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C5a peptidase (ScpA) activity towards human type II and type III interferons

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C5a peptidase, also known as ScpA, is a surface associated serine protease derived from Streptococcus pyogenes and has been described as an important factor in streptococcus virulence, capable of cleaving complement components C5a, C3 and C3a. Although the interactions of ScpA with complement components is well studied, extensive screening of ScpA activity against other pro-inflammatory cytokines is lacking. Here, ScpA’s ability to cleave human pro-inflammatory cytokines was tested, revealing its ability to cleave human IFNγ, IFNλ1, IFNλ2, C5, IL-37 but with significantly reduced activities. The functional consequence of ScpA’s cleavage of IFNγ in its signalling through the Jak-Stat pathway has also been evaluated in an in vitro RPE1 cell model. These newly identified targets for ScpA highlight the complexity of streptococcus infections and indeed, the potential for ScpA to have a therapeutic role in the progression of inflammatory diseases involving these cytokines

History

Publication

Cytokine 180, 156652

Publisher

Elsevier

Other Funding information

Disruptive Technologies Innovation Fund (DTIF) under the National Development Plan 2018-2027, grant number DT/2018/0054.

Also affiliated with

  • Bernal Institute
  • Synthesis and Solid State Pharmaceutical Centre

Department or School

  • Chemical Sciences

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