Microbial functional amyloids serve diverse purposes for structure, adhesion and defence
Open accessAbstract
The functional amyloid state of proteins has in recent years garnered much attention for its role in serving crucial and diverse biological roles. Amyloid is a protein fold characterised by fibrillar morphology, binding of the amyloid-specific dyes Thioflavin T and Congo Red, insolubility and underlying cross-β structure. Amyloids were initially characterised as an aberrant protein fold associated with mammalian disease. However, in the last two decades, functional amyloids have been described in almost all biological systems, from viruses, to bacteria and archaea, to humans. Understanding the structure and role of these amyloids elucidates novel and potentially ancient mechanisms of protein function throughout nature. Many of these microbial functional amyloids are utilised by pathogens for invasion and maintenance of infection. As such, they offer novel avenues for therapies. This review examines the structure and mechanism of known microbial functional amyloids, with a particular focus on the pathogenicity conferred by the production of these structures and the strategies utilised by microbes to interfere with host amyloid structures. The biological importance of microbial amyloid assemblies is highlighted by their ubiquity and diverse functionality.
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Filaments of the Ure2p prion protein have a cross-β core structure
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The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids
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Class I Hydrophobin Vmh2 Adopts Atypical Mechanisms to Self-Assemble into Functional Amyloid Fibrils
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Bacillus subtilis HelD, an RNA Polymerase Interacting Helicase, Forms Amyloid-Like Fibrils
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“Particularly in the bacterial world, the amyloid state represents a functional structure, which can ensure important functions in bacterial fitness and social behavior (122, 123).”
BackgroundComputational methods to predict protein aggregation
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Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils
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“considered that amyloid structures are not always formed as a product of protein misfolding, as it was later revealed that microorganisms and even higher eukaryotes sometimes produce amyloid-like structures for biological purposes [6,7].”
BackgroundInfluentialCell wall–associated effectors of plant-colonizing fungi
TANAKA, S., & Kahmann, R. (2021) · Mycologia · doi:10.1080/00275514.2020.1831293 · Cited by 63 · see citing works
“2 00 9 (C on tin ue d) (Talbot et al. 1993; Bayry et al. 2012; Shanmugam et al. 2019).”
A mechanistic survey of Alzheimer's disease
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The Cryo-EM structures of two amphibian antimicrobial cross-β amyloid fibrils
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Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics
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“…fi lmscaffolding 12 , facilitate resistance to stress conditions 13 , act as bio-adhesives anchoring agents 14 , create channels in the bio fi lm matrix for nutrient uptake and transport 15,16 , and even act as antibacterial agents, achieving dominance over…”
Shanmugam, N., Baker, M., Sanz-Hernández, M., Sierecki, E., Gambin, Y., Steain, M., Pham, C. L. L., & Sunde, M. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106524 · Cited by 29 · see citing works
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Hydrophobin Rodlets on the Fungal Cell Wall
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Self-citationThe Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements
Zajkowski, T., Lee, M., Mondal, S. S., Carbajal, A., Dec, R., Brennock, P. D., Piast, R. W., Snyder, J., Bense, N. B., Dzwolak, W., et al. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab010 · Cited by 27 · see citing works
“Amyloid-forming proteins have been detected and experimentally verified in all domains of life: Eukaryota, Bacteria, and Archaea (Gebbink et al. 2005; Greenwald and Riek 2010; Shanmugam et al. 2019).”
BackgroundBacterial extracellular matrix as a natural source of biotechnologically multivalent materials
Molina‐Santiago, C., de Vicente, A., & Romero, D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.05.008 · Cited by 30 · see citing works
Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions
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“In the interaction between pathogenic bacteria and mammalian tissues, bacterial amyloids act as the virulence factors promoting adhesion [178].”
