Publication:
A single WAP domain-containing protein from Litopenaeus vannamei possesses antiproteinase activity against subtilisin and antimicrobial activity against AHPND-inducing Vibrio parahaemolyticus

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Issued Date

2017

Resource Type

Article

File Type

application/pdf

ISSN

10504648

DOI

10.1016/j.fsi.2017.07.046

Other identifier(s)

2-s2.0-85025825788

Rights Holder(s)

มหาวิทยาลัยศรีนครินทรวิโรฒ

Bibliographic Citation

Fish and Shellfish Immunology. Vol 68, (2017), p.341-348

Suggested Citation

Visetnan S., Supungul P., Tassanakajon A., Donpudsa S., Rimphanitchayakit V. A single WAP domain-containing protein from Litopenaeus vannamei possesses antiproteinase activity against subtilisin and antimicrobial activity against AHPND-inducing Vibrio parahaemolyticus. Fish and Shellfish Immunology. Vol 68, (2017), p.341-348. doi:10.1016/j.fsi.2017.07.046 Retrieved from: https://hdl.handle.net/20.500.14740/4090

Title

A single WAP domain-containing protein from Litopenaeus vannamei possesses antiproteinase activity against subtilisin and antimicrobial activity against AHPND-inducing Vibrio parahaemolyticus

Author(s)

Visetnan S.
 Supungul P.
 Tassanakajon A.
 Donpudsa S.
 Rimphanitchayakit V.

Abstract

The single WAP domain-containing protein (SWD) is a type III crustin antimicrobial peptide whose function is to defense the host animal against the bacterial infection by means of antimicrobial and antiproteinase activities. A study of SWD from Litopenaeus vannamei (LvSWD) is reported herein about its activities and function against bacteria, particularly the AHPND-inducing Vibrio parahaemolyticus (VPAHPND) that causes acute hepatopancreatic necrosis disease (AHPND). The LvSWD is mainly synthesized in hemocytes and up-regulated in response to VPAHPND infection. Over-expressed mature recombinant LvSWD (rLvSWD) and its WAP domain (rLvSWD-WAP) are able to strongly inhibit subtilisin but not trypsin, chymotrypsin and elastase. The rLvSWD inhibits subtilisin with the inhibition constant (Ki) of 14.3 nM. However, only rLvSWD exhibited antimicrobial activity against both Gram-positive and Gram-negative bacteria. Unlike the rLvSWD, the rLvSWD-WAP does not possess antimicrobial activity. Therefore, the killing effect of rLvSWD on VPAHPND and Bacillus megaterium was studied. The MIC of 30 μM against VPAHPND is bactericidal whereas the MIC against B. megaterium is not. With four times the MIC of rLvSWD, the VPAHPND-treated post larval shrimp are able to survive longer with 50% survival rate as long as 78 h as compared to 36 h of the infected shrimp without rLvSWD. The antimicrobial activity of LvSWD against the VPAHPND infection suggests its potential application for disease control in aquaculture. © 2017 Elsevier Ltd

Subject(s)

Polypeptide antibiotic agent
 Proteinase inhibitor
 Single WAP domain containing protein
 Subtilisin
 Unclassified drug
 Antiinfective agent
 Antimicrobial cationic peptide
 Arthropod protein
 Subtilisin
 Acute hepatopancreatic necrosis disease
 Acute hepatopancreatic necrosis disease
 Animal experiment
 Animal model
 Animal tissue
 Antibacterial activity
 Article
 Bacillus megaterium
 Controlled study
 Drug synthesis
 Enzyme inhibition
 In vitro study
 Inhibition constant
 Litopenaeus vannamei
 Liver necrosis
 Minimum bactericidal concentration
 Minimum inhibitory concentration
 Nonhuman
 Pancreas necrosis
 Protein domain
 Protein expression
 Survival rate
 Tissue distribution
 Upregulation
 Vibrio parahaemolyticus
 Amino acid sequence
 Animal
 Antagonists and inhibitors
 Chemistry
 Drug effect
 Enzyme activation
 Genetics
 Immunology
 Innate immunity
 Metabolism
 Microbiology
 Nucleotide sequence
 Penaeidae
 Vibrio parahaemolyticus
 Amino Acid Sequence
 Animals
 Anti-Infective Agents
 Antimicrobial Cationic Peptides
 Arthropod Proteins
 Base Sequence
 Enzyme Activation
 Immunity, Innate
 Penaeidae
 Subtilisin
 Vibrio parahaemolyticus

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URI

https://hdl.handle.net/20.500.14740/4090

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Scopus: Year 1983-2021

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