Surface receptors in lichen symbionts visualized by fluorescence microscopy after use of lectins

Marx, Magdalena; Peveling, Elisabeth

doi:10.1007/bf01279868

Cited by 20 publications

(15 citation statements)

References 30 publications

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“…These facts are consistent with previous results (Max and Peveling 1983;Fontaniella et al 2004). These studies showed that cyanobionts as well as chlorobionts can be recognized by non-lichen lectins, e.g., concanavalin A (ConA) from Canavalia ensiformis (L.) DC, a leguminous plant.…”

Section: Discussionsupporting

confidence: 90%

“…Some lectins from cyanolichens bind their surface ligands in a D-galactose, but also D-mannose-dependent manner (Max and Peveling 1983). To test whether binding of the lectins used in this study also depended of mannose, we assayed desorption of labeled homologous lectin from Nostoc cells for both galactose and mannose.…”

Section: Nostoc Cell Wall Contains Another Lectin Ligand Other Than Gmentioning

confidence: 99%

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Direct and cross-recognition of lichenized Trebouxia Puymaly (Chlorophyta, Trebouxiophyceae) and Nostoc Vaucher ex Bornet (Cyanobacteria, Cyanophyceae) by their homologous and heterologous fungal lectins

et al. 2016

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In this study, we have used affinity chromatography to purify the lectins from a chlorolichen, Evernia prunastri (L.) Ach., and a cyanolichen, Peltigera canina (Ach.) Schard. These species secrete lectins that display arginase activity in addition to their role as recognition proteins. We found that fluorescently labeled lectins display efficient binding to their ligands on the cell wall. Binding was stronger when the lectin reacted with the producing (homologous) photobiont (alga or cyanobacteria) than with the nonproducing (heterologous) species used throughout the study. To address the specificity of lectin binding, we performed desorption experiments of cell-bound lectins with different hexoses. We found that Evernia lectin is only desorbed by galactose, consistent with its specific binding to a single polygalactosylated ligand. Conversely, Peltigera lectin is desorbed not only by galactose, but also by mannose. This indicates that Peltigera lectin recognizes not only a-D-galactose-containing ligands, but also ligands containing a-D-mannose moieties.

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Section: Discussionsupporting

confidence: 90%

Section: Nostoc Cell Wall Contains Another Lectin Ligand Other Than Gmentioning

confidence: 99%

Direct and cross-recognition of lichenized Trebouxia Puymaly (Chlorophyta, Trebouxiophyceae) and Nostoc Vaucher ex Bornet (Cyanobacteria, Cyanophyceae) by their homologous and heterologous fungal lectins

et al. 2016

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“…1) that binds to polygalactosylated urease linked to activated agarose (Figs 2 and 3). Furthermore, Marx & Peveling (1983) found that cyanobionts isolated from different cyanolichen species were able to bind some legume lectins, such as ricin A, this being specific to α‐ and β‐ d ‐galactose. Thus, the occurrence of a polygalactosylated receptor to glycosylated arginases seems to apply to both chloro‐ and cyanobionts.…”

Section: Discussionmentioning

confidence: 99%

“…Thus, the occurrence of a polygalactosylated receptor to glycosylated arginases seems to apply to both chloro‐ and cyanobionts. In addition, other receptors may be present on both photobionts since concanavalin A, a lectin from Canavalia ensiformis that is specific for α‐ d ‐glucose and α‐ d ‐mannose, binds to several cyanobionts (Marx & Peveling 1983) and chlorobionts (Fontaniella et al. 2004).…”

Section: Discussionmentioning

confidence: 99%

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The cell recognition model in chlorolichens involving a fungal lectin binding to an algal ligand can be extended to cyanolichens

et al. 2009

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Leptogium corniculatum, a cyanolichen containing Nostoc as photobiont, produces and secretes arginase to culture medium containing arginine. This secreted arginase was pre-purified by affinity chromatography on beads of activated agarose to which a polygalactosylated urease, purified from Evernia prunastri, was attached. Arginase was eluted from the beads with 50 mm alpha-d-galactose. The eluted arginase binds preferentially to the cell surface of Nostoc isolated from this lichen thallus, although it is also able to bind, to some extent, to the cell surface of the chlorobiont isolated from E. prunastri. Previous studies in chlorolichens have shown that a fungal lectin that develops subsidiary arginase activity can be a factor in recognition of compatible algal cells through binding to a polygalactosylated urease, which acts as a lectin ligand in the algal cell wall. Our experiments demonstrate that this model can now be extended to cyanolichens.

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Selectivity in the Lichen Symbiosis

Bubrick

Frensdorff

Galun

1985

Lichen Physiology and Cell Biology

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Surface receptors in lichen symbionts visualized by fluorescence microscopy after use of lectins

Cited by 20 publications

References 30 publications

Direct and cross-recognition of lichenized Trebouxia Puymaly (Chlorophyta, Trebouxiophyceae) and Nostoc Vaucher ex Bornet (Cyanobacteria, Cyanophyceae) by their homologous and heterologous fungal lectins

Direct and cross-recognition of lichenized Trebouxia Puymaly (Chlorophyta, Trebouxiophyceae) and Nostoc Vaucher ex Bornet (Cyanobacteria, Cyanophyceae) by their homologous and heterologous fungal lectins

The cell recognition model in chlorolichens involving a fungal lectin binding to an algal ligand can be extended to cyanolichens

Selectivity in the Lichen Symbiosis

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