Morris, D. L., Johnson, S., Bleck, C. K. E., Lee, D., & Tjandra, N. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013023 · Cited by 29 · see citing works
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Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity
di Cologna, N. D. M., Samaddar, S., Valle, C. A., Vargas, J., Avilés-Reyes, A., Morales, J. C. T., Ganguly, T., Pileggi, R., Brady, L. J., Lemos, J. A. C., et al. (2021) · Applied and Environmental Microbiology · doi:10.1128/aem.01149-21 · Cited by 25 · see citing works
Metal Nanomaterials and Hydrolytic Enzyme-Based Formulations for Improved Antifungal Activity
Lyagin, I., Aslanli, A., Domnin, M., Stepanov, N., Senko, O. V., Maslova, O. V., & Efremenko, E. N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411359 · Cited by 24 · see citing works
“cerevisiae, Podospora anserina, and Chaetomium globosum cells, correspondently [112].”
BackgroundMolecular and cellular insight into Escherichia coli SslE and its role during biofilm maturation
Corsini, P. M., Wang, S.-Y., Rehman, S., Fenn, K., Sagar, A., Sirovica, S., Cleaver, L., Edwards-Gayle, C., Mastroianni, G., Dorgan, B., et al. (2021) · bioRxiv · doi:10.1038/s41522-022-00272-5 · Cited by 17 · see citing works
Bacterial Protein Homeostasis Disruption as a Therapeutic Intervention
Khodaparast, L., Wu, G., Khodaparast, L., Schmidt, B. Z., Rousseau, F., & Schymkowitz, J. W. H. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.681855 · Cited by 20 · see citing works
“The tandem repeat design of Pept-ins was intended to facilitate the nucleation of the aggregation process and it was inspired by the primary structure of functional amyloids (Shanmugam et al., 2019).”
MethodSpot the Difference: Function versus Toxicity in Amyloid Fibrils
Ulamec, S. M., & Radford, S. E. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.04.007 · Cited by 20 · see citing works
“In 2000, Wösten and de Vocht pioneered the term “functional amyloid” based on their work on hydrophobins, a family of small proteins in fungi that self-assemble at hydrophobic/hydrophilic surfaces and are important for growth and development [3].”
BackgroundSzulc, N., Gąsior‐Głogowska, M., Wojciechowski, J. W., Szefczyk, M., Żak, A. M., Burdukiewicz, M. J., & Kotulska, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105127 · Cited by 19 · see citing works
“Functional amyloids are spread across nearly the whole tree of life, including archaea, bacteria, fungi, protozoa, and viruses [1].”
BackgroundStructural Mimicry in Microbial and Antimicrobial Amyloids
Golan, N., Engelberg, Y., & Landau, M. (2022) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-032620-105157 · Cited by 21 · see citing works
Mourer, T., Ghalid, M. E., Pehau‐Arnaudet, G., Kauffmann, B., Loquet, A., Brûlé, S., Cabral, V., d’Enfert, C., & Bachellier‐Bassi, S. (2023) · npj Biofilms and Microbiomes · doi:10.1038/s41522-023-00371-x · Cited by 18 · see citing works
“For instance, the curli fi bre of E. coli is mainly composed of CsgA but also includes the minor curli subunit CsgB 51,52 .”
BackgroundA Coumarin-Based Array for the Discrimination of Amyloids
Trinh, N., Bhuskute, K. R., Varghese, N. R., Buchanan, J. A., Xu, Y., McCutcheon, F. M., Medcalf, R. L., Jolliffe, K. A., Sunde, M., New, E. J., et al. (2024) · ACS Sensors · doi:10.1021/acssensors.3c01334 · Cited by 17 · see citing works
Self-citationBacterial biofilm functionalization through Bap amyloid engineering
Matilla-Cuenca, L., Taglialegna, A., Gil, C., Toledo‐Arana, A., Lasa, Í., & Valle, J. (2022) · npj Biofilms and Microbiomes · doi:10.1038/s41522-022-00324-w · Cited by 16 · see citing works
Ennerfelt, H. E., Holliday, C., Shapiro, D. A., Zengeler, K. E., Bolte, A. C., Ulland, T., & Lukens, J. R. (2023) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2303760120 · Cited by 15 · see citing works
“Interestingly, fungal pathogens contain an amyloid- like structure on their cell surface that allows for pathogen adhesion and biofilm formation (100, 101), which may explain the multimodal upregulation of a fungal receptor such as CLEC7A.”
