Recombinant expression and characterization of a serine protease inhibitor (Lvserpin7) from the Pacific white shrimp, Litopenaeus vannamei

•A novel serine protease inhibitor (Lvserpin7) was identified and characterized from Litopenaeus vannamei.•Lvserpin7 transcripts were significantly up-regulated in the early stage upon pathogens infection.•rLvserpin7 could bind to both the Gram-positive and Gram-negative bacterias.•rLvserpin7 exhibited inhibition on bacterial protease and prophenoloxidase activation.

Serine protease inhibitors (serpins) are widely known to its inhibitory role on proteases involved in the immune responses. Herein, a novel serine protease inhibitor (Lvserpin7), encoding for 411 amino acids with calculated molecular mass of 46.29 kDa and isoelectric point of 6.98 was characterized from the Pacific white shrimp Litopenaeus vannamei. Lvserpin7 shared 92.9% identities to Penaeus monodon serpin7. Among the tested tissues, Lvserpin7 was mainly expressed in hemocytes and gill. The expression profiles analysis indicated that Lvserpin7 was significantly up-regulated in the early stage upon Vibrio anguillarum, Micrococcus lysodeikticus or White Spot Syndrome Virus (WSSV) infection. Fusion protein expression was induced by IPTG, and the purified recombinant Lvserpin7 protein (rLvserpin7) binds to both the Gram-positive and Gram-negative bacteria. Also rLvserpin7 exhibited inhibitory activity against the proteases secreted by Bacillus subtilis. Moreover, rLvserpin7 showed inhibition role on prophenoloxidase activation. To recap, we proposed that Lvserpin7 was implicated in the shrimp immunity via the inhibition of bacterial proteases and proteases involved in prophenoloxidase system.