Diversity, biogenesis and function of microbial amyloids

Blanco, Luz P.; Evans, Margery L.; Smith, Daniel R.; Badtke, Matthew P.; Chapman, Matthew R.

doi:10.1016/j.tim.2011.11.005

Cited by 320Biochemical and Structural CharacterizationAlzheimer's disease research and treatmentsBacterial biofilms and quorum sensing

Diversity, biogenesis and function of microbial amyloids

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Blanco, Luz P., Evans, Margery L., Smith, Daniel R., Badtke, Matthew P., Chapman, Matthew R.·2012·Trends in Microbiology

DOI 10.1016/j.tim.2011.11.005PMC PMC3278576

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Abstract

Amyloid is a distinct β-sheet-rich fold that many proteins can acquire. Frequently associated with neurodegenerative diseases in humans, including Alzheimer's, Parkinson's and Huntington's diseases, amyloids are traditionally considered the product of protein misfolding. However, the amyloid fold is now recognized as a ubiquitous part of normal cellular biology. Functional amyloids have been identified in nearly all facets of cellular life, with microbial functional amyloids leading the way. Unlike disease-associated amyloids, functional amyloids are assembled by dedicated, directed pathways and ultimately perform a physiological function that benefits the organism. The evolved amyloid assembly and disassembly pathways of microbes have provided novel insights into how cells have harnessed the amyloid assembly process for productive means. An understanding of functional amyloid biogenesis promises to provide a fresh perspective on the molecular events that underlie disease-associated amyloidogenesis. Here, we review functional microbial amyloids with an emphasis on curli fibers and their role in promoting biofilm formation and other community behaviors.

