ArticlePloS one2013
A double WAP domain-containing protein Es-DWD1 from Eriocheir sinensis exhibits antimicrobial and proteinase inhibitory activities.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 54 citations in OpenAlex.
- What are the 100 most cited fungal genera?Studies in mycology · 2024Article
- Marine Invertebrate Antimicrobial Peptides and Their Potential as Novel Peptide Antibiotics.Marine drugs · 2023Review
- A Novel Peptide with Antifungal Activity from Red Swamp CrayfishAntibiotics (Basel, Switzerland) · 2022Article
- On the wave of the crustin antimicrobial peptide family: From sequence diversity to function.Fish and shellfish immunology reports · 2022Review
- Antimicrobial peptides from freshwater invertebrate species: potential for future applications.Molecular biology reports · 2022Review
- Characterization of the Dual Functions ofMarine drugs · 2022Article
- A New Crustin Gene Homolog SpCrus8 Identified inFrontiers in immunology · 2022Article
- Cloning and Analysis of Gene Expression of Two Toll Receptors in Freshwater Pearl MusselFrontiers in physiology · 2018Article
- A C1qDC Protein (HcC1qDC6) with Three Tandem C1q Domains Is Involved in Immune Response of Triangle-Shell Pearl Mussel (Frontiers in physiology · 2017Article
- Antimicrobial peptides in marine invertebrate health and disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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