BackgroundRepurposing Antimicrobial Protegrin-1 as a Dual-Function Amyloid Inhibitor via Cross-seeding
Tang, Y., Zhang, D., & Zheng, J. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00293 · Cited by 15 · see citing works
Nair, V. G., Srinandan, C. S., Yamajala, R. B. R. D., Narbhavi, D., Anupriya, A., Prabhusaran, N., & Nagarajan, S. (2024) · Scientific Reports · doi:10.1038/s41598-024-65780-0 · Cited by 14 · see citing works
Ngah, W. Z. W., Ahmad, H. F., Ankasha, S. J., Makpol, S., & Tooyama, I. (2024) · Antioxidants · doi:10.3390/antiox13121504 · Cited by 12 · see citing works
Hierarchical organization and assembly of the archaeal cell sheath from an amyloid-like protein
Wang, H., Zhang, J., Toso, D. B., Liao, S., Sedighian, F., Gunsalus, R. P., & Zhou, Z. H. (2023) · Nature Communications · doi:10.1038/s41467-023-42368-2 · Cited by 11 · see citing works
“Other microbial functional amyloids are known, including the extracellular fi brillar structures described in both Gram-negative and positive bacteria with roles in bio fi lm formation and adhesion, for example, the curli, Bap and Esp orthologs 39 , P1 adhesions, Harpins and modulins (see review 40 ).”
The Intricate Interplay: Microbial Metabolites and the Gut‐Liver‐Brain Axis in Parkinson's Disease
Kishanchand, D. K., A., A. K. K., Chandrababu, K., Philips, C. A., Sivan, U., & Chakrapani, P. S. B. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70016 · Cited by 11 · see citing works
“These amy-loids can accumulate neural proteins such as A-β, α-syn, and tau (Friedland, McMillan, and Kurlawala 2020; Shanmugam et al. 2019).”
Visualizing Amyloid Assembly at the Nanoscale: Insights from Super‐Resolution Imaging
Bhuskute, K. R., Kikuchi, K., Luo, Z., & Kaur, A. (2024) · Analysis & Sensing · doi:10.1002/anse.202400001 · Cited by 10 · see citing works
Effects of Shear Rate and Protein Concentration on Amyloidogenesis via Interfacial Shear
Adam, J. A., Middlestead, H. R., Debono, N. E., & Hirsa, A. H. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c05171 · Cited by 10 · see citing works
Yarmola, E. G., Ishkov, I. P., di Cologna, N. D. M., Menashe, M., Whitener, R. L., Long, J. R., Abranches, J., Hagen, S. J., & Brady, L. J. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.01661-22 · Cited by 10 · see citing works
Qasemi, A., Rahimi, F., & Katouli, M. (2021) · Pathogens and Global Health · doi:10.1080/20477724.2021.2011578 · Cited by 10 · see citing works
“coli requires the presences of bacterial structures such as curli fimbriae and exopolysaccharides, specifically cellulose, which are the most essential biofilm matrix compounds involved in cell-surface/cell–cell interactions, enabling bacteria to colonize biotic and abiotic surfaces [7].”