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Amyloid fibers are important structural components of biofilms.
“Amyloid fibers are important structural components of biofilms.134,135”
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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454 · see citing works
Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation
Chapman, M., Robinson, L. S., Pinkner, J., Roth, R., Heuser, J., Hammar, M., Normark, S., & Hultgren, S. (2002) · Science · doi:10.1126/science.1067484 · Cited by 1,282 · see citing works
Self-citation
Curli biogenesis and function.
Barnhart, M. M., & Chapman, M. (2006) · Annual Review of Microbiology · doi:10.1146/annurev.micro.60.080805.142106 · Cited by 1,223 · see citing works
Self-citation
[URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiae
Wickner, R. B. (1994) · Science · doi:10.1126/science.7909170 · Cited by 1,216 · see citing works
Functional amyloid – from bacteria to humans
Fowler, D. M., Koulov, A. V., Balch, W. E., & Kelly, J. W. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.03.003 · Cited by 1,052 · see citing works
Calcium Dysregulation and Membrane Disruption as a Ubiquitous Neurotoxic Mechanism of Soluble Amyloid Oligomers*♦
Demuro, A., Mina, E. W., Kayed, R., Milton, S. C. F., Parker, I., & Glabe, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500997200 · Cited by 1,038 · see citing works
Techniques to study amyloid fibril formation in vitro
NILSSON, M. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.012 · Cited by 948 · see citing works
Alzheimer's amyloid fibrils: structure and assembly.
Serpell, L. (2000) · Biochimica et Biophysica Acta · doi:10.1016/s0925-4439(00)00029-6 · Cited by 922 · see citing works
Amyloid fibers provide structural integrity to Bacillus subtilis biofilms
Romero, D., Aguilar, C., Losick, R. M., & Kolter, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910560107 · Cited by 793 · see citing works
Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C. W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J. L., et al. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-18 · Cited by 773 · see citing works
Small-molecule inhibitors target Escherichia coli amyloid biogenesis and biofilm formation
Cegelski, L., Pinkner, J. S., Hammer, N. D., Cusumano, C. K., Hung, C., Chorell, E., Åberg, V., Walker, J. N., Seed, P. C., Almqvist, F., et al. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.242 · Cited by 418 · see citing works
Self-citation
Complex Regulatory Network Controls Initial Adhesion and Biofilm Formation in Escherichia coli via Regulation of the csgD Gene
Prigent‐Combaret, C., Brombacher, E., Vidal, O., Ambert, A., Lejeune, P., Landini, P., & Dorel, C. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.24.7213-7223.2001 · Cited by 410 · see citing works
Production of Cellulose and Curli Fimbriae by Members of the Family Enterobacteriaceae Isolated from the Human Gastrointestinal Tract
Zogaj, X., Bokranz, W., Nimtz, M., & Römling, U. (2003) · Infection and Immunity · doi:10.1128/iai.71.7.4151-4158.2003 · Cited by 385 · see citing works
Hydrophobins, the fungal coat unravelled
Wösten, H. A. B., & de Vocht, M. L. (2000) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(00)00002-2 · Cited by 373 · see citing works
Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis
Glabe, C. G., & Kayed, R. (2006) · Neurology · doi:10.1212/01.wnl.0000192103.24796.42 · Cited by 364 · see citing works
Characterization of the rdar morphotype, a multicellular behaviour in Enterobacteriaceae
Römling, U. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-4557-x · Cited by 339 · see citing works
The Hyphal-Associated Adhesin and Invasin Als3 of Candida albicans Mediates Iron Acquisition from Host Ferritin
Almeida, R. S., Brunke, S., Albrecht, A., Thewes, S., Laue, M., Edwards, J. E., Filler, S. G., & Hube, B. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000217 · Cited by 330 · see citing works
A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in <i>Streptomyces coelicolor</i> by forming amyloid-like fibrils
Claessen, D., Rink, R., de Jong, W., Siebring, J., de Vreugd, P., Boersma, F. G. H., Dijkhuizen, L., & Wösten, H. A. B. (2003) · Genes & Development · doi:10.1101/gad.264303 · Cited by 327 · see citing works
Amyloid adhesins are abundant in natural biofilms
Larsen, P. B., Nielsen, J. L., Dueholm, M. S., Wetzel, R. B., Otzen, D. E., & Nielsen, P. H. (2007) · Environmental Microbiology · doi:10.1111/j.1462-2920.2007.01418.x · Cited by 319 · see citing works
Functional amyloid in Pseudomonas
Dueholm, M. S., Petersen, S. V., Sønderkær, M., Larsen, P. B., Christiansen, G., Hein, K. L., Enghild, J. J., Nielsen, J. L., Nielsen, K. L., Nielsen, P. H., et al. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07269.x · Cited by 301 · see citing works
A Biochemical Guide to Yeast Adhesins: Glycoproteins for Social and Antisocial Occasions
Dranginis, A., Rauceo, J. M., Coronado, J. E., & Lipke, P. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00037-06 · Cited by 296 · see citing works
The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization
Hammer, N. D., Schmidt, J. C., & Chapman, M. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703310104 · Cited by 283 · see citing works
Self-citation
Hydrophobin Genes Involved in Formation of Aerial Hyphae and Fruit Bodies in Schizophyllum.
