Skip to content
Main menu
  • Main page
  • Discover
  • Unexpected connections
  • Topics
  • Random article
  • Search
Your library
  • Saved articles
  • Recent discoveries
  • Rabbit-hole trails
Topic areas
  • Computer Science
  • Mathematics
  • Physics
  • Engineering
  • Biology
  • Economics
  • Curiosities
WikiholeDeeper into Wikipedia
EnglishEN
  • Saved
  • History

  • Article text and media come live from Wikipedia via the official MediaWiki API and are available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply. Each article links to its source and revision.
  • WikiHole is an independent project and is not affiliated with the Wikimedia Foundation.
  • How ranking works
  • All topics
  • Reading history
  • Random article
  • MediaWiki API

S-layer

  • Article
  • Rabbit hole
  • Read
  • View history
Tools
Actions
  • Read
  • View history
General
  • Recent changes
  • Related articles
  • Random discovery
This article
Reading time
10 min
Topic
Biology
Quality
Start-class
Views
216 in 14 days
Last edited
22 Oct 2026
Print/export
  • Printable version
In other projects
  • Wikidata item
From Wikipedia, the free encyclopedia
Rabbit hole:
  1. S-layer

An S-layer (surface layer) is a part of the cell envelope found in almost all archaea, as well as in many types of bacteria.123 The S-layers of both archaea and bacteria consists of a monomolecular layer composed of only one (or, in a few cases, two) identical proteins or glycoproteins, the latter case making it a type of glycocalyx.234 This structure is built via self-assembly and encloses the whole cell surface. Thus, the S-layer protein can represent up to 15% of the whole protein content of a cell.5 S-layer proteins are poorly conserved or not conserved at all, and can differ markedly even between related species. Depending on species, the S-layers have a thickness between 5 and 25 nm and possess identical pores 2–8 nm in diameter.2367

The terminology "S-layer" was used the first time in 1976. The general use was accepted at the "First International Workshop on Crystalline Bacterial Cell Surface Layers, Vienna (Austria)" in 1984, and in the year 1987 S-layers were defined at the Workshop on "Crystalline Bacterial Cell Surface Layers", Vienna as "Two-dimensional arrays of proteinaceous subunits forming surface layers on prokaryotic cells" (see "Preface", page VI in Sleytr "et al. 1988"). For a brief summary on the history of S-layer research see "References" A comprehensive historical account of the development of fundamental and applied S-layer research is given in the following current review.

8
European Molecular Biology Organization
9
.
2
6
3

Loading the rest of the article…

Recent changes

Rabbit hole

Where S-layer leads. Every connection below has a source: a link in this article, a shared Wikipedia category, or CirrusSearch text similarity. Articles already on your trail are left out.

Contents
  • (Top)
  • Location of S-layers
  • Biological functions of the S-layer
  • S-layer structure
  • Self-assembly
  • Application
  • References
  • Recent changes
  • Rabbit hole
Contents
Contents8 sections
  • (Top)
  • Location of S-layers
  • Biological functions of the S-layer
  • S-layer structure
  • Self-assembly
  • In vivo assembly
  • In vitro assembly
  • Application
  • References
  • Recent changes
  • Rabbit hole
Categories:
  • Cell anatomy
  • Membrane biology
  • S-layers

1,149 words · 40 references · revision 1381453661 · CC BY-SA 4.0

General
  • Recent changes
  • Related articles
  • Random discovery
This article
Reading time
10 min
Topic
Biology
Quality
Start-class
Views
216 in 14 days
Last edited
22 Oct 2026

Key concepts

  • Archaea3
  • Bacteria3
  • Cell envelope1
  • Monolayer1
  • Proteins1
  • Glycoproteins1
  • Glycocalyx1
  • Self-assembly1
  • European Molecular Biology Organization1
  • Gram-negative2

The articles this one links to most, weighted towards the introduction.