BackgroundMatrix inhibition by Salmonella excludes uropathogenic E. coli from biofilm
Miryala, S., Nair, V. G., Chandramohan, S., & Srinandan, C. S. (2020) · FEMS Microbiology Ecology · doi:10.1093/femsec/fiaa214 · Cited by 8 · see citing works
Ábrahám, Á., Massignan, F., Gyulai, G., Katona, M. T., Taricska, N., & Kiss, É. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113219 · Cited by 8 · see citing works
Battle, A. R., Norton, R. S., Böcking, T., Noji, H., Kim, K. K., & Nagayama, K. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00553-y · Cited by 8 · see citing works
AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins
Yang, L., Hicks, D. J., Russo, P. S., & McShan, A. C. (2025) · Protein Science · doi:10.1002/pro.70279 · Cited by 8 · see citing works
Identification of Genes in Xanthomonas euvesicatoria pv. rosa That Are Host Limiting in Tomato
Fan, Q., Bibi, S., Vallad, G. E., Goss, E. M., Hurlbert, J. C., Paret, M. L., Jones, J. B., & Timilsina, S. (2022) · Plants · doi:10.3390/plants11060796 · Cited by 6 · see citing works
“Multiple sequence alignment of the amino acid sequences of XopA from Xp 91-118 and Xe07 with the amino acid sequences of HpaG and Hpa1 from X. oryzae pv. oryzicola and X. oryzae pv. oryzae (Figure 1B) show that all four proteins have the two domains, with 100% amino acid identity shared between all four proteins in re…”
BackgroundResultInfluential2019—A year in Biophysical Reviews
Hall, D. R. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00607-1 · Cited by 5 · see citing works
“…in the Issue (from the very many interesting contributions), I recommend the following review articles on the topics of functional amyloids (Shanmugam et al. 2019); cellular sensing of compression (Chen et al. 2019); mechanical control of disulfide bond formation (Passam and Chiu 2019);…”
BackgroundAgha, M. M., Tavili, E., & Dabirmanesh, B. (2024) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.03.009 · Cited by 5 · see citing works
Valette, N., Renou, J., Boutilliat, A., Fernandez-Gonzalez, A. J., Christophe, V. G., Silar, P., Guyeux, C., Charr, J., Cuenot, S., Rosé, C., et al. (2021) · Environmental Microbiology · doi:10.1111/1462-2920.15381 · Cited by 5 · see citing works
Charnley, M., Islam, S., Bindra, G. K., Engwirda, J., Ratcliffe, J., Zhou, J., Mezzenga, R., Hulett, M. D., Han, K., Berryman, J. T., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1201481/v1 · Cited by 5 · see citing works
The Cryo-EM Structures of two Amphibian Antimicrobial Cross-β Amyloid FibrilsPreprint
Bücker, R., Seuring, C., Cazey, C., Veith, K., García-Alai, M., Grünewald, K., & Landau, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.08.475498 · Cited by 5 · see citing works
De Novo Amyloid Peptide–Polymer Blends with Enhanced Mechanical and Biological Properties
Wang, X., Mondal, M., Jankoski, P. E., Kemp, L. K., Clemons, T. D., Rangachari, V., & Morgan, S. E. (2025) · ACS Applied Polymer Materials · doi:10.1021/acsapm.4c04020 · Cited by 3 · see citing works
Analysis of Natural and Engineered Amyloid Aggregates by Spectroscopic and Scattering Techniques
Heyn, T. R., Garamus, V. M., Steffen‐Heins, A., Schwarz, K., & Keppler, J. K. (2021) · Springer proceedings in physics · doi:10.1007/978-3-030-80924-9_11 · Cited by 3 · see citing works
Catalytic physiological amyloids
Arad, E., & Jelinek, R. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.01.014 · Cited by 3 · see citing works
Zajkowski, T., Lee, M., Mondal, S. S., Carbajal, A., Dec, R., Brennock, P. D., Piast, R. W., Snyder, J., Bense, N. B., Dzwolak, W., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.20.212902 · Cited by 3 · see citing works
Protein aggregates carry non-genetic memory in bacteria after stresses
KUKHARENKO, O., Terzova, V., & Zubova, G. (2020) · Biopolymers and Cell · doi:10.7124/bc.000a3f · Cited by 2 · see citing works
“These include binding to thioflavin T and Congo Red dyes with resultant increased fluorescence emission at 485 nm and green birefringence, respectively, fibrillike morphology and a β-sheet rich structure as demonstrated by biophysical investigations [25].”
