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. 2026 Feb 18;17(3):e03855-25. doi: 10.1128/mbio.03855-25

Fig 2.

Molecular evidence of specific binding between bacterial OspC effectors and inflammatory caspases through domain maps, yeast two-hybrid assays, and immunoprecipitation experiments. Data reveal that OspC2 selectively binds CASP5 while OspC3 targets CASP4.

OspC2 and OspC3 distinctly bind and modify CASP5 and CASP4, respectively. (A) Schematic of the domain compositions of CASP4 and CASP5. (B) Images of the Y2H interactions detected between OspC2/CASP5 and OspC3/CASP4 were obtained after 7 days of growth on selective media. (C) HEK293 cells were co-transfected with plasmids that express the designated GFP-OspC effector plus one that expresses a 3× FLAG-tagged catalytically dead full-length variant of CASP4 or CASP5. After 24 h, the cells were lysed, and the FLAG-tagged caspases were immunoprecipitated. Immunoblots of the input and immunoprecipitated fractions were probed with the designated antibodies. The blots shown are representative of at least three experimental repeats.