Print/export
  • Printable version
In other projects
  • Wikidata item

Location of S-layers

TEM micrograph of a freeze-etched and metal shadowed preparation of the archaeum Methanocorpusculum sinense. The S-layer exhibits hexagonal (p6) lattice symmetry with a center-to-center spacing of approx. 16 nm. The rope like structure is a flagellum that has collapsed on the cell surface during cell centrifugation 10 Creative Commons Attribution 4.0 International (CC BY 4.0) licence .
Schematic illustration of the supramolecular architecture of the major classes of prokaryotic cell envelopes containing surface (S) layers. S-layers in archaea with glycoprotein lattices as exclusive wall component are composed either of mushroom-like subunits with pillar-like, hydrophobic trans-membrane domains (a), or lipid-modified glycoprotein subunits (b). Individual S-layers can be composed of glycoproteins possessing both types of membrane anchoring mechanisms. Few archaea possess a rigid wall layer (e.g. pseudomurein in methanogenic organisms) as intermediate layer between the plasma membrane and the S-layer (c). In Gram-positive bacteria (d) the S-layer (glyco)proteins are bound to the rigid peptidoglycan-containing layer via secondary cell wall polymers. In Gram-negative bacteria (e) the S-layer is closely associated with the lipopolysaccharide of the outer membrane. Figure and figure legend were copied from Sleytr et al. 2025,3 which is available under a Creative Commons Attribution 4.0 International (CC BY 4.0) licence .
Schematic drawing of the different S-layer lattice types. The proteins of one morphological unit are shown in red. For a more detailed description of the symmetry properties of S-layers see.11 Creative Commons Attribution 4.0 International (CC BY 4.0) licence .
  • In Gram-negative bacteria, S-layers are associated to the lipopolysaccharides via protein–carbohydrate interactions.23
  • In Gram-positive bacteria whose S-layers often contain surface layer homology (SLH) domains, the binding occurs to the peptidoglycan and to a secondary cell wall polymer (e.g., teichoic acids). In the absence of SLH domains, the binding occurs via electrostatic interactions between the positively charged N-terminus of the S-layer protein and a negatively charged secondary cell wall polymer. In Lactobacilli the binding domain may be located at the C-terminus.2
  • In Gram-negative archaea, S-layer proteins possess a hydrophobic anchor that is associated with the underlying lipid membrane.12
  • In Gram-positive archaea, the S-layer proteins bind to pseudomurein or to methanochondroitin.12

Biological functions of the S-layer

For many bacteria, the S-layer represents the outermost interaction zone with their respective environment.2312 Its functions are very diverse and vary from species to species. In many archaeal species the S-layer is the only cell wall component and, therefore, is important for mechanical and osmotic stabilization.2313 The S-layer is considered to be porous, which contributes to many of its functions.237 A most relevant general function of S-layers of both, bacteria and archaea, seems to be their excellent anti-fouling properties.231415 In Archaea that possess S-Layers as the exclusive cell wall component, a general function of S-layer lattices is that of a cell shape-determining/maintaining scaffold.101617 For an overview of functions of S-layers, see.23 The spectrum of functions associated with S-layers include:

S-layer structure

While ubiquitous among Archaea, and common in bacteria, the S-layers of diverse organisms have unique structural properties, including symmetry and unit cell dimensions, due to fundamental differences in their constituent building blocks.728 Sequence analyses of S-layer proteins have predicted that S-layer proteins have sizes of 40-200 kDa and may be composed of multiple domains some of which may be structurally related.7 Since the first evidence of a macromolecular array on a bacterial cell wall fragment in the 1950s,29 S-layer structures have been investigated extensively by electron microscopy. These studies have provided useful information on overall S-layer morphology.

In general, S-layers exhibit either oblique (p1, p2), square (p4) or hexagonal (p3, p6) lattice symmetry. Depending on the lattice symmetry, each morphological unit of the S-layer is composed of one (p1), two (p2), three (p3), four (p4), or six (p6) identical protein subunits. The center-to-center spacing (or unit cell dimensions) between these subunits range from 4 to 35 nm.237

For example, high-resolution structures of an archaeal S-layer protein (MA0829 from Methanosarcina acetivorans C2A) of the Methanosarcinales S-layer Tile Protein family and a bacterial S-layer protein (SbsB), from Geobacillus stearothermophilus PV72, have been determined by X-ray crystallography.30 In contrast with existing crystal structures, which have represented individual domains of S-layer proteins or minor proteinaceous components of the S-layer, the MA0829 and SbsB structures have allowed high resolution models of the . and . S-layers to be proposed. These models exhibit hexagonal (p6) and oblique (p2) symmetry, for . and . S-layers, respectively, and their molecular features, including dimensions and porosity, are in good agreement with data from electron microscopy studies of archaeal and bacterial S-layers.

