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11 pages, 6709 KiB

Open AccessArticle

Amyloid Assembly Endows Gad m 1 with Biomineralization Properties

by Milagros Castellanos, Almudena Torres-Pardo, Rosa Rodríguez-Pérez and María Gasset

Biomolecules 2018, 8(1), 13; https://doi.org/10.3390/biom8010013 - 20 Mar 2018

Cited by 8 | Viewed by 5126

Abstract

Acid proteins capable of nucleating Ca²⁺ and displaying aggregation capacity play key roles in the formation of calcium carbonate biominerals. The helix-loop helix EF-hands are the most common Ca²⁺-binding motifs in proteins. Calcium is bound by the loop region. These [...] Read more.

Acid proteins capable of nucleating Ca²⁺ and displaying aggregation capacity play key roles in the formation of calcium carbonate biominerals. The helix-loop helix EF-hands are the most common Ca²⁺-binding motifs in proteins. Calcium is bound by the loop region. These motifs are found in many proteins that are regulated by calcium. Gad m 1, an Atlantic cod β-parvalbumin isoform, is a monomeric EF-hand protein that acts as a Ca²⁺ buffer in fish muscle; the neutral and acid apo-forms of this protein can form amyloids. Since Ca²⁺-nucleating proteins have a propensity to form extended β-strand structures, we wondered whether amyloid assemblies of an EF-hand protein were able to influence calcium carbonate crystallization in vitro. Here, we used the Gad m 1 chain as a model to generate monomeric and amyloid assemblies and to analyze their effect on calcite formation in vitro. We found that only amyloid assemblies alter calcite morphology. Full article

(This article belongs to the Special Issue Functional Amyloids)

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15 pages, 2742 KiB

Open AccessArticle

The Functional Amyloid Curli Protects Escherichia coli against Complement-Mediated Bactericidal Activity

by Steven G. Biesecker, Lauren K. Nicastro, R. Paul Wilson and Çağla Tükel

Biomolecules 2018, 8(1), 5; https://doi.org/10.3390/biom8010005 - 24 Jan 2018

Cited by 38 | Viewed by 7016

Abstract

Escherichia coli strains may be beneficial or pathogenic. Many E. coli strains that cause human disease, especially those responsible for bacteremia and sepsis, express virulence factors that impart resistance to the complement system. The bacterial amyloid curli functions in bacterial adherence and enhances [...] Read more.

Escherichia coli strains may be beneficial or pathogenic. Many E. coli strains that cause human disease, especially those responsible for bacteremia and sepsis, express virulence factors that impart resistance to the complement system. The bacterial amyloid curli functions in bacterial adherence and enhances the formation of biofilms. Survival of curli-producing parental and curli-deficient mutant E. coli in the context of a human complement response was evaluated using an in vivo murine model of bacteremia. Results showed that curli production enhanced E. coli survival, which suggests that curli defends against complement-mediated killing. This observation was supported by the results of in vitro assays comparing bacterial survival in human serum. Experiments in which the classical or alternative complement pathways were blocked indicated that the classical pathway is the major contributor to complement activation and that curli inhibits this activity. Our analyses indicate that curli does not appear to play a role in protecting E. coli against alternative pathway complement activation. We found that curli increases binding of E. coli cells to complement component Complement component 1q (C1q) but does not affect Complement component 3b (C3b) binding. We conclude that curli defends E. coli against complement-mediated killing via inhibition of the classical complement pathway. Full article

(This article belongs to the Special Issue Functional Amyloids)

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11293 KiB

Open AccessArticle

The Production of Curli Amyloid Fibers Is Deeply Integrated into the Biology of Escherichia coli

by Daniel R. Smith, Janet E. Price, Peter E. Burby, Luz P. Blanco, Justin Chamberlain and Matthew R. Chapman

Biomolecules 2017, 7(4), 75; https://doi.org/10.3390/biom7040075 - 31 Oct 2017

Cited by 52 | Viewed by 11830

Abstract

Curli amyloid fibers are the major protein component of the extracellular matrix produced by Enterobacteriaceae during biofilm formation. Curli are required for proper biofilm development and environmental persistence by Escherichia coli. Here, we present a complete and vetted genetic analysis of functional [...] Read more.

