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• W2081840282 endingPage "e73563" @default.
• W2081840282 startingPage "e73563" @default.
• W2081840282 abstract "Whey acidic proteins (WAP) belong to a large gene family of antibacterial peptides, which are critical in the host immune response against microbial invasion. The common feature of these proteins is a single WAP domain maintained by at least one four-disulfide core (4-DSC) structure rich in cysteine residues. In this study, a double WAP domain (DWD)-containing protein, Es-DWD1, was first cloned from the Chinese mitten crab (Eriocheirsinensis). The full-length Es-DWD1cDNA was 1193 bp, including a 411 bp open reading frame (ORF) encoding 136 amino acids with a signal peptide of 22 amino acids in the N-terminus. A comparison with other reported invertebrate and vertebrate sequences revealed the presence of WAP domains characteristic of WAP superfamilies. As determined by quantitative real-time RT-PCR, Es-DWD1 transcripts were ubiquitously expressed in all tissues, but it was up-regulated in hemocytes post-challenge with pathogen-associated molecular patterns (PAMPs). The mature recombinant Es-DWD1 (rEs-DWD1) protein exhibited different binding activities to bacteria and fungus. Moreover, rEs-DWD1 could exert agglutination activities against Bacillus subtilis and Pichiapastoris and demonstrated inhibitory activities against the growth of Staphylococcus aureus, Aeromonas hydrophila and P. pastoris. Furthermore, rEs-DWD1 showed a specific protease inhibitory activity in B. subtilis. Coating of rEs-DWD1 onto agarose beads enhanced encapsulation of the beads by crab hemocytes. Collectively, the results suggest that Es-DWD1 is a double WAP domain containing protein with antimicrobial and proteinase inhibitory activities, which play significant roles in the immunity of crustaceans." @default.
• W2081840282 created "2016-06-24" @default.
• W2081840282 creator A5004681952 @default.
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• W2081840282 date "2013-08-13" @default.
• W2081840282 modified "2023-10-18" @default.
• W2081840282 title "A Double WAP Domain-Containing Protein Es-DWD1 from Eriocheir sinensis Exhibits Antimicrobial and Proteinase Inhibitory Activities" @default.
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• W2081840282 doi "https://doi.org/10.1371/journal.pone.0073563" @default.
• W2081840282 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3742519" @default.
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• W2081840282 hasPublicationYear "2013" @default.
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