Self-assembly

In vivo assembly

Assembly of a highly ordered coherent monomolecular S-layer array on a growing cell surface requires a continuous synthesis of a surplus of S-layer proteins and their translocation to sites of lattice growth.231233 Moreover, information concerning this dynamic process were obtained from reconstitution experiments with isolated S-layer subunits on cell surfaces from which they had been removed (homologous reattachment) or on those of other organisms (heterologous reattachment).3834

In vitro assembly

S-layer proteins have the natural capability to self-assemble into regular monomolecular arrays in solution and at interfaces, such as solid supports, the air-water interface, lipid films, liposomes, emulsomes, nanocapsules, nanoparticles or micro beads.233536 S-layer crystal growth follows a non-classical pathway in which a final refolding step of the S-layer protein is part of the lattice formation.3738

Application

Native S-layer proteins have already been used three decades ago in the development of biosensors and ultrafiltration membranes.23 Subsequently, S-layer fusion proteins with specific functional domains (e.g. enzymes, ligands, mimotopes, antibodies or antigens) allowed to investigate completely new strategies for functionalizing surfaces in the life sciences, such as in the development of novel affinity matrices, mucosal vaccines, biocompatible surfaces, micro carriers and encapsulation systems, or in the material sciences as templates for biomineralization.23323940

References

  1. 1Albers SV, Meyer BH (2011). "The archaeal cell envelope". Nature Reviews Microbiology. 9 (6): 414–426. doi:10.1038/nrmicro2576. PMID 21572458. S2CID 10297797.
  2. 2Sleytr UB, Schuster B, Egelseer EM, Pum D (2014). "S-layers: Principles and Applications". FEMS Microbiology Reviews. 38 (5): 823–864. doi:10.1111/1574-6976.12063. PMC 4232325. PMID 24483139.
  3. 3Sleytr UB, Pum D (2025). "S-layers: from a serendipitous discovery to a toolkit for nanobiotechnology". Quarterly Reviews of Biophysics. 58 (e4) e4. :. .
  • protection against bacteriophages, Bdellovibrios, and phagocytosis
  • resistance against low pH
  • barrier against high-molecular-weight substances (e.g., lytic enzymes)
  • adhesion (for glycosylated S-layers)
  • stabilization of the membrane (e.g. the SDBC in Deinococcus radiodurans)1819
  • resistance against electromagnetic stress (e.g. ionizing radiations and high temperatures)1819
  • provision of adhesion sites for exoproteins 20
  • provision of a periplasmic compartment in Gram-positive prokaryotes together with the peptidoglycan and the cytoplasmic membranes 12
  • biomineralization212223
  • molecular sieve and barrier function2242526
  • A great example of a bacterium which utilizes the biological functions of the S-layer is Clostridioides difficile. In C. difficile, the S-layer has helped with biofilm formation, host cell adhesion, and immunomodulation through cell signaling of the host response.27

    31
    M
    acetivorans
    G
    stearothermophilus
    M
    acetivorans
    G
    stearothermophilus
    3
    7
    28

    Finally, in connection with questions of structure-function investigations on S-layers, it should be mentioned that the recent introduction of SymProFold,7 which utlizes the high accuracy of AlphaFold-Multimer predictions to derive symmetrical assemblies from protein sequeces has proven to be a groundbreaking method for the accurate structural prediction of S-layer arrays. The predicted models could be vallidated using available experimental data at the cellular level, and additional crystal structures were obtained to confirm the symmetry and interfaces of numerous SymProFold assemblies. Thus, this methodological approach to the structural elucidation of S-layers opens possibilities for exploring functionalities and designing targeted applications in diverse fields such as nanotechnology, biotechnology, nanomedicine, and environmental sciences.2732

