol.62 No.3 (2024) , 330-341
Suggested Citation
Yuthithum T., Phuphisut O., Reamtong O., Kosoltanapiwat N., Chaimon S., Kobpornchai P., Thawornkuno C., Malaithong P., Sawatdichaikul O., Adisakwattana P. Identification of the protease inhibitory domain of Trichinella spiralis novel cystatin (TsCstN). Parasites, hosts and diseases Vol.62 No.3 (2024) , 330-341. 341. doi:10.3347/PHD.24026 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/101184
Title
Identification of the protease inhibitory domain of Trichinella spiralis novel cystatin (TsCstN)
Corresponding Author(s)
Other Contributor(s)
Abstract
The Trichinella spiralis novel cystatin (TsCstN) inhibits cathepsin L (CatL) activity and inflammation of macrophages during lipopolysaccharide (LPS) induction. To identify the protease inhibitory region, this study applied an in silico modeling approach to simulate truncation sites of TsCstN (Ts01), which created four truncated forms, including TsCstN∆1-39 (Ts02), TsCstN∆1-71 (Ts03), TsCstN∆1-20, ∆73-117 (Ts04), and TsCstN∆1-20, ∆42-117 (Ts05). The superimposition of these truncates modeled with AlphaFold Colab indicated that their structures were more akin to Ts01 than those modeled with I-TASSER. Moreover, Ts04 exhibited the closest resemblance to the structure of Ts01. The recombinant Ts01 (rTs01) and truncated proteins (rTs02, rTs03, and rTs04) were successfully expressed in a prokaryotic expression system while Ts05 was synthesized, with sizes of approximately 14, 12, 8, 10, and 2.5 kDa, respectively. When determining the inhibition of CatL activity, both rTs01 and rTs04 effectively reduced CatL activity in vitro. Thus, the combination of the α1 and L1 regions may be sufficient to inhibit CatL. This study provides comprehensive insights into TsCstN, particularly regarding its protein function and inhibitory domains against CatL.