Objective To construct a double-effect fusion protein functioning as an anti-inflammatory and anticoagulant

which can inhibit the inflammatory response and thrombosis simultaneously in atherosclerosis lesions. Methods Firstly

staphylococcal superantigen-like protein-5 (SSL5) gene sequence was cloned by PCR from Staphylococcus aureus (strain NCTC8325). Secondly

N-terminal pelB leading sequence

SSL5 gene sequence

tick anticoagulant peptide (TAP) gene sequence

with C-terminal both c-Myc and His6 tags were cloned into the pHOG21 expression vector using recombined DNA technique

and the obtained recombinant were further transformed into E. coli BL21(DE3) cells to express the fusion protein TAP-SSL5. Flow cytometry was used to investigate whether the fusion protein could bind with P-selectin glycoprotein ligand-1 (PSGL-1) on monocytes as SSL5. Finally

the inhibitory effect of TAP-SSL5 on factor Xa (FXa) activity were detected by chromogenic substrate assay in vitro.  Results TAP-SSL5 fusion protein binded to PSGL-1 on HL60 monocytes

and inhibited the FXa activity in vitro as well

with an inhibitory rate of 39.5% (P0.01).  Conclusion  The fusion protein TAP-SSL5 is a novel molecule targeting PSGL-1

which has an double-effects of anti-inflammation and anticoagulation.