PHYTOLECTINS FROM THE NITROGEN‐FIXING LICHEN <i>PELTIGERA HORIZONTALIS: THE</i> BINDING PATTERN OF PRIMARY PROTEIN EXTRACT

Petit, Patrice X.

doi:10.1111/j.1469-8137.1982.tb03349.x

Cited by 24 publications

(28 citation statements)

References 24 publications

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“…The phytolectin of P. canina var canina is thermostable. As previously described by Howe and Barrett (1970) in Parmelia michauxiana and by Petit (1982) in Peltigera horizontalis, who showed an agglutinating activity at the primary protein extract level, the phytolectin of P. canina var canina is thermostable in the same condition (10 min at 105 °C). We also note that the agglutinating activity of this phytolectin may be considerably stimulated by numerous divalent cations (Mg2+, Mn2+, Ca2+, Co^^, Cu2+) which abound in lichen thalli, well known for their capacity to retain such compounds.…”

Section: Resultssupporting

confidence: 68%

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PURIFIED PHYTOLECTIN FROM THE LICHEN PELTIGERACANINA VAR CANINA WHICH BINDS TO THE PHYCOBIONT CELL WALLS AND ITS USE AS CYTOCHEMICAL MARKER IN SITU

1983

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SUMMARYA purified phytolectin was isolated from the nitrogen-fixing lichen Peltigera canina var canina. This lectin was thermostable, truly non-specific and may have a molecular weight in its native form of the order of 80000 to 90000. It binds to the appropriate phycobiont cell walls and may be involved in some way in the recognition of, or interactions between, compatible lichen symbionts; it may be used in situ as a cytochemical marker of the free receptor sites in the lichen thalli. We advance a hypothesis that within the lichen the morphological and physiological state of the phycobiont is different in the various parts of the thallus; the capacity of the phycobiont to bind to lectins varies with fiuctuations in the symbiotic relationship between partners.

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Section: Resultssupporting

confidence: 68%

“…In some cases, phytolectins have been shown to bind to the appropriate phycobiont (Lockhart et a/., 1978;Bubrick, Galun and FrensdorflF, 1981;Petit, 1982).…”

Section: Introductionmentioning

confidence: 99%

PURIFIED PHYTOLECTIN FROM THE LICHEN PELTIGERACANINA VAR CANINA WHICH BINDS TO THE PHYCOBIONT CELL WALLS AND ITS USE AS CYTOCHEMICAL MARKER IN SITU

1983

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“…These prokaryotes are hosted either by fungi in the lichen symbiosis or in vascular plants in associations of the Anabaena-Azolla (Peters et al, 1982) or Nostoc-Gunnera (Schaede, 1951) type. Studies on various lichens (Lockhart et al, 1978;Petit, 1978;Petit et al, 1983) led to the isolation of a lectin that apparently belonged to the fungal partner and that might be able to recognize structures on the cyanobacterium wall; the physiological relationship of the two partners may be modulated by variations in the sugars present on the wall of the phycobiont. Similarly, studies (Mellor et al, 1981;Ladha and Watanabe, 1984;McCowen et al, 1987) of the AnabaenaAzolla symbiosis have shown that a lectin belonging to the fern, and which differs according to the species, specifically recognizes the strain of cyanobacterium for which it adapted.…”

mentioning

confidence: 99%

Characterization of a Lectin from Lactarius deterrimus (Research on the Possible Involvement of the Fungal Lectin in Recognition between Mushroom and Spruce during the Early Stages of Mycorrhizae Formation)

Giollant¹,

Guillot²,

Damez³

et al. 1993

Plant Physiol.

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A lectin (LDetL) was isolated from carpophores of the mushroom Lactarius deterrimus, a specific symbiont of the spruce, by a combination of affinity, hydroxylapatite, and gel-filtration chromatography. Its molecular mass, as determined by gel filtration, is about 37,000 D, and its structure is dimeric, with two identical subunits assembled by noncovalent bonds. It appeared homogeneous on high-performance liquid chromatography gel filtration, but isoelectric focusing revealed microheterogeneity, with a main band in the pH zone near 6.5. Amino acid analysis showed that LDetL contains a large proportion of glycine and especially methionine. Hapten inhibition assay indicated that LDetL is most specific for ~-~-g a l a c t o s y l ( l~3 ) -~-N -a c e t y lgalactosamine residues. The lectin was formed in the in vitro-cultivated mycelium, and anti-lectin antibodies revealed by indirect immunofluorescence the presence of lectin in the cell wall. Receptor sites for LDetL were found on the roots, especially on the root hairs, of axenically grown spruce seedlings. The lectin LDL previously isolated by us from the taxonomically related mushroom Lactarius deliciosus, a symbiont of the pine, does not bind to the spruce radicle. This suggests a role of the funga1 lectin in recognition and specificity during the early stages of mycorrhizae formation.

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“…The participation of this class of proteins as a recognition factor for the association of compatible fungi and algae in lichen symbiosis has been suggested (Lockhart et al, 1978 ;Petit, 1982 ;Petit et al, 1983) as an extension of the concept of interaction between pathogenic fungi and their hosts (Rose! n et al, 1996) and many other biological systems where lectins act as recognition molecules (Sharon & Lis, 1989).…”

Section: mentioning

confidence: 99%

A lectin from the lichenized Basidiomycete Dictyonema glabratum

et al. 2000

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A lectin with hemagglutinating activity has been isolated from an aqueous extract of the symbiotic phenotype of Dictyonema glabratum and its cyanobacterial photobiont Scytonema sp. The purified lectin had a pI of 6n8 and its molecular mass was investigated by electrospray ionization mass spectrometry, gel filtration and SDS-PAGE, which indicated its native conformation as a dimer formed by two identical subunits of 16 540 Da. The lectin is a glycoprotein with a low degree of glycosylation, containing galactose, xylose, glucose and mannose as neutral monosaccharides, in addition to glucosamine, which could indicate both N-and O-linkages. Amino acid analysis showed the predominance of nonpolar residues such as phenylalanine. Agglutination of human erythrocytes required divalent cations, which is affected by addition of EDTA. The lectin was more stable at 30mC or less for at least 1 h and between pH 5n0 and 7n0. Among the various compounds tested for hemagglutination inhibition, N-acetylgalactosamine was the most active. The potential role of this lectin in recognition of the compatible cyanobacterial photobiont is discussed.

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PHYTOLECTINS FROM THE NITROGEN‐FIXING LICHEN PELTIGERA HORIZONTALIS: THE BINDING PATTERN OF PRIMARY PROTEIN EXTRACT

Cited by 24 publications

References 24 publications

PURIFIED PHYTOLECTIN FROM THE LICHEN PELTIGERACANINA VAR CANINA WHICH BINDS TO THE PHYCOBIONT CELL WALLS AND ITS USE AS CYTOCHEMICAL MARKER IN SITU

PURIFIED PHYTOLECTIN FROM THE LICHEN PELTIGERACANINA VAR CANINA WHICH BINDS TO THE PHYCOBIONT CELL WALLS AND ITS USE AS CYTOCHEMICAL MARKER IN SITU

Characterization of a Lectin from Lactarius deterrimus (Research on the Possible Involvement of the Fungal Lectin in Recognition between Mushroom and Spruce during the Early Stages of Mycorrhizae Formation)

A lectin from the lichenized Basidiomycete Dictyonema glabratum

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