Wessels, J. G. H., Vries, O. D., Ásgeirsdóttir, S. A., et al. (1991) · The Plant Cell · doi:10.1105/tpc.3.8.793 · Cited by 276 · see citing works
Thin Aggregative Fimbriae and Cellulose Enhance Long-Term Survival and Persistence ofSalmonella
White, A. P., Gibson, D. L., Kim, W., Kay, W. W., & Surette, M. G. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.9.3219-3227.2006 · Cited by 269 · see citing works
Salmonella enterica Virulence Genes Are Required for Bacterial Attachment to Plant Tissue
Barak, J. D., Gorski, L., Naraghi‐Arani, P., & Charkowski, A. O. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.10.5685-5691.2005 · Cited by 257 · see citing works
The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in <i>Streptomyces coelicolor</i>
Elliot, M. A., Karoonuthaisiri, N., Huang, J., Bibb, M. J., Cohen, S. N., Kao, C. M., & Buttner, M. J. (2003) · Genes & Development · doi:10.1101/gad.264403 · Cited by 246 · see citing works
Secretion of curli fibre subunits is mediated by the outer membrane‐localized CsgG protein
Robinson, L. S., Epstein, E. A., Hultgren, S. J., & Chapman, M. R. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04997.x · Cited by 233 · see citing works
Self-citation
Prions of fungi: inherited structures and biological roles
Wickner, R. B., Edskes, H. K., Shewmaker, F., & Nakayashiki, T. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1708 · Cited by 231 · see citing works
An accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms
Romero, D., Vlamakis, H. C., Losick, R. M., & Kolter, R. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07653.x · Cited by 227 · see citing works
Analyses of the Red-Dry-Rough Phenotype of an Escherichia coli O157:H7 Strain and Its Role in Biofilm Formation and Resistance to Antibacterial Agents
Uhlich, G. A., Cooke, P. H., & Solomon, E. B. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.72.4.2564-2572.2006 · Cited by 219 · see citing works
Review: Modulating Factors in Amyloid-β Fibril Formation
McLaurin, J., Yang, D.-S., Yip, C. M., & Fraser, P. E. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4289 · Cited by 217 · see citing works
In Vitro Propagation of the Prion-Like State of Yeast Sup35 Protein
Paushkin, S. V., Kushnirov, V. V., Smirnov, V. N., et al. (1997) · Science · doi:10.1126/science.277.5324.381 · Cited by 210 · see citing works
Mycobacterium tuberculosis produces pili during human infection
Alteri, C. J., Xicohtencatl‐Cortés, J., Hess, S. Y., Caballero-Olín, G., Girón, J. A., & Friedman, R. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602304104 · Cited by 197 · see citing works
In Vitro Polymerization of a Functional Escherichia coli Amyloid Protein
Wang, X., Smith, D. R., Jones, J. W. M., & Chapman, M. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609228200 · Cited by 193 · see citing works
Self-citation
Amyloidosis and Alzheimer’s disease
Ghiso, J. A., & Frangione, B. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00149-7 · Cited by 189 · see citing works
Structural Characterization of the Hydrophobin SC3, as a Monomer and after Self-Assembly at Hydrophobic/Hydrophilic Interfaces
de Vocht, M. L., Scholtmeijer, K., van der Vegte, E. W., et al. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77912-3 · Cited by 189 · see citing works
Amyloid-Like Adhesins Produced by Floc-Forming and Filamentous Bacteria in Activated Sludge
Larsen, P. B., Nielsen, J. L., Otzen, D. E., & Nielsen, P. H. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.02274-07 · Cited by 188 · see citing works
Secretion of virulence determinants by the general secretory pathway in Gram-negative pathogens: an evolving story
Stathopoulos, C., Hendrixson, D. R., Thanassi, D. G., Hultgren, S. J., Geme, J. W. S., & Curtiss, R. (2000) · Microbes and Infection · doi:10.1016/s1286-4579(00)01260-0 · Cited by 160 · see citing works
Microcin E492, a channel-forming bacteriocin from Klebsiella pneumoniae , induces apoptosis in some human cell lines
Hetz, C. A., Bono, M. R., Barros, L. F., & Lagos, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052709699 · Cited by 157 · see citing works
Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences
Ramsook, C. B., Tan, C., Garcia, M. C., Fung, R., Soybelman, G., Henry, R., Litewka, A., O'Meally, S., Otoo, H., Khalaf, R. A., et al. (2009) · Eukaryotic Cell · doi:10.1128/ec.00068-09 · Cited by 156 · see citing works
Localized and efficient curli nucleation requires the chaperone-like amyloid assembly protein CsgF
Nenninger, A. A., Robinson, L. S., & Hultgren, S. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812143106 · Cited by 151 · see citing works
Candida albicans Als Adhesins Have Conserved Amyloid-Forming Sequences
Otoo, H., Lee, K., Qiu, W.-G., & Lipke, P. (2007) · Eukaryotic Cell · doi:10.1128/ec.00309-07 · Cited by 139 · see citing works
Biofilm formation by Escherichia coli is stimulated by synergistic interactions and co-adhesion mechanisms with adherence-proficient bacteria
Castonguay, M., van der Schaaf, S., Koester, W., Krooneman, J., van der Meer, W., Harmsen, H. J. M., & Landini, P. (2005) · Research in Microbiology · doi:10.1016/j.resmic.2005.10.003 · Cited by 138 · see citing works
CsgE is a curli secretion specificity factor that prevents amyloid fibre aggregation
Nenninger, A. A., Robinson, L. S., Hammer, N. D., Epstein, E. A., Badtke, M. P., Hultgren, S. J., & Chapman, M. R. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07706.x · Cited by 136 · see citing works
Self-citation