    doi
    10.1017/S0033583524000106
    PMID
    39819733
  • 4Rodrigues-Oliveira, Thiago; Belmok, Aline; Vasconcellos, Deborah; Schuster, Bernhard; Kyaw, Cynthia M. (2017-12-22). "Archaeal S-Layers: Overview and Current State of the Art". Frontiers in Microbiology. 8: 2597. doi:10.3389/fmicb.2017.02597. ISSN 1664-302X. PMC 5744192. PMID 29312266.
  • 5Sleytr U, Messner P, Pum D, Sára M (1993). "Crystalline bacterial cell surface layers". Mol. Microbiol. 10 (5): 911–6. doi:10.1111/j.1365-2958.1993.tb00962.x. PMID 7934867. S2CID 86119414.
  • 6Sleytr UB (2016). Curiosity and Passion for Science and Art. Series in Structural Biology. Vol. 7. Singapore: World Scientific Publishing. doi:10.1142/10084. ISBN 978-981-3141-81-0.
  • 7Buhlheller C, Sagmeister T, Grininger C, Gubensak N, Sleytr UB, Uson I, Pavkov-Keller T (2024). "SymProFold: Structural prediction of symmetrical biological assemblies". Nat Commun. 15 (1) 8152. Bibcode:2024NatCo..15.8152B. doi:10.1038/s41467-024-52138-3. hdl:10261/372119. PMC 11410804. PMID 39294115.
  • 8Sleytr UB (1976). "Self-assembly of the hexagonally and tetragonally arranged subunits of bacterial surface layers and their reattachment to cell walls". J. Ultrastruct. Res. 55 (3): 360–367. doi:10.1016/S0022-5320(76)80093-7. PMID 6800.
  • 9Sleytr UB, Messner P, Pum D, Sára M (1988). Sleytr UB, Messner P, Pum D, Sára M (eds.). Crystalline Bacterial Cell Surface Layers. Berlin: Springer. doi:10.1007/978-3-642-73537-0. ISBN 978-3-540-19082-0. S2CID 20244135.
  • 10Pum D, Messner P, Sleytr UB (1991). "Role of the S layer in morphogenesis and cell division of the Archaebacterium Methanocorpusculum sinense". J. Bacteriol. 173 (21): 6865–6873. doi:10.1128/jb.173.21.6865-6873.1991. PMC 209039. PMID 1938891.
  • 11Pum D, Breitwieser A, Sleytr UB (2021). "Patterns in Nature - S-Layer Lattices of Bacterial and Archaeal Cells". Crystals. 11 (8): 869. Bibcode:2021Cryst..11..869P. doi:10.3390/cryst11080869.
  • 12Sleytr, UB; Beveridge, TJ (1999). "Bacterial S-layers". Trends Microbiol. 7 (6): 253–260. doi:10.1016/s0966-842x(99)01513-9. PMID 10366863.
  • 13Pfeifer, Kevin; Ehmoser, Eva-Kathrin; Rittmann, Simon K.-M. R.; Schleper, Christa; Pum, Dietmar; Sleytr, Uwe B.; Schuster, Bernhard (2022-07-21). "Isolation and Characterization of Cell Envelope Fragments Comprising Archaeal S-Layer Proteins". Nanomaterials. 12 (14): 2502. doi:10.3390/nano12142502. ISSN 2079-4991. PMC 9320373. PMID 35889727.
  • 14Rothbauer M, Küpcü S, Sticker D, Sleytr UB, Ertl P (2013). "Exploitation of S-layer Anisotropy: pH-dependent Nanolayer Orientation for Cellular Micropatterning". ACS Nano. 7 (9): 8020–8030. doi:10.1021/nn403198a. PMID 24004386.
  • 15Sleytr, U. B.; Schuster, B. (2026). "S-layer (Glyco)protein lattices: Biophysical principles of antifouling at prokaryotic interfaces". Quarterly Reviews of Biophysics. 59 e14. doi:10.1017/S0033583526100213.
  • 16Messner P, Pum D, Sára M, Stetter KO, Sleytr UB (1986). "Ultrastructure of the cell envelope of the archaebacteria Thermoproteus tenax and Thermoproteus neutrophilus". J. Bacteriol. 166 (3): 1046–1054. doi:10.1128/jb.166.3.1046-1054.1986. PMC 215230. PMID 3086286.
