Antimicrobial peptides in the centipede Scolopendra subspinipes mutilans

@article{Yoo2014AntimicrobialPI,
  title={Antimicrobial peptides in the centipede Scolopendra subspinipes mutilans},
  author={Won Gi Yoo and Joon-Ha Lee and Younhee Shin and J Y Shim and Myunghee Jung and Byeong-chul Kang and Jae-Don Oh and Jiyeon Seong and Hak Koy Lee and Hong Sik Kong and Ki-Duk Song and Eun‐Young Yun and In-woo Kim and Young Nam Kwon and Dong Gun Lee and Ui Wook Hwang and Junhyung Park and Jae‐Sam Hwang},
  journal={Functional \& Integrative Genomics},
  year={2014},
  volume={14},
  pages={275-283}
}
The centipede Scolopendra subspinipes mutilans is an environmentally beneficial and medically important arthropod species. Although this species is increasingly applied as a reliable source of new antimicrobial peptides, the transcriptome of this species is a prerequisite for more rational selection of antimicrobial peptides. In this report, we isolated total RNA from the whole body of adult centipedes, S. subspinipes mutilans, that were nonimmunized and immunized against Escherichia coli, and… 
Scolopendrasin I: a novel antimicrobial peptide isolated from the centipede Scolopendra subspinipes mutilans
TLDR
Evidence is provided that this is an efficient strategy for antimicrobial peptide candidate identification and that Scolopendrasin I has potential for successful antibiotic development.
Antimicrobial Activity of the Scolopendrasin V Peptide Identified from the Centipede Scolopendra subspinipes mutilans.
TLDR
It is found that scolopendrasin V's mechanism of action involved binding to the surface of microorganisms via a specific interaction with lipopolysaccharides, lipoteichoic acid, and peptidoglycans, which are components of the bacterial membrane, which provide a basis for developing peptide antibiotics.
Uncovering Antimicrobial Peptide from Zophobas atratus Using Transcriptome Analysis
TLDR
The immunization of Zophobas atratus with Escherichia coli, Staphylococcus aureus, Candida albicans and total RNA was isolated and sequenced provides an insight in Zophoba atRatus transcriptome derived AMPs and understanding its antimicrobial activity.
Antimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipes
TLDR
The data suggest that Pinipesin might be part of a prophylactic immune response during the ecdysis process of centipedes, a promising candidate for the development of non-conventional antibiotics that could help fight infectious diseases and represents an exciting discovery for this taxon.
De Novo Transcriptome Analysis and Detection of Antimicrobial Peptides of the American Cockroach Periplaneta americana (Linnaeus)
TLDR
This work provides prerequisite baseline data for the identification and development of novel antimicrobial peptides, which is expected to provide a better understanding of the phenomenon of innate immunity in similar species.
Anticancer Activity of the Antimicrobial Peptide Scolopendrasin VII Derived from the Centipede, Scolopendra subspinipes mutilans.
TLDR
The results indicated that scolopendrasin VII induced necrotic cell death in leukemia cells, probably through interaction with phosphatidylserine, which is enriched in the membrane of cancer cells.
The transcriptome analysis of Protaetia brevitarsis Lewis larvae
TLDR
These data are the first reported whole transcriptome sequence of P. brevitarsis larvae, which represents a valuable genomic resource for studying this species, thus promoting the utilization of its medical potential.
Recombinant Production and Characterization of a New Toxin from Cryptops iheringi Centipede Venom Revealed by Proteome and Transcriptome Analysis
TLDR
A transcriptomic characterization of the Cryptops iheringi venom gland and a proteomic analysis of its venom indicated that 57.9% of the sequences showed to be putative toxins unknown in public databases; among them, a novel putative toxin named Cryptoxin-1 was pointed out.
...
...

References

SHOWING 1-10 OF 45 REFERENCES
Induction, purification and characterization of an antibacterial peptide scolopendrin I from the venom of centipede Scolopendra subspinipes mutilans.
The crude venom of the centipede Scolopendra subspinipes mutilans, injected with Escherichia coli K12D31 for 3-4 days showed broad-spectrum antimicrobial activity against Gram-positive. Gram-negative
Two novel antimicrobial peptides from centipede venoms.
Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases
TLDR
Data suggest that aureolysin production by S. aureus contributes to the resistance of this pathogen to the innate immune system of humans mediated by LL-37.
APD2: the updated antimicrobial peptide database and its application in peptide design
TLDR
Using frequently occurring residues, database-aided peptide design in different ways is demonstrated, and GLK-19 showed a higher activity against Escherichia coli than human LL-37 and Leu, Ala, Gly and Lys in amphibian peptides.
A theoretical approach to spot active regions in antimicrobial proteins
TLDR
A theoretical approach that predicts antimicrobial proteins from their amino acid sequence in addition to determining their antimicrobial regions can also predict their key active regions, making this a tool for the design of new antimicrobial drugs.
Mechanisms of Antimicrobial Peptide Action and Resistance
TLDR
The intention of this review is to illustrate the contemporary structural and functional themes among mechanisms of antimicrobial peptide action and resistance.
BACTIBASE second release: a database and tool platform for bacteriocin characterization
TLDR
Improvements brought to BACTIBASE include incorporation of various tools for bacteriocin analysis, such as homology search, multiple sequence alignments, Hidden Markov Models, molecular modelling and retrieval through the taxonomy Browser.
Anti‐microbial peptides: from invertebrates to vertebrates
TLDR
This review focuses on AMPs forming α‐helices, β‐hairpin‐like β‐sheets, α‐helix/β‐sheet mixed structures from invertebrate and vertebrate origins, which show some promise for therapeutic use.
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
TLDR
In this review the different models of antimicrobial-peptide-induced pore formation and cell killing are presented and several observations suggest that translocated peptides can alter cytoplasmic membrane septum formation, inhibit cell-wall synthesis, inhibit nucleic-acid synthesis, inhibits protein synthesis or inhibit enzymatic activity.
...
...