Mechanism study on a new antimicrobial peptide Sphistin derived from the N-terminus of crab histone H2A identified in haemolymphs of Scylla paramamosain

Chen, Bei; Fan, Dan-Qing; Zhu, Kexin; Shan, Zhongguo; Chen, Fang-Yi; Lin, Hui; Cai, Ling; Wang, Kejian

doi:10.1016/j.fsi.2015.10.010

Cited by 54 publications

(26 citation statements)

References 76 publications

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“…3 ). Similarly, other CAMPs including RI18, a PMAP-36-derived peptide, and Sphistin, a crab histone H2A-derived peptide, also induced bacterial cell surface damage when tested against Escherichia coli and Staphylococcus aureus , respectively 21 , 33 . On the contrary, other histone-derived antimicrobial peptides, such as buforin II, DesHDAP1 and DesHDAP2, can induce bacterial cell death by translocating through the lipid bilayer without causing significant membrane permeabilization 34 – 36 .…”

Section: Discussionmentioning

confidence: 98%

Histone H5 is a potent Antimicrobial Agent and a template for novel Antimicrobial Peptides

Jodoin

Hincke

2018

Sci Rep

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Modern medicine is challenged continuously by the increasing prevalence of antibiotic resistant bacteria. Cationic antimicrobial peptides and their derivatives are interesting potential alternatives to antibiotics due to their rapid action, broad-spectrum of antimicrobial activity and limited emergence of bacterial resistance. This study reports the novel antimicrobial properties of histone H5, purified from chicken erythrocytes, and histone H5-derived synthetic peptides. Broth microdilution assays revealed that histone H5 has potent broad-spectrum antimicrobial activity against Gram-positive and Gram-negative planktonic bacteria (MIC range: 1.9 ± 1.8 to 4.9 ± 1.5 µg/mL), including vancomycin-resistant Enterococcus (VRE) and methicillin-resistant Staphylococcus aureus (MRSA). Moreover, histone H5 displayed anti-biofilm activity against established Listeria monocytogenes and Pseudomonas aeruginosa biofilms. Scanning electron microscopy demonstrated bacterial membrane damage after histone H5 treatment, while a hemolytic assay revealed that histone H5 is non-toxic towards mammalian erythrocytes, even at a concentration of 1 mg/mL. Although the predicted H5-derived antimicrobial peptides tested in this study were located within the antimicrobial domain of histone H5, their synthetic versions did not possess more potent antimicrobial activity than the full length protein. Overall, this study demonstrates that histone H5 is a potent antimicrobial and therefore a promising template for the development of novel histone H5-derived antimicrobial peptides.

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Section: Discussionmentioning

confidence: 98%

Histone H5 is a potent Antimicrobial Agent and a template for novel Antimicrobial Peptides

Jodoin

Hincke

2018

Sci Rep

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“…Nonetheless, it was interesting to note that SpHyastatin acted only on the cell membrane of S. aureus and P. pastoris and thus shared a similar cell-killing mechanism to magainin II that kills E. coli via permeabilizing the cell membrane without penetrating it ( Matsuzaki, 1998 ). Sphistin, the N-terminus of crab histone H2A, also induces microbial cell death solely by permeabilizing target membrane other than penetrating cell membrane ( Chen et al, 2015 ). Obviously, the binding positions of SpHyastatin on the tested microbial cells were distinct among S. aureus , P. fluorescens and P. pastoris , whereas P. fluorescens exhibited a lower degree of cell rupture than S. aureus and P. pastoris ( Figure 5 ).…”

Section: Discussionmentioning

confidence: 99%

The New Antimicrobial Peptide SpHyastatin from the Mud Crab Scylla paramamosain with Multiple Antimicrobial Mechanisms and High Effect on Bacterial Infection

Shan¹,

Zhu²,

Peng³

et al. 2016

Front. Microbiol.