The formation of the rodlet layer of streptomycetes is the result of the interplay between rodlins and chaplins
Claessen, D., Stokroos, I., Deelstra, H. J., Penninga, N. A., Bormann, C., Salas, J. A., Dijkhuizen, L., & Wösten, H. A. B. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04143.x · Cited by 136 · see citing works
The Molecular Basis of Functional Bacterial Amyloid Polymerization and Nucleation
Wang, X., Hammer, N. D., & Chapman, M. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800466200 · Cited by 135 · see citing works
Self-citation
The Functional Curli Amyloid Is Not Based on In-register Parallel β-Sheet Structure
Shewmaker, F. P., McGlinchey, R. P., Thurber, K. R., McPhie, P., Dyda, F., Tycko, R., & Wickner, R. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.007054 · Cited by 133 · see citing works
Amyloid Formation Modulates the Biological Activity of a Bacterial Protein
Biéler, S., Estrada, L. D., Lagos, R., Baeza, M., Castilla, J., & Soto, C. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502031200 · Cited by 132 · see citing works
Antimicrobial Protegrin-1 Forms Amyloid-Like Fibrils with Rapid Kinetics Suggesting a Functional Link
Jang, H., Arce, F. T., Mustata, M., Ramachandran, S., Capone, R. F., Nussinov, R., & Lal, R. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.01.072 · Cited by 132 · see citing works
Candida albicans Als proteins mediate aggregation with bacteria and yeasts.
Klotz, S., Gaur, N., Armond, R. L. D., Sheppard, D., Khardori, N., Edwards, J., Lipke, P., & El-azizi, M. (2007) · Medical Mycology · doi:10.1080/13693780701299333 · Cited by 125 · see citing works
Differential Binding of Escherichia coli O157:H7 to Alfalfa, Human Epithelial Cells, and Plastic Is Mediated by a Variety of Surface Structures
Torres, A. G., Jeter, C., Langley, W. A., & Matthysse, A. G. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.12.8008-8015.2005 · Cited by 122 · see citing works
Structural predictions of AgfA, the insoluble fimbrial subunit of Salmonella thin aggregative fimbriae 1 1Edited by W. Baumeister
Collinson, S. K., Parker, J. M. R., Hodges, R. S., & Kay, W. W. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2882 · Cited by 116 · see citing works
Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesis
Wang, X., Zhou, Y., Ren, J.-J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908714107 · Cited by 116 · see citing works
Lipoprotein trafficking in Escherichia coli
Narita, S., Matsuyama, S., & Tokuda, H. (2004) · Archives of Microbiology · doi:10.1007/s00203-004-0682-4 · Cited by 112 · see citing works
Attachment and biofilm formation on stainless steel by Escherichia coli O157:H7 as affected by curli production
Ryu, J., Kim, H., Frank, J. F., et al. (2004) · Letters in Applied Microbiology · doi:10.1111/j.1472-765x.2004.01591.x · Cited by 110 · see citing works
Structural and Functional Diversity of Microcins, Gene-Encoded Antibacterial Peptides from Enterobacteria
Duquesne, S., Petit, V. W., Péduzzi, J., & Rebuffat, S. (2007) · Microbial Physiology · doi:10.1159/000104748 · Cited by 109 · see citing works
Fibrillation of the Major Curli Subunit CsgA under a Wide Range of Conditions Implies a Robust Design of Aggregation
Dueholm, M. S., Nielsen, S. B., Hein, K. L., Nissen, P., Chapman, M. R., Christiansen, G., Nielsen, P. H., & Otzen, D. E. (2011) · Biochemistry · doi:10.1021/bi200967c · Cited by 109 · see citing works
Self-citation
Amyloidogenesis of Type III-dependent Harpins from Plant Pathogenic Bacteria
Oh, J., Kim, J., Jeon, E., Yoo, C.-H., Moon, J. S., Rhee, S., & Hwang, I. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m602576200 · Cited by 105 · see citing works
Sequence Determinants of Bacterial Amyloid Formation
Wang, X., & Chapman, M. R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.05.019 · Cited by 104 · see citing works
Self-citation
Antibacterial and Antitumorigenic Properties of Microcin E492, a Pore- Forming Bacteriocin
Lagos, R., Tello, M., Mercado, G., Garcia, V., & Monasterio, O. (2009) · Current Pharmaceutical Biotechnology · doi:10.2174/138920109787048643 · Cited by 104 · see citing works
The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils.
Nordstedt, C., Näslund, J., Tjernberg, L. O., Karlström, A. R., Thyberg, J., & Terenius, L. Y. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47347-4 · Cited by 103 · see citing works
Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae that are anchored to the cell surface via cellulose
de Jong, W., Wösten, H. A. B., Dijkhuizen, L., & Claessen, D. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06838.x · Cited by 102 · see citing works
Atomic Resolution Insights into Curli Fiber Biogenesis
Taylor, J. D., Zhou, Y., Salgado, P. S., Patwardhan, A., McGuffie, M. J., Pape, T., Grabe, G. J., Epstein, E. A., Constable, S. C., Simpson, P. J., et al. (2011) · Structure · doi:10.1016/j.str.2011.05.015 · Cited by 88 · see citing works
Self-citation
Microcin E492 antibacterial activity: evidence for a TonB‐dependent inner membrane permeabilization on Escherichia coli
Destoumieux‐Garzón, D., Thomas, X., Santamaría, M., Goulard, C., Barthélémy, M., Boscher, B., Bessin, Y., Molle, G., Pons, A., Letellìer, L., et al. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03610.x · Cited by 88 · see citing works
Visualization of Aggregation of the Rnq1 Prion Domain and Cross-seeding Interactions with Sup35NM
