A double WAP domain-containing protein PmDWD from the black tiger shrimp Penaeus monodon is involved in the controlling of proteinase activities in lymphoid organ

Suthianthong, Pranisa; Pulsook, Naritsara; Supungul, Premruethai; Tassanakajon, Anchalee; Rimphanitchayakit, Vichien

doi:10.1016/j.fsi.2010.12.029

Cited by 18 publications

(9 citation statements)

References 40 publications

(44 reference statements)

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“…1 A). The SWDPm2 [1], PmDWD [25], human SLPI and human elafin [18] have both antibacterial and antiproteinase activities. The human EPPIN is composed of a WAP domain and a Kunitz domain.…”

Section: Mutagenesis and Recombinant Expressionmentioning

confidence: 99%

“…The DWDs have only recently been identified in a number of shrimp species and are believed to be an invertebrate version of mammalian secretory leukocyte protease inhibitor (SLPI) for they have similarly two WAP domains [15,25]. The shrimp DWDs have only very selective antiproteinase activity.…”

Section: Introductionmentioning

confidence: 99%

“…The shrimp DWDs have only very selective antiproteinase activity. They do not inhibit commercially available proteinases like trypsin, chymotrypsin, elastase or even subtilisin that has broad substrate specificity but inhibit secretory proteinases from selected bacteria [7,9,25].…”

Section: Introductionmentioning

confidence: 99%

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The N-terminal glycine-rich and cysteine-rich regions are essential for antimicrobial activity of crustinPm1 from the black tiger shrimp Penaeus monodon

Suthianthong

Donpudsa

Supungul

et al. 2012

Fish & Shellfish Immunology

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“…1 A). The SWDPm2 [1], PmDWD [25], human SLPI and human elafin [18] have both antibacterial and antiproteinase activities. The human EPPIN is composed of a WAP domain and a Kunitz domain.…”

Section: Mutagenesis and Recombinant Expressionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The N-terminal glycine-rich and cysteine-rich regions are essential for antimicrobial activity of crustinPm1 from the black tiger shrimp Penaeus monodon

Suthianthong

Donpudsa

Supungul

et al. 2012

Fish & Shellfish Immunology

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“…Type III crustin from P. monodon exhibits anti-Gram-positive, but not anti-Gram-negative bacteria activity and it is a competitive inhibitor of subtilisin A [16]. However, the DWD crustins do not show apparent activity [17].…”

Section: Introductionmentioning

confidence: 96%

Anti-Vibrio Response of CarcininPm 1 from Penaeus monodon and Its Heterologous Expression

Zhou

et al. 2019

E3S Web Conf.

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Crustins are crucial antimicrobial peptides in shrimp and play very important roles in innate immunity. In this research, a Type I crustin from Penaeus monodon (CarcininPm1) contained 108 residues was studied. The first 16 residues are signal peptide. It contained ten cysteines but did not form an intact whey acidic protein (WAP) domain. CarcininPm1 was observed to widely distribute in all tissues, while highly expressed in intestine. The expression level of CarcininPm1 in hepatopancreas was up-regulated 12- 20 times during 4-12h post challenged by Vibrio parahaemolyticus. And the transcription in heart, stomach and gills was also significantly enhanced at 4h post challenge. The mature peptide was expressed successfully in Eschericha coli by fusing to a SUMO protein, with protein production around 8 mg/mL. After cleavage with SUMO protease, carcininPm1 was obtained indicating its potential applications.

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“…Some crustin variants, such as CrustinPm1 (21), Fi-Crustin2 (22) are only effective against gram-negative bacteria such as E. coli, Edwardsiella tarda and A. hydrophila, while CrusSp (23), CruFc (24), CrusEs2 (25), CrustinPm1 and CrustinPm4 (4) had only antibacterial activities against gram-positive bacteria, such as S. aureus, Micrococcus luteus and Bacillus subtilis. Exceptionally, several crustins have no obvious antibacterial activity, such as Fc-DWD (26), PcDWD (26), Pc-SWD (27), PmDWD (28), and LvCrustin I-1 (29). However, they have also been confirmed to play an important role in host immunity (e.g., recombinant LvCrustin I-1 could regulate intestinal microbiota homeostasis in L. vannamei (29)) and may act as host defense peptides.…”

Section: Introductionmentioning

confidence: 99%

A New Crustin Gene Homolog SpCrus8 Identified in Scylla paramamosain Exerting In Vivo Protection Through Opsonization and Immunomodulation

Jiang

Chen

et al. 2022

Front. Immunol.

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Crustins are the most abundant class of antimicrobial peptides in crustaceans and are essential for protecting animals from infection. Among them, type II crustins usually exhibit potent antimicrobial activity. Interestingly, in this study, a newly identified type II crustin gene homolog (named SpCrus8) from mud crab Scylla paramamosain, the recombinant proteins of which (rSpCrus8 and rTrx-SpCrus8) showed no obvious antibacterial effects, but could significantly reduce the bacterial load in crab hemolymph and improve the survival rate of crabs infected with Vibrio alginolyticus. The immune-related function of SpCrus8 and the underlying mechanism deserve further investigation. It was found that the SpCrus8 gene was widely distributed in various tissues of adult crabs. In the hepatopancreas of crabs infected with V. alginolyticus or Staphylococcus aureus, transcripts of the SpCrus8 gene were remarkably induced, indicating that the SpCrus8 gene was involved in the immune response to bacterial infection in vivo. In addition, rSpCrus8 and rTrx-SpCrus8 had strong binding activity not only to microbial surface components (lipopolysaccharide, lipoteichoic acid, peptidoglycan, and glucan), but also to the tested bacteria (S. aureus, Pseudomonas aeruginosa and V. alginolyticus). Notably, rSpCrus8 and rTrx-SpCrus8 could significantly promote hemocyte phagocytosis. After rSpCrus8 and rTrx-SpCrus8 treatment, a large number of fluorescent microspheres were observed to aggregate into clusters and be phagocytosed by multiple hemocytes, while hemocytes in the control group phagocytosed only individual microspheres, indicating that SpCrus8 played an important role in opsonization. When the SpCrus8 gene was knocked down, the expression levels of the key phagocytosis-related genes SpRab5 and SpRab7 were significantly downregulated, as well as the IMD signaling pathway genes SpIKKβ and SpRelish, and another crustin gene SpCrus5. Correspondingly, all the SpIKKβ, SpRelish and SpCrus5 genes were significantly upregulated after rSpCrus8 treatment, suggesting that SpCrus8 might be involved in the immunomodulation of S. paramamosain. Taken together, this study revealed the immune-related functions of the SpCrus8 gene in opsonization and regulation, which will help us further understand the role of the crustin gene family in the immune system of mud crabs and provide new insights into the function of type II crutins.

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A double WAP domain-containing protein PmDWD from the black tiger shrimp Penaeus monodon is involved in the controlling of proteinase activities in lymphoid organ

Cited by 18 publications

References 40 publications

The N-terminal glycine-rich and cysteine-rich regions are essential for antimicrobial activity of crustinPm1 from the black tiger shrimp Penaeus monodon

The N-terminal glycine-rich and cysteine-rich regions are essential for antimicrobial activity of crustinPm1 from the black tiger shrimp Penaeus monodon

Anti-Vibrio Response of CarcininPm 1 from Penaeus monodon and Its Heterologous Expression

A New Crustin Gene Homolog SpCrus8 Identified in Scylla paramamosain Exerting In Vivo Protection Through Opsonization and Immunomodulation

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