V. Functions of S-layers

Beveridge, Terrance; Pouwels, Peter H.; Sára, Margit; Kotiranta, Anja; Lounatmaa, Kari; Kari, Kirsti; Kerosuo, Eero; Haapasalo, Markus; Egelseer, Eva M.; Schocher, I; Sleytr, Uwe B.; Morelli, L.; Callegari, Maria Luisa; Nomellini, John F.; Bingle, Wade H.; Smit, John; Leibovitz, Emmanuelle; Lemaire, Marc; Miras, Isabelle; Salamitou, Sylvie; Béguin, Pierre; Ohayon, Hélène; Gounon, Pierre; Matuschek, Markus; Sahm, Kerstin; Bahl, Hubert; Grogono-Thomas, Rosemary; Dworkin, Joel; Blaser, Martin J.; Woodland, Ralph M.; Newell, Diane G.; Kessel, Martin; Koval, Susan F.

doi:10.1111/j.1574-6976.1997.tb00305.x

Cited by 116 publications

(50 citation statements)

References 192 publications

(285 reference statements)

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“…Our results agree with those of Koval (unpubl. data cited in Beveridge et al 1997) who found that S-layer-bearing bacteria from various taxa were ingested at equivalent or higher rates than their S-layer-negative variants (i.e., mutants) by the ciliate Tetrahymena thermophila and the flagellate Paraphysomonas vestita. In contrast, Koval and Hynes (1991) found the S layer of several gram-negative bacteria to be protective against Bdellovibrio.…”

Section: Discussionmentioning

confidence: 97%

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: Discussionmentioning

confidence: 97%

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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“…S-layer proteins are sometimes glycosylated with molecular weights ranging from 40-200 kDa. The surface boundary layer, possibly the most ancient biological membrane,9,11,12 is thought to play a critical role in the organism's interaction with the external environment, in nutrient uptake, cell excretion, signaling and surface interactions 13,14. As in most archaea that lack pseudomurein, the M. acetivorans and M. mazei S-layer is a protective coat surrounding the lipid membrane and contributes to cell size and shape 15-18.…”

Section: Introductionmentioning

confidence: 99%

S-layer, Surface-Accessible, and Concanavalin A Binding Proteins of Methanosarcina acetivorans and Methanosarcina mazei

et al. 2009

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The outermost cell envelope structure of many archaea and bacteria contains a proteinaceous lattice termed the surface layer or S-layer. It is typically composed of only one or two abundant, often posttranslationally modified proteins that self-assemble to form the highly organized arrays. Surprisingly, over a hundred proteins were annotated to be S-layer components in the archaeal species Methanosarcina acetivorans C2A and Methanosarcina mazei Gö1, reflecting limitations of current predictions. An in vivo biotinylation methodology was devised to affinity tag surface-exposed proteins while overcoming unique challenges in working with these fragile organisms. Cells were adapted to growth under N 2 fixing conditions, thus minimizing free amines reactive to the NHSlabel, and high pH media compatible with the acylation chemistry was used. A 3-phase separation procedure was employed to isolate intact, labeled cells from lysed-cell derived proteins. Streptavidin affinity enrichment followed by stringent wash conditions removed non-specifically bound proteins. This methodology revealed S-layer proteins in M. acetivorans C2A and M. mazei Gö1 to be MA0829 and MM1976, respectively. Each was demonstrated to exist as multiple glycosylated forms using SDS-PAGE coupled with glycoprotein-specific staining, and by interaction with the lectin, Concanavalin A. A number of additional surface-exposed proteins and glycoproteins were identified and included all three subunits of the thermosome: the latter suggests that the chaperonin complex is both surface-and cytoplasmically-localized. This approach provides an alternative strategy to study surface proteins in the archaea.

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“…S-layers have evolved in the course of evolution as a consequence of the direct interaction of prokaryotic cells with different habitats and changing ecological conditions, presumably providing them with a selection advantage. It is recognized that S-layers can act (i) as frameworks to determine cell shape and to aid in the cell division process in some archaea; (ii) as structures involved in cell adhesion and surface recognition; and (iii) as protective coats, molecular sieves, molecule and ion traps or adhesion zones for exoenzymes (for reviews see [18,79]). The S-layer glycan chains, which protrude from the cell surface up to 30-40 nm, create a polysaccharide coat similar to that of lipopolysaccharide O-antigens from Gram-negative bacteria.…”

Section: Surface Layer (S-layer) Glycoproteinsmentioning

confidence: 99%

Prokaryotic glycosylation

2001

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With the advances of molecular biology and with improved analytical techniques a significant change of perception has taken place regarding prokaryotic glycoproteins. Glycosylation of proteins from prokaryotes is no longer considered a specific feature of certain organisms but has been demonstrated for many archaea and bacteria. Besides the occurrence of glycosylated enzymes, antigens and other cell envelope components, surface layer (S-layer) glycoproteins represent the best-studied examples of glycosylated prokaryotic proteins. They are widely distributed among archaeal wild-type strains, but among bacteria they have been mainly observed with Gram-positive organisms. There is, in general, an enormous increase of reports on the presence of glycosylated proteins among prokaryotes. For their isolation and characterization a great number of methods are available, aiming at the identification of the covalent linkage between the carbohydrate and the polypeptide portion. So far, several differences in structure and biosynthesis have been observed in comparison to eukaryotic glycoproteins. In this review we introduce a protocol which has been successfully applied to the investigation of the complex structures, linkage units, and polypeptide consensus sequences of glycosylated bacterial S-layer proteins.

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V. Functions of S-layers

Cited by 116 publications

References 192 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

S-layer, Surface-Accessible, and Concanavalin A Binding Proteins of Methanosarcina acetivorans and Methanosarcina mazei

Prokaryotic glycosylation

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