Vitrenko, Y. A., Gracheva, E. O., Richmond, J. E., & Liebman, S. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609269200 · Cited by 86 · see citing works
Recruitment of Class I Hydrophobins to the Air:Water Interface Initiates a Multi-step Process of Functional Amyloid Formation
Morris, V. K., Ren, Q., Macindoe, I., Kwan, A. H., Byrne, N., & Sunde, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.214197 · Cited by 74 · see citing works
Prying into prions
Dobson, C. M. (2005) · Nature · doi:10.1038/435747a · Cited by 73 · see citing works
Evidence That the Pseudomonas syringae pv. syringae hrp-Linked hrmA Gene Encodes an Avr-Like Protein That Acts in an hrp-Dependent Manner Within Tobacco Cells
Alfano, J. R., Kim, H., Delaney, T. P., et al. (1997) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi.1997.10.5.580 · Cited by 71 · see citing works
Microcin E492 forms ion channels in phospholipid bilayer membranes
Lagos, R., Wilkens, M., Vergara, C., et al. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80096-d · Cited by 70 · see citing works
Global Cell Surface Conformational Shift Mediated by a Candida albicans Adhesin
Rauceo, J. M., Gaur, N. K., Lee, K.-G., Edwards, J. E., Klotz, S. A., & Lipke, P. N. (2004) · Infection and Immunity · doi:10.1128/iai.72.9.4948-4955.2004 · Cited by 68 · see citing works
Structure, Function, and Amyloidogenesis of Fungal Prions: Filament Polymorphism and Prion Variants
Baxa, U., Cassese, T., Kajava, A. V., et al. (2006) · Advances in protein chemistry · doi:10.1016/s0065-3233(06)73005-4 · Cited by 65 · see citing works
The Assembly of Individual Chaplin Peptides from Streptomyces coelicolor into Functional Amyloid Fibrils
Sawyer, E. B., Claessen, D., Haas, M., Hurgobin, B., & Gras, S. L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018839 · Cited by 65 · see citing works
Structure and Function of Glycosylated Tandem Repeats from Candida albicans Als Adhesins
Frank, A. T., Ramsook, C. B., Otoo, H. N., Tan, C., Soybelman, G., Rauceo, J. M., Gaur, N. K., Klotz, S. A., & Lipke, P. N. (2010) · Eukaryotic Cell · doi:10.1128/ec.00235-09 · Cited by 63 · see citing works
In vivo aggregation of the HET‐s prion protein of the fungus Podospora anserina
Coustou-Linares, V., Maddelein, M., Bégueret, J., et al. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02707.x · Cited by 61 · see citing works
Propagation of the [PIN + ] prion by fragments of Rnq1 fused to GFP
Vitrenko, Y. A., Pavon, M. E., Stone, S., et al. (2007) · Current Genetics · doi:10.1007/s00294-007-0127-0 · Cited by 51 · see citing works
Curli provide the template for understanding controlled amyloid propagation
Wang, X., & Chapman, M. R. (2008) · Prion · doi:10.4161/pri.2.2.6746 · Cited by 50 · see citing works
Self-citation
Spatial Clustering of the Curlin Secretion Lipoprotein Requires Curli Fiber Assembly
Epstein, E. A., Reizian, M. A., & Chapman, M. R. (2008) · Journal of Bacteriology · doi:10.1128/jb.01244-08 · Cited by 48 · see citing works
Self-citation
The Filament-specific Rep1-1 Repellent of the Phytopathogen Ustilago maydis Forms Functional Surface-active Amyloid-like Fibrils
Teertstra, W. R., van der Velden, G. J., de Jong, J. F., Kruijtzer, J. A. W., Liskamp, R. M. J., Kroon-Batenburg, L. M. J., Müller, W. H., Gebbink, M. F. B. G., & Wösten, H. A. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900095200 · Cited by 43 · see citing works
Dual amyloid domains promote differential functioning of the chaplin proteins during Streptomyces aerial morphogenesis
Capstick, D. S., Jomaa, A., Hanke, C., Ortega, J., & Elliot, M. (2011) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1018715108 · Cited by 41 · see citing works
Fungal hydrophobins form a sheath preventing immune recognition of airborne conidia
Aimanianda, V., & Latgé, J. (2010) · Virulence · doi:10.4161/viru.1.3.11317 · Cited by 40 · see citing works
Analysis of Erwinia chrysanthemi EC16 pelE∷uidA, pelL∷uidA, and hrpN∷uidA Mutants Reveals Strain-Specific Atypical Regulation of the Hrp Type III Secretion System
Ham, J. H., Cui, Y., Alfano, J. R., et al. (2004) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi.2004.17.2.184 · Cited by 33 · see citing works
Distinct Subregions of Swi1 Manifest Striking Differences in Prion Transmission and SWI/SNF Function
Du, Z., Crow, E. T., Kang, H. S., & Li, L. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00225-10 · Cited by 33 · see citing works
Scanning electron microscopy analysis of agedMycobacterium tuberculosiscells
Dahl, J. L. (2005) · Canadian Journal of Microbiology · doi:10.1139/w05-001 · Cited by 23 · see citing works
A Small, Glutamine-Free Domain Propagates the [SWI+] Prion in Budding Yeast
Crow, E. T., Du, Z., & Li, L. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05338-11 · Cited by 21 · see citing works
Sodium dodecyl sulfate–agarose gel electrophoresis for the detection and isolation of amyloid curli fibers
Sitaras, C., Naghavi, M., & Herrington, M. B. (2010) · Analytical Biochemistry · doi:10.1016/j.ab.2010.09.038 · Cited by 16 · see citing works
Scanning electron microscopy of mycobacteria.
Merkal, R. S., Rhoades, K. R., Gallagher, J. E., et al. (1973) · PubMed · doi:10.1164/arrd.1973.108.2.381 · Cited by 12 · see citing works
Absence of repellents in Ustilago maydis induces genes encoding small secreted proteins
Teertstra, W. R., Krijgsheld, P., & Wösten, H. A. B. (2011) · Antonie van Leeuwenhoek · doi:10.1007/s10482-011-9581-2 · Cited by 7 · see citing works

