The identification of two peptide sequences of light subunits of the Lathyrus ochrus isolectins containing a sequential epitope

Lueken, Konstanze; Mazarguil, Honoré; Rougé, Pierre

doi:10.1016/0165-2478(88)90160-5

Cited by 5 publications

(2 citation statements)

References 20 publications

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“…ELISA measurements were performed as previously described [21]. Briefly, the wells of a microtitration plate (Flow Laboratories) were loaded with 150 µl of antigen (arcelin-1, PHA-E, PHA-L or PHA from lima bean) solution in 0.1 M Na # CO $ \ NaHCO $ buffer, pH 9.6, used at various concentrations ranging from 0.625 to 50 µg\ml.…”

Section: Elisa Measurementsmentioning

confidence: 99%

Characterization and sugar-binding properties of arcelin-1, an insecticidal lectin-like protein isolated from kidney bean (Phaseolus vulgaris L. cv. RAZ-2) seeds

Fabre

Causse

Mourey

et al. 1998

Biochemical Journal

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Arcelin-1 is a lectin-like protein found in the seeds of wild varieties of the kidney bean (Phaseolus vulgaris). This protein displays insecticidal properties, but the mechanism of action is as yet unknown. In the present study we investigated the biochemical and biophysical properties of arcelin-1 from Phaseolus vulgaris cv. RAZ-2. Native arcelin-1 is a dimeric glycoprotein of 60 kDa, built from the non-covalent association of two identical monomers. This dimer resists dissociation by chaotropic agents and is highly resistant to proteolytic enzymes. Each subunit contains 10% (w/w) neutral sugars which belong to the high-mannose and complex-type glycans attached to three glycosylation sites. No interaction of the protein with simple sugars could be detected, but arcelin-1 displays an intrinsic specificity in binding complex glycans. Arcelin-1 therefore differs from the closely related phytohaemagglutinin lectins and alpha-amylase inhibitor in several respects: oligomerization states, sugar-binding affinities and the type and number of glycan chains. These features may be related to the toxicity of arcelin-1.

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Section: Elisa Measurementsmentioning

confidence: 99%

Characterization and sugar-binding properties of arcelin-1, an insecticidal lectin-like protein isolated from kidney bean (Phaseolus vulgaris L. cv. RAZ-2) seeds

Fabre

Causse

Mourey

et al. 1998

Biochemical Journal

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“…Depending on their structural organization, plant lectins usually exhibit a high degree of resistance to the degradation by trypsin-like proteases together with a pronounced capacity to trigger the synthesis of specific anti-lectin IgG. In this respect, IgG-binding epitopes have been identified on the molecular surface of Man-specific twochain lectins from the Vicieae tribe [122,123], and monoclonal antibodies that specifically recognize lentil and Lathyrus ochrus lectins, were easily prepared [124,125]. Even Manspecific dietary lectins, such as BanLec from banana and ASA from garlic, have been reported to induce an immune response since specific anti-lectin IgG have been identified in the serum of banana and garlic consumers [126,127].…”

Section: Biomedical Perspectives For Antiviral Lectinsmentioning

confidence: 99%

Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses

Barre

Damme

Klonjkowski

et al. 2022

Cells

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Pathogenic enveloped viruses are covered with a glycan shield that provides a dual function: the glycan structures contribute to virus protection as well as host cell recognition. The three classical types of N-glycans, in particular complex glycans, high-mannose glycans, and hybrid glycans, together with some O-glycans, participate in the glycan shield of the Ebola virus, influenza virus, human cytomegalovirus, herpes virus, human immunodeficiency virus, Lassa virus, and MERS-CoV, SARS-CoV, and SARS-CoV-2, which are responsible for respiratory syndromes. The glycans are linked to glycoproteins that occur as metastable prefusion glycoproteins on the surface of infectious virions such as gp120 of HIV, hemagglutinin of influenza, or spike proteins of beta-coronaviruses. Plant lectins with different carbohydrate-binding specificities and, especially, mannose-specific lectins from the Vicieae tribe, such as pea lectin and lentil lectin, can be used as glycan probes for targeting the glycan shield because of their specific interaction with the α1,6-fucosylated core Man3GlcNAc2, which predominantly occurs in complex and hybrid glycans. Other plant lectins with Neu5Ac specificity or GalNAc/T/Tn specificity can also serve as potential glycan probes for the often sialylated complex glycans and truncated O-glycans, respectively, which are abundantly distributed in the glycan shield of enveloped viruses. The biomedical and therapeutical potential of plant lectins as antiviral drugs is discussed.

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Localisation of amino acid sequence stretches containing a continuous epitope on the surface of the two Lathyrus ochrus isolectins

et al. 1990

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The identification of two peptide sequences of light subunits of the Lathyrus ochrus isolectins containing a sequential epitope

Cited by 5 publications

References 20 publications

Characterization and sugar-binding properties of arcelin-1, an insecticidal lectin-like protein isolated from kidney bean (Phaseolus vulgaris L. cv. RAZ-2) seeds

Characterization and sugar-binding properties of arcelin-1, an insecticidal lectin-like protein isolated from kidney bean (Phaseolus vulgaris L. cv. RAZ-2) seeds

Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses

Localisation of amino acid sequence stretches containing a continuous epitope on the surface of the two Lathyrus ochrus isolectins

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