Characterization of a double WAP domain-containing protein from the red swamp crayfish Procambarus clarkii

Zhang, Hongwei; Man, Xin; Wang, Yue; Song, Qisheng; Stanley, David; Hui, Kai-Min; Zhang, Xiaowen

doi:10.1016/j.fsi.2017.10.019

Cited by 21 publications

(6 citation statements)

References 26 publications

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“…Similar aggulutination and opsonization were also found in type I crustin MjCruI-1 from Marsupenaeus japonicus (31). Most crustins with protease inhibitory activity are mainly type III and IV crustins, such as LvSWD (32), MjSWD (33), Mj-DWD (34), Fc-DWD (26), and Pc-DWD (35). Taken together, although different custins perform various activities, their roles in host immunity are essential.…”

Section: Introductionsupporting

confidence: 52%

“…Of the crustins in S. paramamosain, except for CruSp, which was most expressed in the hemocytes, SpCrus2-6 were highly expressed in the gills (8,17,46). Additionally, it is noted that most crustins in shrimp were identified from hemocytes, such as SWDPm1 (47), Pc-crustin 4 (8), Pc-DWD (35), Fi-crustin (22), and LvSWD3 (48). The expression levels of PtCrustin2 and 3 from Portunus trituratus was highest in the eye stalk, followed by the gills (20).…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Introductionsupporting

confidence: 52%

Section: Discussionmentioning

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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“…Finally, Type V crustins from insect order Hymenoptera, are similar to Type I crustins; nevertheless, with an aromatic amino acid-rich domain between the cysteine-rich domain and WAP domain (Zhang and Zhu 2012 ). Zhao and Wang ( 2008 ) had proposed a divergent evolution for WAP domains in crustaceans, exhibiting different function such as antimicrobial activity and proteinase inhibitor activity (Du et al 2010 ; Jiang et al 2013 ; Zhang et al 2017 ). Neighbour joining analysis in present study revealed two main branches of WAP domain containing proteins in crustaceans, one group containing the ‘crustin signature domain’ with WAP domain peptides (Type I and Type II crustins) and the other group which do not possess the signature crustin domain, yet containing the WAP domains (SWDs and DWDs), similar to previous studies such as Zhao and Wang, ( 2008 ) and Mu et al, ( 2010 ).…”

Section: Discussionmentioning

confidence: 99%

Characterisation of a novel crustin isoform from mud crab, Scylla serrata (Forsskål, 1775) and its functional analysis in silico

Anju

Anooja

Athira

et al. 2022

In Silico Pharmacol.

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A 336-base pair (bp) sized mRNA sequence encoding 111 amino acid size crustin isoform (MC-crustin) was obtained from the gill sample of the green mud crab, Scylla serrata . MC-crustin possessed an N-terminal signal peptide region comprising of 21 amino acid residues, followed by a 90 amino acid mature peptide region having a molecular weight of 10.164 kDa, charge + 4.25 and theoretical p I of 8.27. Sequence alignment and phylogenetic tree analyses revealed the peptide to be a Type I crustin, with four conserved cysteine residues forming the cysteine rich region, followed by WAP domain. MC-crustin was cationic with cysteine/proline rich structure and was predicted with antimicrobial, anti-inflammatory, anti-angiogenic and anti-hypertensive property making it a potential molecule for possible therapeutic applications.

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“…However, several examples of type IV crustins with a clear role in the host innate immunity of crustaceans have since been reported. A good example is the type IV crustin from the red swamp crayfish Procambarus clarkia , reported in 2017 [ 123 ]. Antimicrobial activities have also been established for both SWD and DWD peptides in recent reports, such as that published by Visetnan et al, in 2017 [ 124 ].…”

Section: Defense Mechanisms In Crustaceansmentioning

confidence: 99%

Marine Arthropods as a Source of Antimicrobial Peptides

et al. 2022

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Peptide therapeutics play a key role in the development of new medical treatments. The traditional focus on endogenous peptides has shifted from first discovering other natural sources of these molecules, to later synthesizing those with unique bioactivities. This review provides concise information concerning antimicrobial peptides derived from marine crustaceans for the development of new therapeutics. Marine arthropods do not have an adaptive immune system, and therefore, they depend on the innate immune system to eliminate pathogens. In this context, antimicrobial peptides (AMPs) with unique characteristics are a pivotal part of the defense systems of these organisms. This review covers topics such as the diversity and distribution of peptides in marine arthropods (crustacea and chelicerata), with a focus on penaeid shrimps. The following aspects are covered: the defense system; classes of AMPs; molecular characteristics of AMPs; AMP synthesis; the role of penaeidins, anti-lipopolysaccharide factors, crustins, and stylicins against microorganisms; and the use of AMPs as therapeutic drugs. This review seeks to provide a useful compilation of the most recent information regarding AMPs from marine crustaceans, and describes the future potential applications of these molecules.

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Characterization of a double WAP domain-containing protein from the red swamp crayfish Procambarus clarkii

Cited by 21 publications

References 26 publications

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

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

Characterisation of a novel crustin isoform from mud crab, Scylla serrata (Forsskål, 1775) and its functional analysis in silico

Marine Arthropods as a Source of Antimicrobial Peptides

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