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Sochocka, M., Donskow-Łysoniewska, K., Diniz, B. S., Kurpas, D., Brzozowska, E., & Leszek, J. (2019) · Molecular Neurobiology · doi:10.1007/s12035-018-1188-4 · Cited by 584 · see citing works
Role of gut microbiota and nutrients in amyloid formation and pathogenesis of Alzheimer disease
Pistollato, F., Sumalla Cano, S., Elio, I., Masias Vergara, M., Giampieri, F., & Battino, M. (2016) · Nutrition Reviews · doi:10.1093/nutrit/nuw023 · Cited by 496 · see citing works
The dental plaque biofilm matrix
Jakubovics, N. S., Goodman, S. D., Mashburn‐Warren, L., Stafford, G. P., & Cieplik, F. (2021) · Periodontology 2000 · doi:10.1111/prd.12361 · Cited by 488 · see citing works
Dysregulated bile acid synthesis and dysbiosis are implicated in Western diet-induced systemic inflammation, microglial activation, and reduced neuroplasticity
Jena, P. K., Sheng, L., Di Lucente, J., Jin, L., Maezawa, I., & Wan, Y. Y. (2018) · The FASEB Journal · doi:10.1096/fj.201700984rr · Cited by 134 · see citing works
Strengthening relationships: amyloids create adhesion nanodomains in yeasts
Lipke, P. N., Garcia, M. C., Alsteens, D., Ramsook, C. B., Klotz, S. A., & Dufrêne, Y. F. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2011.10.002 · Cited by 104 · see citing works
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Shanmugam, N., Baker, M. O. D. G., Ball, S. R., Steain, M., Pham, C. L. L., & Sunde, M. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00526-1 · Cited by 75 · see citing works
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Wiatrak, B., Balon, K., Jawień, P., Bednarz, D., Jęśkowiak, I., & Szeląg, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094862 · Cited by 58 · see citing works
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Masrati, G., Landau, M., Ben-Tal, N., Lupas, A., Kosloff, M., & Kosinski, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167127 · Cited by 53 · see citing works

