Antibacterial and antiproteinase activities of a double whey acidic protein domain-containing protein from Penaeus vannamei Boone, 1931 (Decapoda, Penaeidae)

Double whey acidic protein domain-containing proteins (DWDs) or secretory leukocyte protease inhibitor (SLPI)-like proteins, have been identified in many species of Crustacea. The PvDWD1 from Penaeus vannamei was the first SLPI-like protein identified in a crustacean. Herein, we report that the expression of PvDWD1 was up-regulated at 6 h after acute hepatopancreatic necrosis disease (AHPND)-causing Vibrio parahaemolyticus (VPAHPND) challenge. Similarly, after a different stress other than bacterial infection, the chronic non-lethal heat shock (NLHS) induction, the expression of the PvDWD1 gene was increased at 6 and 24 h after chronic NLHS treatment. The recombinant PvDWD1 (rPvDWD1) protein was over-expressed and tested for its deleterious activity against the bacteria. The rPvDWD1 protein exhibited growth inhibitory activity against Bacillus megaterium and VPAHPND. Moreover, the rPvDWD1 protein possessed an antiproteinase activity against the secreted proteinases from Bacillus subtilis and VPAHPND. The PvDWD1 perhaps functions in shrimp immunity through antimicrobial and antiproteinase properties.

Green fluorescent protein gene for site-specific integration into the locus of the rabbit whey acidic protein gene

The high content of whey acidic protein in rabbit milk makes the gene of this protein a promising candidate for its replacement by the gene of pharmacologically active protein using the CRISPR/Cas9 system. The plasmid that contains 5’ and 3’ arms of homology to the rabbit WAP gene was created. A fragment containing a green fluorescent protein gene under the CMV promoter has been integrated into this site. A strategy of making double-stranded cuts in the gene WAP and receiving four pX330 plasmids encoding the endonuclease Cas9 and guide RNAs was developed. The plasmid containing a fragment cmvEGFP was designed for site-specific integration by homologous recombination into the gene WAP to assess the effectiveness of site-specificity of components of the CRISPR/Саѕ9 in vitro.

The role of whey acidic protein four-disulfide-core proteins in respiratory health and disease

Members of the whey acidic protein (WAP) or WAP four-disulfide-core (WFDC) family of proteins are a relatively under-explored family of low molecular weight proteins. The two most prominent WFDC proteins, secretory leukocyte protease inhibitor (SLPI) and elafin (or the precursor, trappin-2), have been shown to possess multiple functions including anti-protease, anti-bacterial, anti-viral and anti-inflammatory properties. It is therefore of no surprise that both SLPI and elafin/trappin-2 have been developed as potential therapeutics. Given the abundance of SLPI and elafin/trappin-2 in the human lung, most work in the area of WFDC research has focused on the role of WFDC proteins in protecting the lung from proteolytic attack. In this review, we will outline the current evidence regarding the expanding role of WFDC protein function with a focus on WFDC activity in lung disease as well as emerging data regarding the function of some of the more recently described WFDC proteins.