Serine protease inhibitor derived from Trichinella spiralis (TsSERP) inhibits neutrophil elastase and impairs human neutrophil functions
Issued Date
2022-10-25
Resource Type
eISSN
22352988
Scopus ID
2-s2.0-85141367674
Pubmed ID
36389172
Journal Title
Frontiers in Cellular and Infection Microbiology
Volume
12
Rights Holder(s)
SCOPUS
Bibliographic Citation
Frontiers in Cellular and Infection Microbiology Vol.12 (2022)
Suggested Citation
Kobpornchai P., Reamtong O., Phuphisut O., Malaitong P., Adisakwattana P. Serine protease inhibitor derived from Trichinella spiralis (TsSERP) inhibits neutrophil elastase and impairs human neutrophil functions. Frontiers in Cellular and Infection Microbiology Vol.12 (2022). doi:10.3389/fcimb.2022.919835 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/84885
Title
Serine protease inhibitor derived from Trichinella spiralis (TsSERP) inhibits neutrophil elastase and impairs human neutrophil functions
Author's Affiliation
Other Contributor(s)
Abstract
During early infection with Trichinella spiralis, host neutrophils destroy newborn larvae migrating in the bloodstream, preventing infection. However, parasites secrete various immunomodulatory molecules to escape the host’s defense mechanisms, allowing them to infect the host and live for long periods. T. spiralis secretes serine protease inhibitors (TsSERPs), which are key inhibitory molecules that regulate serine proteases involved in digestion and inflammation. However, the modulatory roles of TsSERP in the inhibition of neutrophil serine proteases (NSPs) and neutrophil functions are unknown. Therefore, the immunomodulatory properties of recombinant TsSERP1 (rTsSERP1) on NSPs and neutrophil functions were investigated in this study. rTsSERP1 preferentially inhibited human neutrophil elastase (hNE). In addition, incubation of rTsSERP1 with fMLP-induced neutrophils impaired their phagocytic ability. The formation of neutrophil extracellular traps (NETs) was activated with phorbol myristate acetate (PMA), and NETs were dramatically reduced when treated with rTsSERP1. Furthermore, rTsSERP1 suppressed the production of proinflammatory cytokines and chemokines during neutrophil activation, which are essential for neutrophil-mediated local or systemic inflammation regulation. In conclusion, T. spiralis immune evasion mechanisms are promoted by the inhibitory properties of TsSERP1 against neutrophil elastase and neutrophil defense functions, and these might be promising alternative treatment targets for inflammatory disorders.