Curli amyloid fibers are the major protein component of the extracellular matrix produced by Enterobacteriaceae during biofilm formation. Curli are required for proper biofilm development and environmental persistence by Escherichia coli. Here, we present a complete and vetted genetic analysis of functional amyloid fiber biogenesis. The Keio collection of single gene deletions was screened on Congo red indicator plates to identify E. coli mutants that had defective amyloid production. We discovered that more than three hundred gene products modulated curli production. These genes were involved in fundamental cellular processes such as regulation, environmental sensing, respiration, metabolism, cell envelope biogenesis, transport, and protein turnover. The alternative sigma factors, σ^S and σ^E, had opposing roles in curli production. Mutations that induced the σ^E or Cpx stress response systems had reduced curli production, while mutant strains with increased σ^S levels had increased curli production. Mutations in metabolic pathways, including gluconeogenesis and the biosynthesis of lipopolysaccharide (LPS), produced less curli. Regulation of the master biofilm regulator, CsgD, was diverse, and the screen revealed several proteins and small RNAs (sRNA) that regulate csgD messenger RNA (mRNA) levels. Using previously published studies, we found minimal overlap between the genes affecting curli biogenesis and genes known to impact swimming or swarming motility, underlying the distinction between motile and sessile lifestyles. Collectively, the diversity and number of elements required suggest curli production is part of a highly regulated and complex developmental pathway in E. coli. Full article

(This article belongs to the Special Issue Functional Amyloids)

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11347 KiB

Open AccessArticle

Structure-Dependent Interfacial Properties of Chaplin F from Streptomyces coelicolor

by Mina Dokouhaki, Emma L. Prime, Andrew Hung, Greg G. Qiao, Li Day and Sally L. Gras

Biomolecules 2017, 7(3), 68; https://doi.org/10.3390/biom7030068 - 19 Sep 2017

Cited by 2 | Viewed by 4459

Abstract

Chaplin F (Chp F) is a secreted surface-active peptide involved in the aerial growth of Streptomyces. While Chp E demonstrates a pH-responsive surface activity, the relationship between Chp F structure, function and the effect of solution pH is unknown. Chp F peptides [...] Read more.

Chaplin F (Chp F) is a secreted surface-active peptide involved in the aerial growth of Streptomyces. While Chp E demonstrates a pH-responsive surface activity, the relationship between Chp F structure, function and the effect of solution pH is unknown. Chp F peptides were found to self-assemble into amyloid fibrils at acidic pH (3.0 or the isoelectric point (pI) of 4.2), with ~99% of peptides converted into insoluble fibrils. In contrast, Chp F formed short assemblies containing a mixture of random coil and β-sheet structure at a basic pH of 10.0, where only 40% of the peptides converted to fibrils. The cysteine residues in Chp F did not appear to play a role in fibril assembly. The interfacial properties of Chp F at the air/water interface were altered by the structures adopted at different pH, with Chp F molecules forming a higher surface-active film at pH 10.0 with a lower area per molecule compared to Chp F fibrils at pH 3.0. These data show that the pH responsiveness of Chp F surface activity is the reverse of that observed for Chp E, which could prove useful in potential applications where surface activity is desired over a wide range of solution pH. Full article

(This article belongs to the Special Issue Functional Amyloids)

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2818 KiB

Open AccessArticle

Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils

by Megan Garvey, Heath Ecroyd, Nicholas J. Ray, Juliet A. Gerrard and John A. Carver

Biomolecules 2017, 7(3), 67; https://doi.org/10.3390/biom7030067 - 12 Sep 2017

Cited by 22 | Viewed by 5915

Abstract

Amyloid fibril formation occurs from a wide range of peptides and proteins and is typically associated with a loss of protein function and/or a gain of toxic function, as the native structure of the protein undergoes major alteration to form a cross β-sheet [...] Read more.