[123I-MIBG myocardial SPECT in two patients with familial amyloid polyneuropathy].
Itoh, A., Sone, S., Kasuga, T., et al. (1995) · PubMed · Cited by 1 · see citing works
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Beilschmidt, L. K., & Puccio, H. M. (2014) · Biochimie · doi:10.1016/j.biochi.2014.01.009 · Cited by 107 · see citing works
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Saha, P. P., Vishwanathan, V., Bankapalli, K., & D’Silva, P. (2017) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2017_5 · Cited by 22 · see citing works
Fe/S protein biogenesis in trypanosomes — A review
Lukeš, J., & Basu, S. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.08.015 · Cited by 31 · see citing works
Daphniphyllum alkaloids: Structures, Biogenesis, and Activities
Morita, H., & Kobayashi, J. (2007) · doi:10.1002/9783527621071.ch18 · Cited by 5 · see citing works

Authors: Blanco, L. P., Evans, M. L., Smith, D. R., Badtke, M. P., & Chapman, M. R.
Affiliations: University of Michigan (US)
Corresponding author: Chapman, Matthew R.
ORCID: Blanco, Luz P.
Smith, Daniel R.
Chapman, Matthew R.
Venue: Trends in Microbiology
Publisher: Elsevier BV
Published: 2012-02
Volume: 20
Issue: 2
Pages: 66-73
ISSN: 0966-842X (ISSN-L)
DOI: 10.1016/j.tim.2011.11.005
PMC: PMC3278576
OpenAlex: W1974059817
Cited by: 320
References: 88
Citations by year: 2026: 8 · 2025: 12 · 2024: 21 · 2023: 10 · 2022: 21 · 2021: 21 · 2020: 26 · 2019: 25 · 2018: 34 · 2017: 22 · 2016: 27 · 2015: 30 · 2014: 24 · 2013: 26 · 2012: 12
FWCI: 1.83
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Microbiology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (T32GM008353, T32GM145304)
National Institute of Allergy and Infectious Diseases (AI073847, R01AI073847, R56AI073847)
Chemical Sciences, Geosciences, and Biosciences Division
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
Keywords: functional amyloids, amyloid assembly, curli fibers, biofilm formation, protein misfolding
MeSH terms: Amyloid, Bacteria, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Biofilms, Adhesins, Bacterial, Escherichia coli Proteins, Biodiversity, Protein Multimerization

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Diversity, biogenesis and function of microbial amyloids

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