Dataset Information

Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo dragon) by Large Scale Analyses and De Novo Assisted Sequencing using Electron Transfer Dissociation Mass Spectrometry

ABSTRACT: We have employed a custom bioprospecing approach to identify cationic antimicrobial peptides from Komodo dragon plasma. Through these analyses we identified forty eight novel potential cationic antimicrobial peptides, with all but one of the identified peptides being derived from histone proteins. The antimicrobial effectiveness of eight of these peptides was evaluated against Pseudomonas aeruginosa 9027 and Staphylococcus aureus 25983, with seven peptides exhibiting antimicrobial activity against both microbes, and one only showing significant potency against Pseudomonas aeruginosa 9027. This study demonstrates the power and promise of our bioprospecting approach to CAMP discovery and it reveals the presence of a plethora of novel histone-derived antimicrobial peptides in the plasma of the dragon. These findings may have broader implications regarding the role that intact histones and histone-derived peptides play in defending the host from infection.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Varanus Komodoensis

TISSUE(S): Blood Plasma

SUBMITTER: Barney Bishop

LAB HEAD: Barney Bishop

PROVIDER: PXD005043 | Pride | 2017-02-08

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Sample220_Komodo_Unchallenged.mgf	Mgf
	Sample220_Komodo_Unchallenged.mzXML	Mzxml
	Sample220_Komodo_Unchallenged.raw	Raw
	Sample220_PEAKS63.mzid	Mzid
	Sample222_Komodo_LPS.mgf	Mgf

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Publications

Discovery of Novel Antimicrobial Peptides from Varanus komodoensis (Komodo Dragon) by Large-Scale Analyses and De-Novo-Assisted Sequencing Using Electron-Transfer Dissociation Mass Spectrometry.

Bishop Barney M BM Juba Melanie L ML Russo Paul S PS Devine Megan M Barksdale Stephanie M SM Scott Shaylyn S Settlage Robert R Michalak Pawel P Gupta Kajal K Vliet Kent K Schnur Joel M JM van Hoek Monique L ML

Journal of proteome research 20170224 4

Komodo dragons are the largest living lizards and are the apex predators in their environs. They endure numerous strains of pathogenic bacteria in their saliva and recover from wounds inflicted by other dragons, reflecting the inherent robustness of their innate immune defense. We have employed a custom bioprospecting approach combining partial de novo peptide sequencing with transcriptome assembly to identify cationic antimicrobial peptides from Komodo dragon plasma. Through these analyses, we ...[more]

PMID: 28164707

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Project description:Antimicrobial peptides (AMPs) constitute a broad range of bioactive compounds in diverse organisms, including fish. They are effector molecules for the innate immune response, against pathogens, tissue damage and infections. Still, AMPs from African Catfish, Clarias gariepinus skin mucus are largely unexplored despite their possible therapeutic role in combating antimicrobial resistance. In this study, African Catfish Antimicrobial peptides (ACAPs) were identified from the skin mucus of African Catfish, C. gariepinus. Native peptides were extracted from fish mucus scrapings in 10% acetic acid (v/v) and ultra-filtered using 5kDa molecular cut-off membrane. The extract was purified using C18 Solid Phase Extraction. The antibacterial activity was determined using the Agar Well Diffusion method and broth-dilution method utilizing Staphylococcus aureus (ATCC 25923) and Escherichia coli (ATCC 25922). Thereafter, Sephadex G-25 gel filtration was further utilized in bio-guided isolation of the most active fractions prior to peptide identification using Orbitrap Fusion Lumos Tribrid Mass Spectrometry. The skin mucus extracted from African Catfish from all the three major lakes of Uganda exhibited antimicrobial activity on E. coli and S. aureus. Lake Albert’s C. gariepinus demonstrated the best activity with the lowest MIC of 2.84 µg/mL and 0.71 µg/mL on S. aureus and E. coli respectively. Sephadex G-25 peak I mass spectrometry analysis alongside in silico analysis revealed seven short peptides (11-15 amino acid residues) of high antimicrobial scores (0.561-0.905 units). In addition, these peptides had a low molecular weight (1005.57-1622.05 Da), and had percentage hydrophobicity above 54%. Up to four of these antimicrobial peptides demonstrated α-helix structure conformation, rendering them amphipathic. The ﬁndings of this study indicate that novel antimicrobial peptides can be sourced from the skin mucus of C. gariepinus. Such antimicrobial peptides are potential alternatives to the traditional antibiotics and can be of great application to food and pharmaceutical industries; however, further studies are still needed to establish their drug-likeness and safety profiles.