Amyloid fibril formation occurs from a wide range of peptides and proteins and is typically associated with a loss of protein function and/or a gain of toxic function, as the native structure of the protein undergoes major alteration to form a cross β-sheet array. It is now well recognised that some amyloid fibrils have a biological function, which has led to increased interest in the potential that these so-called functional amyloids may either retain the function of the native protein, or gain function upon adopting a fibrillar structure. Herein, we investigate the molecular chaperone ability of α-crystallin, the predominant eye lens protein which is composed of two related subunits αA- and αB-crystallin, and its capacity to retain and even enhance its chaperone activity after forming aggregate structures under conditions of thermal and chemical stress. We demonstrate that both eye lens α-crystallin and αB-crystallin (which is also found extensively outside the lens) retain, to a significant degree, their molecular chaperone activity under conditions of structural change, including after formation into amyloid fibrils and amorphous aggregates. The results can be related directly to the effects of aging on the structure and chaperone function of α-crystallin in the eye lens, particularly its ability to prevent crystallin protein aggregation and hence lens opacification associated with cataract formation. Full article

(This article belongs to the Special Issue Functional Amyloids)

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1791 KiB

Open AccessArticle

Direct Identification of Functional Amyloid Proteins by Label-Free Quantitative Mass Spectrometry

by Heidi N. Danielsen, Susan H. Hansen, Florian-Alexander Herbst, Henrik Kjeldal, Allan Stensballe, Per H. Nielsen and Morten S. Dueholm

Biomolecules 2017, 7(3), 58; https://doi.org/10.3390/biom7030058 - 4 Aug 2017

Cited by 12 | Viewed by 6782

Abstract

Functional amyloids are important structural and functional components of many biofilms, yet our knowledge of these fascinating polymers is limited to a few examples for which the native amyloids have been isolated in pure form. Isolation of the functional amyloids from other cell [...] Read more.

Functional amyloids are important structural and functional components of many biofilms, yet our knowledge of these fascinating polymers is limited to a few examples for which the native amyloids have been isolated in pure form. Isolation of the functional amyloids from other cell components represents a major bottleneck in the search for new functional amyloid systems. Here we present a label-free quantitative mass spectrometry method that allows identification of amyloid proteins directly in cell lysates. The method takes advantage of the extreme structural stability and polymeric nature of functional amyloids and the ability of concentrated formic acid to depolymerize the amyloids. An automated data processing pipeline that provides a short list of amyloid protein candidates was developed based on an amyloid-specific sigmoidal abundance signature in samples treated with increasing concentrations of formic acid. The method was evaluated using the Escherichia coli curli and the Pseudomonas Fap system. It confidently identified the major amyloid subunit for both systems, as well as the minor subunit for the curli system. A few non-amyloid proteins also displayed the sigmoidal abundance signature. However, only one of these contained a sec-dependent signal peptide, which characterizes most of all secreted proteins, including all currently known functional bacterial amyloids. Full article

(This article belongs to the Special Issue Functional Amyloids)

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2060 KiB

Open AccessArticle

Metal Binding Properties of the N-Terminus of the Functional Amyloid Orb2

by Thalia H. Bajakian, Silvia A. Cervantes, Maria A. Soria, Maïwenn Beaugrand, Ji Yun Kim, Rachel J. Service and Ansgar B. Siemer

Biomolecules 2017, 7(3), 57; https://doi.org/10.3390/biom7030057 - 1 Aug 2017

Cited by 4 | Viewed by 4793

Abstract

The cytoplasmic polyadenylation element binding protein (CPEB) homologue Orb2 is a functional amyloid that plays a key regulatory role for long-term memory in Drosophila. Orb2 has a glutamine, histidine-rich (Q/H-rich) domain that resembles the Q/H-rich, metal binding domain of the Hpn-like protein [...] Read more.