BackgroundInfluentialChemical Approaches for Array Based Detection of Amyloids
Simon, P. M., Xu, Y., & Kaur, A. (2025) · Advanced Sensor Research · doi:10.1002/adsr.202500108 · Cited by 1 · see citing works
Encapsulated Control: Shaping Insulin Fibrillation through Polymer Confinement
Murmiliuk, A., Filippov, S. K., Iwase, H., Schwärzer, K., Allgaier, J., & Rădulescu, A. (2025) · Biomacromolecules · doi:10.1021/acs.biomac.5c02110 · Cited by 1 · see citing works
Beg, A. Z., & Khan, A. U. (2020) · Biophysical Reviews · doi:10.1007/s12551-020-00759-5 · Cited by 1 · see citing works
Islam, S., Charnley, M., Bindra, G. K., Ratcliffe, J., Zhou, J., Mezzenga, R., Hulett, M. D., Han, K., Berryman, J. T., & Reynolds, N. P. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.24.469537 · Cited by 1 · see citing works
Competitive exclusion of uropathogenic E. coli biofilm by Salmonella through matrix inhibitionPreprint
Miryala, S., Chandramohan, S., & Srinandan, C. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.18.911263
Fluorescence Detection of Peptides, Proteins, Glycans
Demchenko, A. P. (2023) · Springer eBooks · doi:10.1007/978-3-031-19089-6_12
Positive and Negative Aspects of Protein Aggregation Induced by Phase Separation
Kurokawa, R. (2023) · Springer eBooks · doi:10.1007/978-981-99-4886-4_5
Amyloid peptide – synthetic polymer blends with enhanced mechanical and biological propertiesPreprint
Wang, X., Mondal, M., Jankoski, P. E., Kemp, L. K., Clemons, T. D., Rangachari, V., & Morgan, S. E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.29.605712
Amyloids. Evolutionary Past and Biotechnological Future
Nevzglyadova, O. V., Mikhailova, E. V., & Soidla, T. R. (2024) · Cell and Tissue Biology · doi:10.1134/s1990519x24700512
“Research over the past 10–15 years has shown that amyloids can not only be positively functional (Lall et al., 2021), but even realize some key biological functions (Shanmugam et al., 2019; Rubel et al., 2020; Levkovich et al., 2021; Santos and Ventura, 2021).”
Antimicrobial peptides act as a component of brain immunity against microbes in Alzheimer’s disease
Chandrashekar, M., Velmurugan, G., Mishra, A., & Chinnathambi, S. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.016
Vinutha, A. S., Akshay, S., Agash, S. G. S., Chandrasekhar, G., Bhattacharya, A., & Rajasekaran, R. (2026) · Archives of Microbiology · doi:10.1007/s00203-026-04797-7
“Considering the role of functional amyloids in biofilm formation, surface adhesion, and antibiotic resis - tance, targeting these structures is crucial (Admane and Biswas 2025 , Akbey and Andreasen 2022 , Matilla-Cuenca et al. 2021, Shanmugam et al. 2019).”
Passalacqua, E., Barberi, G., Amico, P., Martino, S. D., & Rosa, M. D. (2026) · RSC Medicinal Chemistry · doi:10.1039/d6md00420b
Intrinsic Disorder as a New Frontier in Antimicrobial Resistance and Bacterial Fitness
Callaghan, J., Ryan, M. P., Hudson, S. P., & Thompson, D. (2026) · MicrobiologyOpen · doi:10.1002/mbo3.70415
“Desiccation tolerance is a characteristic feature of curliated bacteria, and microbes with an upregulated expression of amyloid‐encoding genes are innately resistant to drying (Shanmugam et al. 2019).”
Kumar, R., Aves, M., & Mitra, D. (2026) · IGI Global eBooks · doi:10.4018/979-8-2600-0206-3.ch001
- Authors
- Shanmugam, N., Baker, M. O. D. G., Ball, S. R., Steain, M., Pham, C. L. L., & Sunde, M.
- Affiliations
- The University of Sydney (AU)
- Corresponding author
- Sunde, Margaret
- Venue
- Biophysical Reviews
- Published
- 2019-05-02
- Volume
- 11
- Issue
- 3
- Pages
- 287-302
- ISSN
- 1867-2450 (ISSN-L)
- 1867-2469
- PMC
- PMC6557962
- OpenAlex
- W2943742239
- Semantic Scholar
- b0e8d3dc3822c8e0bbe9b1ed0806292c3cb026c9
- Cited by
- 75
- References
- 149
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 8 · 2023: 8 · 2022: 14 · 2021: 17 · 2020: 13 · 2019: 4 · 2018: 1
- FWCI
- 1.06
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Biophysical Reviews (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Australian Government
- Australian Research Council (DP180101275)
- 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 › Prion Diseases and Protein Misfolding
- Keywords
- functional amyloids, protein self-assembly, cross-β structure, bacterial adhesion, pathogenicity, host-pathogen interaction, thioflavin T, Congo red, amyloid structure
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