  • 17Zink IA, Pfeifer K, Wimmer E, Sleytr UB, Schuster B, Schleper C (2019). "CRISPR-mediated gene silencing reveals involvement of the archaeal S-layer in cell division and virus infection". Nat. Commun. 10 4797. Bibcode:2019NatCo..10.4797Z. doi:10.1038/s41467-019-12745-x. PMC 6805947. PMID 31641111.
  • 18Farci D, Slavov C, Tramontano E, Piano D (2016). "The S-layer Protein DR_2577 Binds Deinoxanthin and under Desiccation Conditions Protects against UV-Radiation in Deinococcus radiodurans". Frontiers in Microbiology. 7: 155. doi:10.3389/fmicb.2016.00155. PMC 4754619. PMID 26909071.
  • 19Farci D, Slavov C, Piano D (2018). "Coexisting properties of thermostability and ultraviolet radiation resistance in the main S-layer complex of Deinococcus radiodurans". Photochem Photobiol Sci. 17 (1): 81–88. Bibcode:2018PcPbS..17...81F. doi:10.1039/c7pp00240h. PMID 29218340.
  • 20Egelseer E, Schocher I, Sára M, Sleytr UB (1995). "The S-layer from Bacillus stearothermophilus DSM 2358 functions as adhesion site for a high-molecular-weight amylase". J Bacteriol. 177 (6): 1444–1451. doi:10.1128/jb.177.6.1444-1451.1995. PMC 176758. PMID 7533757.
  • 21Schultze-Lam S, Harauz G, Beveridge TJ (1992). "Participation of a cyanobacterial S layer in fine-grain mineral formation". J. Bacteriol. 174 (24): 7971–7981. doi:10.1128/jb.174.24.7971-7981.1992. PMC 207533. PMID 1459945.
  • 22Shenton W, Pum D, Sleytr UB, Mann S (1997). "Synthesis of CdS superlattices using self-assembled bacterial S-layers". Nature. 389 (6651): 585–587. doi:10.1038/39287. S2CID 4317884.
  • 23Mertig M, Kirsch R, Pompe W, Engelhardt H (1999). "Fabrication of highly oriented nanocluster arrays by biomolecular templating". Eur. Phys. J. D. 9 (1): 45–48. Bibcode:1999EPJD....9...45M. doi:10.1007/s100530050397. S2CID 120507258.
  • 24Sára M, Sleytr, UB (1987). "Production and characteristics of ultrafiltration membranes with uniform pores from two-dimensional arrays of proteins". J. Membr. Sci. 33 (1): 27–49. doi:10.1016/S0376-7388(00)80050-2.
  • 25von Kügelgen, Andriko; Cassidy, C. Keith; van Dorst, Sofie; Pagani, Lennart L.; Batters, Christopher; Ford, Zephyr; Löwe, Jan; Alva, Vikram; Stansfeld, Phillip J.; Bharat, Tanmay A. M. (6 June 2024). "Membraneless channels sieve cations in ammonia-oxidizing marine archaea". Nature. 630 (8015): 230–236. Bibcode:2024Natur.630..230V. doi:10.1038/s41586-024-07462-5. PMC 11153153. PMID 38811725.
  • 26Schuster B, Sleytr UB (2021). "S-Layer Ultrafiltration Membranes". Membranes. 11 (4): 275. doi:10.3390/membranes11040275. PMC 8068369. PMID 33918014.
  • 27Ormsby, Michael J.; Vaz, Filipa; Kirk, Joseph A.; Barwinska-Sendra, Anna; Hallam, Jennifer C.; Lanzoni-Mangutchi, Paola; Cole, John; Chaudhuri, Roy R.; Salgado, Paula S.; Fagan, Robert P.; Douce, Gillian R. (2023-06-29). "An intact S-layer is advantageous to Clostridioides difficile within the host". PLOS Pathogens. 19 (6) e1011015. doi:10.1371/journal.ppat.1011015. ISSN 1553-7374. PMC 10310040. PMID 37384772.
  • 28Pavkov-Keller T, Howorka S, Keller W (2011). "The structure of bacterial S-layer proteins". Molecular Assembly in Natural and Engineered Systems. Progress in Molecular Biology and Translational Science V. 103. Vol. 103. pp. 73–130. doi:10.1016/B978-0-12-415906-8.00004-2. ISBN 978-0-12-415906-8. PMID 21999995.