The cytoplasmic polyadenylation element binding protein (CPEB) homologue Orb2 is a functional amyloid that plays a key regulatory role for long-term memory in Drosophila. Orb2 has a glutamine, histidine-rich (Q/H-rich) domain that resembles the Q/H-rich, metal binding domain of the Hpn-like protein (Hpnl) found in Helicobacter pylori. In the present study, we used chromatography and isothermal titration calorimetry (ITC) to show that the Q/H-rich domain of Orb2 binds Ni²⁺ and other transition metals ions with μM affinity. Using site directed mutagenesis, we show that several histidine residues are important for binding. In particular, the H61Y mutation, which was previously shown to affect the aggregation of Orb2 in cell culture, completely inhibited metal binding of Orb2. Finally, we used thioflavin T fluorescence and electron microscopy images to show that Ni²⁺ binding induces the aggregating of Orb2 into structures that are distinct from the amyloid fibrils formed in the absence of Ni²⁺. These data suggest that transition metal binding might be important for the function of Orb2 and potentially long-term memory in Drosophila. Full article

(This article belongs to the Special Issue Functional Amyloids)

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4360 KiB

Open AccessArticle

Sequence Identification, Recombinant Production, and Analysis of the Self-Assembly of Egg Stalk Silk Proteins from Lacewing Chrysoperla carnea

by Martin Neuenfeldt and Thomas Scheibel

Biomolecules 2017, 7(2), 43; https://doi.org/10.3390/biom7020043 - 13 Jun 2017

Cited by 7 | Viewed by 5206

Abstract

Egg stalk silks of the common green lacewing Chrysoperla carnea likely comprise at least three different silk proteins. Based on the natural spinning process, it was hypothesized that these proteins self-assemble without shear stress, as adult lacewings do not use a spinneret. To [...] Read more.

Egg stalk silks of the common green lacewing Chrysoperla carnea likely comprise at least three different silk proteins. Based on the natural spinning process, it was hypothesized that these proteins self-assemble without shear stress, as adult lacewings do not use a spinneret. To examine this, the first sequence identification and determination of the gene expression profile of several silk proteins and various transcript variants thereof was conducted, and then the three major proteins were recombinantly produced in Escherichia coli encoded by their native complementary DNA (cDNA) sequences. Circular dichroism measurements indicated that the silk proteins in aqueous solutions had a mainly intrinsically disordered structure. The largest silk protein, which we named ChryC1, exhibited a lower critical solution temperature (LCST) behavior and self-assembled into fibers or film morphologies, depending on the conditions used. The second silk protein, ChryC2, self-assembled into nanofibrils and subsequently formed hydrogels. Circular dichroism and Fourier transform infrared spectroscopy confirmed conformational changes of both proteins into beta sheet rich structures upon assembly. ChryC3 did not self-assemble into any morphology under the tested conditions. Thereby, through this work, it could be shown that recombinant lacewing silk proteins can be produced and further used for studying the fiber formation of lacewing egg stalks. Full article

(This article belongs to the Special Issue Functional Amyloids)

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7795 KiB

Open AccessArticle

Amyloid Fibrils from Hemoglobin

by Nadishka Jayawardena, Manmeet Kaur, Smitha Nair, Jenny Malmstrom, David Goldstone, Leonardo Negron, Juliet A. Gerrard and Laura J. Domigan

Biomolecules 2017, 7(2), 37; https://doi.org/10.3390/biom7020037 - 11 Apr 2017

Cited by 27 | Viewed by 9656

Abstract

Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and drug delivery, as nanowires, [...] Read more.

Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and drug delivery, as nanowires, hydrogels, and thin films. Amyloid fibrils have been prepared from many proteins, but there has been no definitive characterization of amyloid fibrils from hemoglobin to date. Here, nanofiber formation was carried out under denaturing conditions using solutions of apo-hemoglobin extracted from bovine waste blood. A characteristic amyloid fibril morphology was confirmed by transmission electron microscopy (TEM) and atomic force microscopy (AFM), with mean fibril dimensions of approximately 5 nm diameter and up to several microns in length. The thioflavin T assay confirmed the presence of β-sheet structures in apo-hemoglobin fibrils, and X-ray fiber diffraction showed the characteristic amyloid cross-β quaternary structure. Apo-hemoglobin nanofibers demonstrated high stability over a range of temperatures (−20 to 80 °C) and pHs (2–10), and were stable in the presence of organic solvents and trypsin, confirming their potential as nanomaterials with versatile applications. This study conclusively demonstrates the formation of amyloid fibrils from hemoglobin for the first time, and also introduces a cost-effective method for amyloid fibril manufacture using meat industry by-products. Full article

(This article belongs to the Special Issue Functional Amyloids)

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Review

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2337 KiB

Open AccessReview

Revealing Accessibility of Cryptic Protein Binding Sites within the Functional Collagen Fibril

by Cody L. Hoop, Jie Zhu, Ana Monica Nunes, David A. Case and Jean Baum

Biomolecules 2017, 7(4), 76; https://doi.org/10.3390/biom7040076 - 1 Nov 2017

Cited by 24 | Viewed by 6901

Abstract

Fibrillar collagens are the most abundant proteins in the extracellular matrix. Not only do they provide structural integrity to all of the connective tissues in the human body, but also their interactions with multiple cell receptors and other matrix molecules are essential to [...] Read more.

Fibrillar collagens are the most abundant proteins in the extracellular matrix. Not only do they provide structural integrity to all of the connective tissues in the human body, but also their interactions with multiple cell receptors and other matrix molecules are essential to cell functions, such as growth, repair, and cell adhesion. Although specific binding sequences of several receptors have been determined along the collagen monomer, processes by which collagen binding partners recognize their binding sites in the collagen fibril, and the critical driving interactions, are poorly understood. The complex molecular assembly of bundled triple helices within the collagen fibril makes essential ligand binding sites cryptic or hidden from the molecular surface. Yet, critical biological processes that require collagen ligands to have access to interaction sites still occur. In this contribution, we will discuss the molecular packing of the collagen I fibril from the perspective of how collagen ligands access their known binding regions within the fibril, and we will present our analysis of binding site accessibility from the fibril surface. Understanding the basis of these interactions at the atomic level sets the stage for developing drug targets against debilitating collagen diseases and using collagen as drug delivery systems and new biomaterials. Full article

(This article belongs to the Special Issue Functional Amyloids)

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1053 KiB

Open AccessReview

Why are Functional Amyloids Non-Toxic in Humans?

by Matthew P. Jackson and Eric W. Hewitt

Biomolecules 2017, 7(4), 71; https://doi.org/10.3390/biom7040071 - 22 Sep 2017

Cited by 68 | Viewed by 8776

Abstract

Amyloids were first identified in association with amyloidoses, human diseases in which proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an array of functional amyloid fibrils that perform physiological roles in humans. Given the potential for the production of toxic [...] Read more.

Amyloids were first identified in association with amyloidoses, human diseases in which proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an array of functional amyloid fibrils that perform physiological roles in humans. Given the potential for the production of toxic species in amyloid assembly reactions, it is remarkable that cells can produce these functional amyloids without suffering any obvious ill effect. Although the precise mechanisms are unclear, there are a number of ways in which amyloid toxicity may be prevented. These include regulating the level of the amyloidogenic peptides and proteins, minimising the production of prefibrillar oligomers in amyloid assembly reactions, sequestrating amyloids within membrane bound organelles, controlling amyloid assembly by other molecules, and disassembling the fibrils under physiological conditions. Crucially, a better understanding of how toxicity is avoided in the production of functional amyloids may provide insights into the prevention of amyloid toxicity in amyloidoses. Full article

