A novel single WAP domain-containing protein isoform with antibacterial relevance in Litopenaeus vannamei

• A SWD protein isoform gene in Litopenaeus vanname was identified.
• Lv-SWDi was obviously upregulated at 12 h after Vibrio injection.
• Endogenous Lv-SWDi protein was obviously upregulated after Vibrio injection.
• Purified rLv-SWDi could directly bind to Gram-positive and Gram-negative bacteria.
• rLv-SWDi could inhibit secretory protease activity from Bacillus subtilis.

Single WAP domain (SWD)-containing protein is a small protein containing a whey acidic protein (WAP) domain at the C-terminal region. SWD-containing protein exhibits structural similarity to the family of serine proteinase inhibitors. As of this writing, some SWD domain-containing proteins have been identified in crustaceans, and their functions included antibacterial and anti-proteinase activities. We identified a SWD protein isoform gene in Litopenaeus vanname (Lv-SWDi). Very high sequence similarity was found between Lv-SWDi and Lv-SWD. Results of time-course analysis for the gene expression profile showed that Lv-SWDi could produce a rapid feedback and an obvious upregulation at 12 h after Vibrio injection. Endogenous Lv-SWDi protein was obviously upregulated, and the highest expression level was reached at 24 h after Vibrio injection. The purified rLv-SWDi could directly bind to Gram-positive and Gram-negative bacteria. Results of the proteinase inhibitory assay also showed that rLv-SWDi could inhibit secretory protease activity from Bacillus subtilis. Lv-SWDi is a part of an important immunity-relevant gene and may serve important functions in defense against bacteria.