A new crustin homologue (SpCrus6) involved in the antimicrobial and antiviral innate immunity in mud crab, Scylla paramamosain

Du, Zhiqiang; Wang, Yue; Ma, Hongyu; Shen, Xiu-li; Wang, Kai; Du, Jie; Yu, Xiaodong; Fang, Wenhong; Li, Xin-Cang

doi:10.1016/j.fsi.2018.10.072

Cited by 36 publications

(35 citation statements)

References 57 publications

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“…The findings revealed that some CRRs of crustins played a role in anti-WSSV immune responses by interacting with the specific viral component. In fact, we notice that the cysteine-distribution patterns in the CRRs of SpCrus2 and SpCrus6 differ even though these two CRRs contain the same number of cysteine residues [17,25]. Thus, the structures of these two CRRs and their binding manner to WSSV may differ despite the fact that they both interact with VP26.…”

Section: Discussionmentioning

confidence: 90%

“…In S. paramamosain, previous studies have shown that SpCrus2 and SpCrus6 are significantly upregulated after WSSV challenge; however, SpCrus3, SpCrus4, and SpCrus5 do not exhibit any expression change post-viral infection [17,[23][24][25]. SpCrus6 also inhibits the proliferation of WSSV by interacting with the viral structural protein VP26 [25]. Given that SpCrus6 is a type I crustin and the mature peptide has only a CRR (including a cysteinerich domain and a WAP domain) without GRR, the antiviral activity of SpCrus6 should be exerted by its CRR.…”

Section: Discussionmentioning

confidence: 98%

“…In crustaceans, a single species can express a series of crustins with diverse antimicrobial activities against different pathogens. For instance, six crustins have been characterized in S. paramamosain, and they displayed broad antimicrobial activities [17,[22][23][24][25]. Based on the sequence and structural differences, these six crustins have been divided into two classes (types I and II).…”

Section: Discussionmentioning

confidence: 99%

“…Some crustins are reportedly involved in antiviral immune responses [18][19][20]. In S. paramamosain, previous studies have shown that SpCrus2 and SpCrus6 are significantly upregulated after WSSV challenge; however, SpCrus3, SpCrus4, and SpCrus5 do not exhibit any expression change post-viral infection [17,[23][24][25]. SpCrus6 also inhibits the proliferation of WSSV by interacting with the viral structural protein VP26 [25].…”

Section: Discussionmentioning

confidence: 99%

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SpCrus2 Glycine-Rich Region Contributes Largely to the Antiviral Activity of the Whole-Protein Molecule by Interacting with VP26, a WSSV Structural Protein

et al. 2021

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Crustins are cysteine-rich cationic antimicrobial peptides with diverse biological functions including antimicrobial and proteinase inhibitory activities in crustaceans. Although a few crustins reportedly respond to white spot syndrome virus (WSSV) infection, the detailed antiviral mechanisms of crustins remain largely unknown. Our previous research has shown that SpCrus2, from mud crab Scylla paramamosain, is a type II crustin containing a glycine-rich region (GRR) and a cysteine-rich region (CRR). In the present study, we found that SpCrus2 was upregulated in gills after WSSV challenge. Knockdown of SpCrus2 by injecting double-stranded RNA (dsSpCrus2) resulted in remarkably increased virus copies in mud crabs after infection with WSSV. These results suggested that SpCrus2 played a critical role in the antiviral immunity of mud crab. A GST pull-down assay showed that recombinant SpCrus2 interacted specifically with WSSV structural protein VP26, and this result was further confirmed by a co-immunoprecipitation assay with Drosophila S2 cells. As the signature sequence of type II crustin, SpCrus2 GRR is a glycine-rich cationic polypeptide with amphipathic properties. Our study demonstrated that the GRR and CRR of SpCrus2 exhibited binding activities to VP26, with the former displaying more potent binding ability than the latter. Interestingly, pre-incubating WSSV particles with recombinant SpCrus2 (rSpCrus2), rGRR, or rCRR inhibited virus proliferation in vivo; moreover, rSpCrus2 and rGRR possessed similar antiviral abilities, which were much stronger than those of rCRR. These findings indicated that SpCrus2 GRR contributed largely to the antiviral ability of SpCrus2, and that the stronger antiviral ability of GRR might result from its stronger binding activity to the viral structural protein. Overall, this study provided new insights into the antiviral mechanism of SpCrus2 and the development of new antiviral drugs.

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Section: Discussionmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

SpCrus2 Glycine-Rich Region Contributes Largely to the Antiviral Activity of the Whole-Protein Molecule by Interacting with VP26, a WSSV Structural Protein

et al. 2021

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“…A recombinant crustin, Sp-Crus6, was pre-incubated with WSSV viruses and injected in S. paramamosain crub gills. As a result, a decrease of virion load was observed at 48, 72, and 96 hpi, detected by Real Time-qPCR amplification of WSSV fragment [182].…”

Section: Crustaceansmentioning

confidence: 97%

Ten-Year Research Update Review: Antiviral Activities from Marine Organisms

et al. 2020

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Oceans cover more than 70 percent of the surface of our planet and are characterized by huge taxonomic and chemical diversity of marine organisms. Several studies have shown that marine organisms produce a variety of compounds, derived from primary or secondary metabolism, which may have antiviral activities. In particular, certain marine metabolites are active towards a plethora of viruses. Multiple mechanisms of action have been found, as well as different targets. This review gives an overview of the marine-derived compounds discovered in the last 10 years. Even if marine organisms produce a wide variety of different compounds, there is only one compound available on the market, Ara-A, and only another one is in phase I clinical trials, named Griffithsin. The recent pandemic emergency caused by SARS-CoV-2, also known as COVID-19, highlights the need to further invest in this field, in order to shed light on marine compound potentiality and discover new drugs from the sea.

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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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A new crustin homologue (SpCrus6) involved in the antimicrobial and antiviral innate immunity in mud crab, Scylla paramamosain

Cited by 36 publications

References 57 publications

SpCrus2 Glycine-Rich Region Contributes Largely to the Antiviral Activity of the Whole-Protein Molecule by Interacting with VP26, a WSSV Structural Protein

SpCrus2 Glycine-Rich Region Contributes Largely to the Antiviral Activity of the Whole-Protein Molecule by Interacting with VP26, a WSSV Structural Protein

Ten-Year Research Update Review: Antiviral Activities from Marine Organisms

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

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