(This article belongs to the Special Issue Functional Amyloids)

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4115 KiB

Open AccessReview

The Physiological and Pathological Implications of the Formation of Hydrogels, with a Specific Focus on Amyloid Polypeptides

by Létitia Jean, Alex C. Foley and David J. T. Vaux

Biomolecules 2017, 7(4), 70; https://doi.org/10.3390/biom7040070 - 22 Sep 2017

Cited by 9 | Viewed by 6283

Abstract

Hydrogels are water-swollen and viscoelastic three-dimensional cross-linked polymeric network originating from monomer polymerisation. Hydrogel-forming polypeptides are widely found in nature and, at a cellular and organismal level, they provide a wide range of functions for the organism making them. Amyloid structures, arising from [...] Read more.

Hydrogels are water-swollen and viscoelastic three-dimensional cross-linked polymeric network originating from monomer polymerisation. Hydrogel-forming polypeptides are widely found in nature and, at a cellular and organismal level, they provide a wide range of functions for the organism making them. Amyloid structures, arising from polypeptide aggregation, can be damaging or beneficial to different types of organisms. Although the best-known amyloids are those associated with human pathologies, this underlying structure is commonly used by higher eukaryotes to maintain normal cellular activities, and also by microbial communities to promote their survival and growth. Amyloidogenesis occurs by nucleation-dependent polymerisation, which includes several species (monomers, nuclei, oligomers, and fibrils). Oligomers of pathological amyloids are considered the toxic species through cellular membrane perturbation, with the fibrils thought to represent a protective sink for toxic species. However, both functional and disease-associated amyloids use fibril cross-linking to form hydrogels. The properties of amyloid hydrogels can be exploited by organisms to fulfil specific physiological functions. Non-physiological hydrogelation by pathological amyloids may provide additional toxic mechanism(s), outside of membrane toxicity by oligomers, such as physical changes to the intracellular and extracellular environments, with wide-spread consequences for many structural and dynamic processes, and overall effects on cell survival. Full article

(This article belongs to the Special Issue Functional Amyloids)

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1092 KiB

Open AccessReview

The Role of Functional Amyloids in Multicellular Growth and Development of Gram-Positive Bacteria

by Anna Dragoš, Ákos T. Kovács and Dennis Claessen

Biomolecules 2017, 7(3), 60; https://doi.org/10.3390/biom7030060 - 7 Aug 2017

Cited by 27 | Viewed by 7453

Abstract

Amyloid fibrils play pivotal roles in all domains of life. In bacteria, these fibrillar structures are often part of an extracellular matrix that surrounds the producing organism and thereby provides protection to harsh environmental conditions. Here, we discuss the role of amyloid fibrils [...] Read more.

Amyloid fibrils play pivotal roles in all domains of life. In bacteria, these fibrillar structures are often part of an extracellular matrix that surrounds the producing organism and thereby provides protection to harsh environmental conditions. Here, we discuss the role of amyloid fibrils in the two distant Gram-positive bacteria, Streptomyces coelicolor and Bacillus subtilis. We describe how amyloid fibrils contribute to a multitude of developmental processes in each of these systems, including multicellular growth and community development. Despite this variety of tasks, we know surprisingly little about how their assembly is organized to fulfill all these roles. Full article

(This article belongs to the Special Issue Functional Amyloids)

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2208 KiB

Open AccessReview

Functional Amyloids in Reproduction

by Aveline Hewetson, Hoa Quynh Do, Caitlyn Myers, Archana Muthusubramanian, Roger Bryan Sutton, Benjamin J. Wylie and Gail A. Cornwall

Biomolecules 2017, 7(3), 46; https://doi.org/10.3390/biom7030046 - 29 Jun 2017

Cited by 43 | Viewed by 6440

Abstract

Amyloids are traditionally considered pathological protein aggregates that play causative roles in neurodegenerative disease, diabetes and prionopathies. However, increasing evidence indicates that in many biological systems nonpathological amyloids are formed for functional purposes. In this review, we will specifically describe amyloids that carry [...] Read more.

