Isolation and characterization of a novel two-component hemolysin, erylysin A and B, from an edible mushroom, Pleurotus eryngii

Shibata, Toshihiro; Kudou, M; Hoshi, Yoshinobu; Kudo, Ayako; Nanashima, Naoki; Miyairi, Kazuo

doi:10.1016/j.toxicon.2010.08.010

Cited by 35 publications

(24 citation statements)

References 20 publications

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“…Only the crystal structure of the bacterial aegerolysin Cry34A (from Bacillus thuringiensis) has been determined to date (Schnepf 2013;Schnepf et al 2005). This solved structure confirmed previous experimental Nayak et al 2011a;Shibata et al 2010) and prediction data, all of which argued that the aegerolysins are β-structured proteins (Berne et al 2009;Ota et al 2014).…”

Section: Introductionsupporting

confidence: 68%

“…aegerita and recombinant terrelysin from Aspergillus terreus have been suggested to be hemolytic (Berne et al 2002;Nayak et al 2011a). On the contrary, OlyA, pleurotolysin A (PlyA), and erylysin A (EryA), which are aegerolysins from Pleurotus spp., are not hemolytically active per se, as each functions as part of the bi-component pore-forming proteins that include pleurotolysin B (PlyB) and erylysin B (EryB), respectively, which belong to the family of proteins with a membrane attack complex/ perforin (MACPF) domain Gilbert et al 2013;Ota et al 2013;Shibata et al 2010;Tomita et al 2004). As well as having hemolytic activity, OlyA (or an isoformic PlyA) and its partnering protein (PlyB, with the MACPF domain) can also form pores in lipid vesicles composed of either total erythrocyte lipids or sphingomyelin and cholesterol (Ota et al 2013;Sepčić et al 2004;Tomita et al 2004).…”

Section: Activities Of the Aegerolysin Proteinsmentioning

confidence: 99%

See 1 more Smart Citation

Fungal aegerolysin-like proteins: distribution, activities, and applications

Novak

Kraševec

Skočaj

et al. 2014

Appl Microbiol Biotechnol

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The aegerolysin protein family (from aegerolysin of the mushroom Agrocybe aegerita) comprises proteins of ∼15-20 kDa from various eukaryotic and bacterial taxa. Aegerolysins are inconsistently distributed among fungal species, and variable numbers of homologs have been reported for species within the same genus. As such noncore proteins, without a member of a protein family in each of the sequenced fungi, they can give insight into different species-specific processes. Some aegerolysins have been reported to be hemolytically active against mammalian erythrocytes. However, some function as bi-component proteins that have membrane activity in concert with another protein that contains a membrane attack complex/perforin domain. The function of most of aegerolysins is unknown, although some have been suggested to have a role in development of the organism. Potential biotechnological applications of aegerolysins are already evident, despite the limited scientific knowledge available at present. Some mushroom aegerolysins, for example, can be used as markers to detect and label specific membrane lipids. Others can be used as biomarkers of fungal exposure, where their genes can serve as targets for detection of fungi and their progression during infectious diseases. Antibodies against aegerolysins can also be raised as immuno-diagnostic tools. Aegerolysins have been shown to serve as a species determination tool for fungal phytopathogen isolates in terms of some closely related species, where commonly used internal transcribed spacer barcoding has failed. Moreover, strong promoters that regulate aegerolysin genes can promote secretion of heterologous proteins from fungi and have been successfully applied in simultaneous multi-gene expression techniques.

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Section: Introductionsupporting

confidence: 68%

Section: Activities Of the Aegerolysin Proteinsmentioning

confidence: 99%

Fungal aegerolysin-like proteins: distribution, activities, and applications

Novak

Kraševec

Skočaj

et al. 2014

Appl Microbiol Biotechnol

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“…However, detailed characterization of PlyA has not yet been performed. Recently, erylysin (Ery), an ortholog of Oly, was isolated from Pleurotus eryngii ( 25 ). Similar to Ply, Ery is a two-component hemolysin composed of EryA and EryB.…”

Section: Construction Expression and Purifi Cation Of Recombinant Pmentioning

confidence: 99%

“…Therefore, we examined the effect of PlyA2-EGFP preincubation with liposomes on cell surface staining (Oly) (80% identity). EryA and Oly share a high degree of sequence identity (98%) ( 25 ).…”

Section: Measurement Of Hemolysismentioning

confidence: 99%

Binding of a pleurotolysin ortholog from Pleurotus eryngii to sphingomyelin and cholesterol-rich membrane domains

Bhat

Kishimoto

Abe

et al. 2013

Journal of Lipid Research

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“…Pleurotolysin proteins are two-component hemolysins, which require the interaction of both of the two non-homologous components, Pleurotolysin A and Pleurotolysin B, to exhibit strong cytolytic activity [Ota et al, 2014; Shibata et al, 2010]. Cooperative pore formation causes leakage of potassium ions from cells and subsequent colloid-osmotic hemolysis [Tomita et al, 2004], and like perforins, pleurotolysins can deliver cationic macromolecules such as granzymes [Stewart et al, 2014].…”

Section: Introductionmentioning

confidence: 99%

The Membrane Attack Complex/Perforin Superfamily

Moreno–Hagelsieb

Vitug²,

Medrano-Soto³

et al. 2017

Microb Physiol

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The membrane attack complex/perforin (MACPF) superfamily consists of a diverse group of proteins involved in bacterial pathogenesis and sporulation as well as eukaryotic immunity, embryonic development, neural migration and fruiting body formation. The present work shows that the evolutionary relationships between the members of the superfamily, previously suggested by comparison of their tertiary structures, can also be supported by analyses of their primary structures. The superfamily includes the MACPF family (TC 1.C.39), the cholesterol-dependent cytolysin (CDC) family (TC 1.C.12.1 and 1.C.12.2) and the pleurotolysin pore-forming (pleurotolysin B) family (TC 1.C.97.1), as revealed by expansion of each family by comparison against a large protein database, and by the comparisons of their hidden Markov models. Clustering analyses demonstrated grouping of the CDC homologues separately from the 12 MACPF subfamilies, which also grouped separately from the pleurotolysin B family. Members of the MACPF superfamily revealed a remarkably diverse range of proteins spanning eukaryotic, bacterial, and archaeal taxonomic domains, with notable variations in protein domain architectures. Our strategy should also be helpful in putting together other highly divergent protein families.

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Isolation and characterization of a novel two-component hemolysin, erylysin A and B, from an edible mushroom, Pleurotus eryngii

Cited by 35 publications

References 20 publications

Fungal aegerolysin-like proteins: distribution, activities, and applications

Fungal aegerolysin-like proteins: distribution, activities, and applications

Binding of a pleurotolysin ortholog from Pleurotus eryngii to sphingomyelin and cholesterol-rich membrane domains

The Membrane Attack Complex/Perforin Superfamily

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