Nematode-derived drosomycin-type antifungal peptides provide evidence for plant-to-ecdysozoan horizontal transfer of a disease resistance gene

Zhu, Shunyi; Gao, Bin

doi:10.1038/ncomms4154

Cited by 24 publications

(37 citation statements)

References 51 publications

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“…However, all 15 cremycins have only six cysteines (instead of the eight found in drosomycin), and their spacing is consistent with insect defensins (Fig. 1a; Additional file 1: Figure S1) [21]. Long-chain scorpion toxins, such as from Centruroides sculpturatus, also have additional cysteines corresponding to C1 and C10 that form a fourth disulfide bond, but the sequence spacing is characterized by a long C-terminal extension between C9 and C10 that is not present in drosomycin and plant defensins (Fig.…”

Section: Resultsmentioning

confidence: 86%

“…Other than the drosomycin family in Drosophila and plant defensins, only one nematode sequence seems consistent with this spacing (NEMBASE: PSC02929). Zhu and Gao reported a family of drosomycin-type antifungal peptides (DTAFPs) from Caenorhabditis remanei called “cremycins” [21]. However, all 15 cremycins have only six cysteines (instead of the eight found in drosomycin), and their spacing is consistent with insect defensins (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The sponge ASABF-like peptide has activity against Gram-positive and Gram-negative bacteria, fungi, yeast, and is hemolytic [36]. Antimicrobial activity has been tested for two of the fifteen cremycins, reported to be drosomycin-type antifungal peptides: cremycin-5 showed antifungal activity, but cremycin-15 showed antibacterial activity without any antifungal activity [21]. …”

Section: Resultsmentioning

confidence: 99%

“…The clearest demonstration of the inconsistent and confusing nomenclature is the cremycins from Caenorhabditis remanei. These peptides are described as drosomycin-like antifungal peptides, but their sequences are not particularly drosomycin-like and only one of the two tested (of 15 total) has antifungal activity [21]. To further confuse the nomenclature, invertebrate big defensins are not part of the CS-αβ superfamily, but are more likely related to vertebrate defensins [22].…”

Section: Introductionmentioning

confidence: 99%

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Establishing a reference array for the CS-αβ superfamily of defensive peptides

Tarr

2016

BMC Res Notes

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Background“Invertebrate defensins” belong to the cysteine-stabilized alpha-beta (CS-αβ), also known as the scorpion toxin-like, superfamily. Some other peptides belonging to this superfamily of defensive peptides are indistinguishable from “defensins,” but have been assigned other names, making it unclear what, if any, criteria must be met to qualify as an “invertebrate defensin.” In addition, there are other groups of defensins in invertebrates and vertebrates that are considered to be evolutionarily unrelated to those in the CS-αβ superfamily. This complicates analyses and discussions of this peptide group. This paper investigates the criteria for classifying a peptide as an invertebrate defensin, suggests a reference cysteine array that may be helpful in discussing peptides in this superfamily, and proposes that the superfamily (rather than the name “defensin”) is the appropriate context for studying the evolution of invertebrate defensins with the CS-αβ fold.MethodsCS-αβ superfamily sequences were identified from previous literature and BLAST searches of public databases. Sequences were retrieved from databases, and the relevant motifs were identified and used to create a conceptual alignment to a ten-cysteine reference array. Amino acid sequences were aligned in MEGA6 with manual adjustments to ensure accurate alignment of cysteines. Phylogenetic analyses were performed in MEGA6 (maximum likelihood) and MrBayes (Bayesian).ResultsAcross invertebrate taxa, the term “defensin” is not consistently applied based on number of cysteines, cysteine spacing pattern, spectrum of antimicrobial activity, or phylogenetic relationship. The analyses failed to reveal any criteria that unify “invertebrate defensins” and differentiate them from other defensive peptides in the CS-αβ superfamily. Sequences from various groups within the CS-αβ superfamily of defensive peptides can be described by a ten-cysteine reference array that aligns their defining structural motifs.ConclusionsThe proposed ten-cysteine reference array can be used in addition to current nomenclature to compare sequences in the CS-αβ superfamily and clarify their features relative to one another. This will facilitate analysis and discussion of “invertebrate defensins” in an appropriate evolutionary context, rather than relying on nomenclature.Electronic supplementary materialThe online version of this article (doi:10.1186/s13104-016-2291-0) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 86%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Establishing a reference array for the CS-αβ superfamily of defensive peptides

Tarr

2016

BMC Res Notes

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“…These cases include insect drosomycins and nematode cremycins, which are probably acquired from plants (Zhu & Gao, 2014). The Alo-3 sequence, which is an antifungal peptide found in many plants Kenig and Reading (1979) TA B L E 1 Antibiotics produced by Streptomyces clavuligerus and in the animal kingdom only in the beetle Acrocinus longimanus (Barbault et al, 2003), is the product of an HGT event proposed to explain the presence of this gene in the beetle (Husnik et al, 2013).…”

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confidence: 99%

A putative antimicrobial peptide from Hymenoptera in the megaplasmid pSCL4 of Streptomyces clavuligerus ATCC 27064 reveals a singular case of horizontal gene transfer with potential applications

Ayala-Ruano

Santander-Gordón

Tejera

et al. 2019

Ecology and Evolution

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Streptomyces clavuligerus is a Gram‐positive bacterium that is a high producer of secondary metabolites with industrial applications. The production of antibiotics such as clavulanic acid or cephamycin has been extensively studied in this species; nevertheless, other aspects, such as evolution or ecology, have received less attention. Furthermore, genes that arise from ancient events of lateral transfer have been demonstrated to be implicated in important functions of host species. This approximation discovered relevant genes that genomic analyses overlooked. Thus, we studied the impact of horizontal gene transfer in the S. clavuligerus genome. To perform this task, we applied whole‐genome analysis to identify a laterally transferred sequence from different domains. The most relevant result was a putative antimicrobial peptide (AMP) with a clear origin in the Hymenoptera order of insects. Next, we determined that two copies of these genes were present in the megaplasmid pSCL4 but absent in the S. clavuligerus ATCC 27064 chromosome. Additionally, we found that these sequences were exclusive to the ATCC 27064 strain (and so were not present in any other bacteria) and we also verified the expression of the genes using RNAseq data. Next, we used several AMP predictors to validate the original annotation extracted from Hymenoptera sequences and explored the possibility that these proteins had post‐translational modifications using peptidase cleavage prediction. We suggest that Hymenoptera AMP‐like proteins of S. clavuligerus ATCC 27064 may be useful for both species adaptation and as an antimicrobial molecule with industrial applications.

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