Amyloids are traditionally considered pathological protein aggregates that play causative roles in neurodegenerative disease, diabetes and prionopathies. However, increasing evidence indicates that in many biological systems nonpathological amyloids are formed for functional purposes. In this review, we will specifically describe amyloids that carry out biological roles in sexual reproduction including the processes of gametogenesis, germline specification, sperm maturation and fertilization. Several of these functional amyloids are evolutionarily conserved across several taxa, including human, emphasizing the critical role amyloids perform in reproduction. Evidence will also be presented suggesting that, if altered, some functional amyloids may become pathological. Full article

(This article belongs to the Special Issue Functional Amyloids)

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1938 KiB

Open AccessReview

Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins

by Alessandra Piscitelli, Paola Cicatiello, Alfredo Maria Gravagnuolo, Ilaria Sorrentino, Cinzia Pezzella and Paola Giardina

Biomolecules 2017, 7(3), 45; https://doi.org/10.3390/biom7030045 - 26 Jun 2017

Cited by 33 | Viewed by 5653

Abstract

Class I hydrophobins produced from fungi are amongst the first proteins recognized as functional amyloids. They are amphiphilic proteins involved in the formation of aerial structures such as spores or fruiting bodies. They form chemically robust layers which can only be dissolved in [...] Read more.

Class I hydrophobins produced from fungi are amongst the first proteins recognized as functional amyloids. They are amphiphilic proteins involved in the formation of aerial structures such as spores or fruiting bodies. They form chemically robust layers which can only be dissolved in strong acids. These layers adhere to different surfaces, changing their wettability, and allow the binding of other proteins. Herein, the modification of diverse types of surfaces with Class I hydrophobins is reported, highlighting the applications of the coated surfaces. Indeed, these coatings can be exploited in several fields, spanning from biomedical to industrial applications, which include biosensing and textile manufacturing. Full article

(This article belongs to the Special Issue Functional Amyloids)

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2756 KiB

Open AccessReview

Diversity of Amyloid Motifs in NLR Signaling in Fungi

by Antoine Loquet and Sven J. Saupe

Biomolecules 2017, 7(2), 38; https://doi.org/10.3390/biom7020038 - 13 Apr 2017

Cited by 24 | Viewed by 6336

Abstract

Amyloid folds not only represent the underlying cause of a large class of human diseases but also display a variety of functional roles both in prokaryote and eukaryote organisms. Among these roles is a recently-described activity in signal transduction cascades functioning in host [...] Read more.

Amyloid folds not only represent the underlying cause of a large class of human diseases but also display a variety of functional roles both in prokaryote and eukaryote organisms. Among these roles is a recently-described activity in signal transduction cascades functioning in host defense and programmed cell death and involving Nod-like receptors (NLRs). In different fungal species, prion amyloid folds convey activation signals from a receptor protein to an effector domain by an amyloid templating and propagation mechanism. The discovery of these amyloid signaling motifs derives from the study of [Het-s], a fungal prion of the species Podospora anserina. These signaling pathways are typically composed of two basic components encoded by adjacent genes, the NLR receptor bearing an amyloid motif at the N-terminal end and a cell death execution protein with a HeLo pore-forming domain bearing a C-terminal amyloid motif. Activation of the NLR receptor allows for amyloid folding of the N-terminal amyloid motifs which then template trans-conformation of the homologous motif in the cell death execution protein. A variety of such motifs, which differ by their sequence signature, have been described in fungi. Among them, the PP-motif bears resemblance with the RHIM amyloid motif involved in the necroptosis pathway in mammals suggesting an evolutionary conservation of amyloid signaling from fungi to mammals. Full article

(This article belongs to the Special Issue Functional Amyloids)

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