The Bacterial Surface Layer Provides Protection against Antimicrobial Peptides

Fuente-Núñez, César de la; Mertens, Jan; Smit, John; Hancock, Robert E. W.

doi:10.1128/aem.01493-12

Cited by 33 publications

(22 citation statements)

References 26 publications

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“…However, to our knowledge there is no evidence to support this contention, and indeed S-layer proteins can serve as the receptors for bacteriophages (Plaut et al 2014). S layers may defend against antimicrobial peptides, as found for free-living and pathogenic bacteria (S ara and Sleytr 2000;De La Fuente-Nuñez et al 2012). Finally, S layer promotion of attachment may be beneficial (e.g., the ability to form transient associates, or to persist in aggregates), although marine planktonic Synechococcus appear to be predominantly free-living (Delong et al 1993;personal observation).…”

Section: Dietmentioning

confidence: 99%

The Synechococcus cell surface protein SwmA increases vulnerability to predation by flagellates and ciliates

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Fredrickson

et al. 2016

Limnology & Oceanography

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The genus Synechococcus, a major contributor to ocean productivity, exhibits wide genetic variability and a distinct biogeography of genetic subgroups. Synechococcus sp. strain WH8102 is a motile Sargasso Sea isolate belonging to Clade III in subcluster 5.1. Non‐flagellar motility in WH8102 depends upon two large cell surface proteins, SwmA and SwmB. In the marine plankton, Synechococcus can experience high rates of mortality from protist predators, suggesting strong selective pressure for the maintenance of anti‐predation defenses. We used knockout mutants deficient in large cell surface proteins (SwmA‐ and SwmB‐) to test the hypothesis that these proteins defend WH8102 against predation by ciliates and flagellates, important consumers of Synechococcus in aquatic ecosystems. Contrary to our hypothesis, we found that wild‐type WH8102 were preyed upon at higher rates than SwmA‐ by ciliates and by two of three tested flagellate species. Thus the SwmA protein, constitutively produced by WH8102, made this strain more rather than less vulnerable to predation. SwmA proteins link to form the S layer, a cell coating known to promote adhesion in other microbial systems, suggesting the predation vulnerability arises from increased attachment between consumers and prey. Given the SwmA‐related enhancement of predation rates, our findings suggest two possibilities for WH8102 and perhaps other Clade III Synechococcus: (1) factors other than protist predation select for production of the S layer; (2) ingestion actually increases fitness, by exposing digestion‐resistant cells to beneficial conditions in the food vacuole.

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Section: Dietmentioning

confidence: 99%

The Synechococcus cell surface protein SwmA increases vulnerability to predation by flagellates and ciliates

Strom

Bright

Fredrickson

et al. 2016

Limnology & Oceanography

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“…In pathogenic bacteria, S-layers may contribute to virulence by several mechanisms, including adhesion, coaggregation (Shimotahira et al 2013), antigenic variation (Thompson 2002; Spigaglia et al 2011), protection from complement or from phagocytosis (Doig et al 1992; Thompson 2002; Shimotahira et al 2013) or modulation of T-cell or cytokine responses (Wang et al 2000; Ausiello et al 2006; Sekot et al 2011; Settem et al 2013). Further, S-layer proteins may protect the bacterial cell from various environmental factors such as mechanical and osmotic stresses (Engelhardt 2007a, b), antimicrobial peptides (de la Fuente-Núñez et al 2012), radiation (Kotiranta et al 1999), changes in environmental pH (Gilmour et al 2000), bacteriophages (Howard and Tipper 1973), bacterial or eukaryotic microbial predators (Koval and Hynes 1991; Tarao et al 2009) or bacteriolytic enzymes (Lortal et al 1992). Some S-layer proteins have the potential to act as degradative enzymes (Calabi et al 2001; Ahn et al 2006; Prado Acosta et al 2008), and the S-layer protein of a marine Synechococcus strain is involved in motility (Brahamsha 1996; McCarren et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Lactobacillus surface layer proteins: structure, function and applications

Hynönen

Palva

2013

Appl Microbiol Biotechnol

221

196

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Bacterial surface (S) layers are the outermost proteinaceous cell envelope structures found on members of nearly all taxonomic groups of bacteria and Archaea. They are composed of numerous identical subunits forming a symmetric, porous, lattice-like layer that completely covers the cell surface. The subunits are held together and attached to cell wall carbohydrates by non-covalent interactions, and they spontaneously reassemble in vitro by an entropy-driven process. Due to the low amino acid sequence similarity among S-layer proteins in general, verification of the presence of an S-layer on the bacterial cell surface usually requires electron microscopy. In lactobacilli, S-layer proteins have been detected on many but not all species. Lactobacillus S-layer proteins differ from those of other bacteria in their smaller size and high predicted pI. The positive charge in Lactobacillus S-layer proteins is concentrated in the more conserved cell wall binding domain, which can be either N- or C-terminal depending on the species. The more variable domain is responsible for the self-assembly of the monomers to a periodic structure. The biological functions of Lactobacillus S-layer proteins are poorly understood, but in some species S-layer proteins mediate bacterial adherence to host cells or extracellular matrix proteins or have protective or enzymatic functions. Lactobacillus S-layer proteins show potential for use as antigen carriers in live oral vaccine design because of their adhesive and immunomodulatory properties and the general non-pathogenicity of the species.

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“…lytic enzymes), (iv) stabilization of the membrane, (v) provision of adhesion sites for exoproteins, and (vi) provision of a periplasmic compartment in Gram-positive prokaryotes together with the peptidoglycan and the cytoplasmic membranes [5,28,[87][88][89][90]. Interestingly, in the S-layer of Deinococcus radiodurans ion-gating properties of microbial S-layer protein arrays have also been determined [91].…”

Section: S-layer Proteinsmentioning

confidence: 99%

Biomimetic interfaces based on S-layer proteins, lipid membranes and functional biomolecules

Schuster

Sleytr

2014

J. R. Soc. Interface.

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Designing and utilization of biomimetic membrane systems generated by bottom-up processes is a rapidly growing scientific and engineering field. Elucidation of the supramolecular construction principle of archaeal cell envelopes composed of S-layer stabilized lipid membranes led to new strategies for generating highly stable functional lipid membranes at mesoand macroscopic scale. In this review, we provide a state-of-the-art survey of how S-layer proteins, lipids and polymers may be used as basic building blocks for the assembly of S-layer-supported lipid membranes. These biomimetic membrane systems are distinguished by a nanopatterned fluidity, enhanced stability and longevity and, thus, provide a dedicated reconstitution matrix for membrane-active peptides and transmembrane proteins. Exciting areas in the (lab-on-a-) biochip technology are combining composite S-layer membrane systems involving specific membrane functions with the silicon world. Thus, it might become possible to create artificial noses or tongues, where many receptor proteins have to be exposed and read out simultaneously. Moreover, S-layer-coated liposomes and emulsomes copying virus envelopes constitute promising nanoformulations for the production of novel targeting, delivery, encapsulation and imaging systems.

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The Bacterial Surface Layer Provides Protection against Antimicrobial Peptides

Cited by 33 publications

References 26 publications

The Synechococcus cell surface protein SwmA increases vulnerability to predation by flagellates and ciliates

The Synechococcus cell surface protein SwmA increases vulnerability to predation by flagellates and ciliates

Lactobacillus surface layer proteins: structure, function and applications

Biomimetic interfaces based on S-layer proteins, lipid membranes and functional biomolecules

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