Distribution of MACPF/CDC Proteins

Anderluh, Gregor; Kisovec, Matic; Kraševec, Nada; Gilbert, R.J.C.

doi:10.1007/978-94-017-8881-6_2

Cited by 41 publications

(38 citation statements)

References 105 publications

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“…shows alignments and phylogenetical relations of NigA1 and NigA2 aegerolysin proteins to at least partly functionally studied fungal aegerolysins. MACPF‐like proteins have low sequence identity (< 20%) and high numbers of introns coded in their genes (Anderluh et al ., ). Both proteins, NigB1 and NigB2, were confirmed by having MACPF‐like signature (Y/F‐G‐X 2 ‐F/Y‐X 6 ‐G‐G) in protein models generated using MACPF/CDC proteins as templates.…”

Section: Resultsmentioning

confidence: 97%

“…The family of proteins with membrane-attack-complex/ perforin (MACPF) domain (PF01823) is a large protein family containing proteins from all kingdom of life, among which the animal-derived MACPF proteins are prevailing (Gilbert et al, 2013). While roles of MACPF proteins in the producing organisms are generally well-defined, roles of fungal MACPF-like proteins that represent only a smaller group of approximately 200 proteins, remain to be elucidated (Anderluh et al, 2014;Ota et al, 2014). The only MACPF-like protein from genus Aspergillus described to date is SpoC1-C1C protein from Aspergillus nidulans that was highly expressed during later stages of sporulation and in spores (Stephens et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

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Functional studies of aegerolysin and MACPF‐like proteins in Aspergillus niger

Novak

Čepin

Hodnik

et al. 2019

Molecular Microbiology

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Summary Proteins of the aegerolysin family have a high abundance in Fungi. Due to their specific binding to membrane lipids, and their membrane‐permeabilization potential in concert with protein partner(s) belonging to a membrane‐attack‐complex/perforin (MACPF) superfamily, they were proposed as useful tools in different biotechnological and biomedical applications. In this work, we performed functional studies on expression of the genes encoding aegerolysin and MACPF‐like proteins in Aspergillus niger. Our results suggest the sporulation process being crucial for strong induction of the expression of all these genes. However, deletion of either of the aegerolysin genes did not influence the growth, development, sporulation efficiency and phenotype of the mutants, indicating that aegerolysins are not key factors in the sporulation process. In all our expression studies we noticed a strong correlation in the expression of one aegerolysin and MACPF‐like gene. Aegerolysins were confirmed to be secreted from the fungus. We also showed the specific interaction of a recombinant A. niger aegerolysin with an invertebrate‐specific membrane sphingolipid. Moreover, using this protein labelled with mCherry we successfully stained insect cells membranes containing this particular sphingolipid. Our combined results suggest, that aegerolysins in this species, and probably also in other aspergilli, could be involved in defence against predators.

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Section: Resultsmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Functional studies of aegerolysin and MACPF‐like proteins in Aspergillus niger

Novak

Čepin

Hodnik

et al. 2019

Molecular Microbiology

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“…Although the overall fold of the MACPF domain is conserved, there are substantial differences between specific cases such as in the degree of bending of the central β-sheet, the lengths and positions of the TMHs, etc. The sequences of MACPF domain proteins vary greatly among different species, with the only identified signature motif being a Y(F)-G-T(S)-H-X 7 -G-G motif (where X is any amino acid), which maps to one of the central β-strands [1,5] (figure 1 a,b ). Interestingly, a highly conserved tryptophan following a tandem glycine motif (GGX n W) is identified among the MACPF domains involved in pore formation, but is absent in development-related MACPF domains (such as astrotactins (ASTNs), Torso-like (Tsl) and bone morphogenetic protein and retinoic acid-induced neural-specific proteins (BRINPs)) (figure 1 a,b ).…”

Section: Structure Of Membrane Attack Complex/perforin Proteins and Mmentioning

confidence: 99%

Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms

Tien

Gilbert

2017

Phil. Trans. R. Soc. B

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Pore-forming proteins play critical roles in pathogenic attack and immunological defence. The membrane attack complex/perforin (MACPF) group of homologues represents, with cholesterol-dependent cytolysins, the largest family of such proteins. In this review, we begin by describing briefly the structure of MACPF proteins, outlining their common mechanism of pore formation. We subsequently discuss some examples of MACPF proteins likely implicated in pore formation or other membrane-remodelling processes. Finally, we focus on astrotactin and bone morphogenetic protein and retinoic acid-induced neural-specific proteins, highly conserved MACPF family members involved in developmental processes, which have not been well studied to date or observed to form a pore—and which data suggest may act by alternative mechanisms.This article is part of the themed issue ‘Membrane pores: from structure and assembly, to medicine and technology’.

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“…The cholesterol-dependent cytolysin (CDC) family is the largest family of bacterial pore-forming toxins and belongs to the MACPF (Membrane Attack Complex and Perforin)/CDC superfamily, which also comprises eukaryotic pore-forming proteins (Anderluh et al, 2014). CDCs are major virulence factors that generally recognize membrane cholesterol as their binding receptor and are used by pathogenic bacteria to exert multiple functions during infection.…”

Section: Defensin-susceptible Bacterial Toxins/effector Proteinsmentioning

confidence: 99%

Targeting and inactivation of bacterial toxins by human defensins

Kudryashova

Seveau

Kudryashov

2017

Biological Chemistry

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Defensins as a prominent family of antimicrobial peptides (AMP) are major effectors of the innate immunity with a broad range of immune modulatory and antimicrobial activities. Particularly, defensins are the only recognized fast-response molecules that can neutralize a broad range of bacterial toxins, many of which are among the deadliest compounds on the planet. For a decade, the mystery of how a small and structurally conserved group of peptides can neutralize a heterogeneous group of toxins with little to no sequential and structural similarity remained unresolved. Recently, it was found that defensins recognize and target structural plasticity/thermodynamic instability, fundamental physicochemical properties that unite many bacterial toxins and distinguish them from the majority of host proteins. Binding of human defensins promotes local unfolding of the affected toxins, destabilizes their secondary and tertiary structures, increases susceptibility to proteolysis, and leads to their precipitation. While the details of toxin destabilization by defensins remain obscure, here we briefly review properties and activities of bacterial toxins known to be affected by or to be resilient to defensins and discuss how recognized features of defensins correlate with the observed inactivation.

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Distribution of MACPF/CDC Proteins

Cited by 41 publications

References 105 publications

Functional studies of aegerolysin and MACPF‐like proteins in Aspergillus niger

Functional studies of aegerolysin and MACPF‐like proteins in Aspergillus niger

Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms

Targeting and inactivation of bacterial toxins by human defensins

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