  • 29Houwink, AL (1953). "A macromolecular mono-layer in the cell wall of Spirillum spec". Biochim Biophys Acta. 10 (3): 360–6. doi:10.1016/0006-3002(53)90266-2. PMID 13058992.
  • 30Arbing MA, Chan S, Shin A, Phan T, Ahn CJ, Rohlin L, Gunsalus RP (2012). "Structure of the surface layer of the methanogenic archaean Methanosarcina acetivorans". Proc Natl Acad Sci U S A. 109 (29): 11812–7. Bibcode:2012PNAS..10911812A. doi:10.1073/pnas.1120595109. PMC 3406845. PMID 22753492.
  • 31Baranova E, Fronzes R, Garcia-Pino A, Van Gerven N, Papapostolou D, Péhau-Arnaudet G, Pardon E, Steyaert J, Howorka S, Remaut H (2012). "SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly" (PDF). Nature. 487 (7405): 119–22. Bibcode:2012Natur.487..119B. doi:10.1038/nature11155. PMID 22722836. S2CID 4389187.
  • 32Ilk N, Egelseer EM, Sleytr UB (2011). "S-layer fusion proteins - construction principles and applications". Curr. Opin. Biotechnol. 22 (6): 824–831. doi:10.1016/j.copbio.2011.05.510. PMC 3271365. PMID 21696943.
  • 33Fagan RP, Fairweather NF (2014). "Biogenesis and functions of bacterial S-layers" (PDF). Nature Reviews. Microbiology. 12 (3): 211–222. doi:10.1038/nrmicro3213. PMID 24509785. S2CID 24112697.
  • 34Sleytr UB (1975). "Heterologous reattachment of regular arrays of glycoproteins on bacterial surfaces". Nature. 257 (5525): 400–402. Bibcode:1975Natur.257..400S. doi:10.1038/257400a0. PMID 241021. S2CID 4298430.
  • 35Pum D, Sleytr UB (2014). "Reassembly of S-layer proteins". Nanotechnology. 25 (31) 312001. Bibcode:2014Nanot..25E2001P. doi:10.1088/0957-4484/25/31/312001. PMID 25030207. S2CID 39889746.
  • 36Schuster B, Sleytr UB (2014). "Biomimetic interfaces based on S-layer proteins, lipid membranes and functional biomolecules". J. R. Soc. Interface. 11 (96) 20140232. doi:10.1098/rsif.2014.0232. PMC 4032536. PMID 24812051.
  • 37Chung S, Shin SH, Bertozzi CR, De Yoreo JJ (2010). "Self-catalyzed growth of S layers via an amorphous-to-crystalline transition limited by folding kinetics". Proc. Natl. Acad. Sci. USA. 107 (38): 16536–16541. Bibcode:2010PNAS..10716536C. doi:10.1073/pnas.1008280107. PMC 2944705. PMID 20823255.
  • 38Shin SH, Chung S, Sanii B, Comolli LR, Bertozzi CR, De Yoreo JJ (2012). "Direct observation of kinetic traps associated with structural transformations leading to multiple pathways of S-layer assembly". Proc. Natl. Acad. Sci. USA. 109 (32): 12968–12973. Bibcode:2012PNAS..10912968S. doi:10.1073/pnas.1201504109. PMC 3420203. PMID 22822216.
  • 39Sleytr, Uwe B; Schuster, Bernhard (2026). "S-layers as natural building blocks for nanobiotechnology and synthetic biology". Current Opinion in Microbiology. 92: 102787. doi:10.1016/j.mib.2026.102787.{{cite journal}}: CS1 maint: article number as page number (link)
  • 40Qing R, Xue MT, Zhao JY, Wu LD, Breitwieser A, Smorodina E, Schubert T, Azzellino G, Jin D, Kong J, Palacios T, Sleytr UB, Zhang SG (2023). "Scalable biomimetic sensing system with membrane receptor dual-monolayer probe and graphene transistor arrays". Science Advances. 9 (29) eadf1402. Bibcode:2023SciA....9F1402Q. doi:10.1126/sciadv.adf1402. hdl:10852/108278. PMC 10361598. PMID 37478177.
  • Created
    5 Sept 2004
    History
    193 edits
    104 contributors
    2 edits in the last 30 days
    Last edited
    22 Oct 2026