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SpHyastatin was first identified as a new cationic antimicrobial peptide in hemocytes of the mud crab Scylla paramamosain. Based on the amino acid sequences deduced, it was predicted that this peptide was composed of two different functional domains, a proline-rich domain (PRD) and a cysteine-rich domain (CRD). The recombinant product of SpHyastatin displayed potent antimicrobial activities against the human pathogen Staphylococcus aureus and the aquatic animal pathogens Aeromonas hydrophila and Pseudomonas fluorescens. Compared with the CRD of SpHyastatin, the PRD presented better antimicrobial and chitin binding activities, but both regions were essential for allowing SpHyastatin complete antimicrobial activity. The binding properties of SpHyastatin to different microbial surface molecules suggested that this might be an initial and crucial step for performing its antimicrobial activities. Evaluated using propidium iodide uptake assays and scanning electron microscopy images, the antimicrobial mechanism of SpHyastatin was found to be prone to disrupt cell membrane integrity. Interestingly, SpHyastatin exerted its role specifically on the surface of S. aureus and Pichia pastoris whereas it directly killed P. fluorescens through simultaneous targeting the membrane and the cytoplasm, indicating that SpHyastatin could use different antimicrobial mechanisms to kill different species of microbes. As expected, the recombinant SpHyastatin increased the survival rate of crabs challenged with Vibrio parahaemolyticus. In addition, SpHyastatin could modulate some V. parahaemolyticus-responsive genes in S. paramamosain.

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“…As part of the ongoing effort to support and enhance the aquaculture of Scylla species, much work has focused on understanding the biology of these crabs (e.g., Bao et al, 2015;Chen et al, 2015;Girish et al, 2015;Gong et al, 2015;Huang et al, 2014Huang et al, , 2015Ikhwanuddin et al, 2014;Kornthong et al, 2014;Sun et al, 2015;Wang et al, 2015aWang et al, , 2015bXie et al, 2014;Zeng et al, 2016;Zhao et al, 2015). One outcome of these studies has been the development of extensive transcriptomic resources for several Scylla species (e.g., Bao et al, 2015;Kornthong et al, 2014;Ma et al, 2014;Xie et al, 2014), including S. olivacea, for which approximately 160,000 transcriptome shotgun assembly (TSA) sequences are now available in GenBank (e.g., BioProject Accession No.…”

Section: Introductionmentioning

confidence: 99%

Prediction of Scylla olivacea (Crustacea; Brachyura) peptide hormones using publicly accessible transcriptome shotgun assembly (TSA) sequences

Christie

2016

General and Comparative Endocrinology

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The aquaculture of crabs from the genus Scylla is of increasing economic importance for many Southeast Asian countries. Expansion of Scylla farming has led to increased efforts to understand the physiology and behavior of these crabs, and as such, there are growing molecular resources for them. Here, publicly accessible Scylla olivacea transcriptomic data were mined for putative peptide-encoding transcripts; the proteins deduced from the identified sequences were then used to predict the structures of mature peptide hormones. Forty-nine pre/preprohormone-encoding transcripts were identified, allowing for the prediction of 187 distinct mature peptides. The identified peptides included isoforms of adipokinetic hormone-corazonin-like peptide, allatostatin A, allatostatin B, allatostatin C, bursicon β, CCHamide, corazonin, crustacean cardioactive peptide, crustacean hyperglycemic hormone/molt-inhibiting hormone, diuretic hormone 31, eclosion hormone, FMRFamide-like peptide, HIGSLYRamide, insulin-like peptide, intocin, leucokinin, myosuppressin, neuroparsin, neuropeptide F, orcokinin, pigment dispersing hormone, pyrokinin, red pigment concentrating hormone, RYamide, short neuropeptide F, SIFamide and tachykinin-related peptide, all well-known neuropeptide families. Surprisingly, the tissue used to generate the transcriptome mined here is reported to be testis. Whether or not the testis samples had neural contamination is unknown. However, if the peptides are truly produced by this reproductive organ, it could have far reaching consequences for the study of crustacean endocrinology, particularly in the area of reproductive control. Regardless, this peptidome is the largest thus far predicted for any brachyuran (true crab) species, and will serve as a foundation for future studies of peptidergic control in members of the commercially important genus Scylla.

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Mechanism study on a new antimicrobial peptide Sphistin derived from the N-terminus of crab histone H2A identified in haemolymphs of Scylla paramamosain

Cited by 54 publications

References 76 publications

Histone H5 is a potent Antimicrobial Agent and a template for novel Antimicrobial Peptides

Histone H5 is a potent Antimicrobial Agent and a template for novel Antimicrobial Peptides

The New Antimicrobial Peptide SpHyastatin from the Mud Crab Scylla paramamosain with Multiple Antimicrobial Mechanisms and High Effect on Bacterial Infection

Prediction of Scylla olivacea (Crustacea; Brachyura) peptide hormones using publicly accessible transcriptome shotgun assembly (TSA) sequences

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