    193 revisions in total · 104 contributors · +58 / 0 bytes across 2 edits by 2 contributors in the last 30 days

    1. 22 Oct 2026, 16:36 UTCMausfieldNo edit summary+41diff
    2. 12 Oct 2026, 05:52 UTCOAbotmOpen access bot: doi updated in citation with #oabot.+17diff
    3. 9 Oct 2026, 09:29 UTCBSnanomRecent references have been added+236diff
    4. 4 Sept 2026, 21:30 UTCRkottadded Category:S-layers using HotCat+22diff
    5. 11 Aug 2026, 12:17 UTCJCW-CleanerBotmmark free doi+35diff
    6. 20 Mar 2026, 21:25 UTCInternetowyGołąbnavbox+13diff
    7. 23 Feb 2026, 08:42 UTCHekkerz§ growthexperiments-addlink-summary-summary:3|0|0+12diff
    8. 6 Feb 2026, 05:48 UTCSteel1943mfix common MOS:REFSPACE spacing errors, replaced: ) <ref → )<ref (2), /ref>A → /ref> A−1diff

    View full revision history

    Created
    5 Sept 2004
    History
    193 edits
    104 contributors
    2 edits in the last 30 days
    Last edited
    22 Oct 2026

    Go deeper: linked from this article

    • Linked from the introduction

      Archaea

      Domain of organisms

      Archaea (ar-KEE-ə) is a domain of organisms.

      60 min readGo deeper
    • Linked from the introduction

      Bacteria

      Domain of microorganisms

      Bacteria are ubiquitous, mostly free-living organisms often consisting of one biological cell. They constitute a large domain of prokaryotic microorganisms.

      58 min readGo deeper
    • Linked from the introduction

      Protein

      Biomolecule consisting of chains of amino acid residues

      Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues.

      39 min readGo deeper
    • Linked from the introduction

      Self-assembly

      Process in which disordered components form an organized structure or pattern

      Self-assembly is a process in which a disordered system of pre-existing components forms an organized structure or pattern as a consequence of specific, local interactions among the components themselves, without external direction.

      15 min readGo deeper
    • Linked from the introduction

      Monolayer

      Single closely packed layer of entities such as atoms

      A monolayer is a single, closely packed layer of entities, commonly atoms or molecules. Monolayers can also be made out of cells. Self-assembled monolayers form spontaneously on surfaces.

      3 min readGo deeper
    • Linked from the introduction

      Glycocalyx

      Carbohydrate-rich layer at the periphery of a cell

      The glycocalyx (pl.: glycocalyces or glycocalyxes), also referred to as the pericellular matrix and cell coat, is an external organelle consisting of a layer of glycosylated biomolecules called glycoconjugates (such as glycoproteins and glycolipids).

      7 min readGo deeper

    Adjacent: shared categories and similar text

    • Linked in “S-layer structure”

      Crystallography

      Scientific study of crystal structures

      Crystallography is the branch of science devoted to the study of molecular and crystalline structure and properties.

      8 min readGo deeper
    • Shares category “Membrane biology”

      Biofilm

      Film of microorganisms on a surface

      A biofilm is a syntrophic community of microorganisms in which cells stick to each other and often also to a surface.

      50 min readGo deeper
    • Linked in “Biological functions of the S-layer”

      PH

      Measure of the level of acidity or basicity of an aqueous solution

      In chemistry, pH (or; pee-AYCH) is a logarithmic scale used to specify the acidity or basicity of aqueous solutions.

      19 min readGo deeper
    • Linked in “Self-assembly”

      Crystal growth

      Major stage of a crystallization process

      Crystal growth is a major stage of a crystallization process, and consists of the addition of new atoms, ions, or polymer strings into the characteristic arrangement of the crystalline lattice.

      8 min readGo deeper
    • Linked in “Biological functions of the S-layer”

      Molecular sieve

      Filter material with homogeneously sized pores in the nanometer range

      A molecular sieve is a material with pores of uniform size comparable to that of individual molecules, linking the interior of the solid to its exterior.

      6 min readGo deeper
    • Linked in “Biological functions of the S-layer”

      Enzyme

      Large biological molecule that acts as a catalyst

      An enzyme is a biological macromolecule, usually a protein, that acts as a biological catalyst, accelerating chemical reactions without being consumed in the process.

      37 min readGo deeper
    • Shares category “S-layers”

      Lipopolysaccharide

      Class of molecules found in the outer membrane of gram-negative bacteria

      Lipopolysaccharide (LPS), now more commonly known as endotoxin, is a collective term for components of the outermost membrane of the cell envelope of gram-negative bacteria, such as E. coli and Salmonella with a common structural architecture.

      24 min readGo deeper
    • Linked in “Biological functions of the S-layer”

      Bacteriophage

      Virus that infects bacteria

      A bacteriophage, also known informally as a phage, is a virus that infects and replicates within bacteria. The term is derived from Ancient Greek φαγεῖν (phagein) 'to devour' and bacteria.

      33 min readGo deeper