Co-crystallization and preliminary X-ray diffraction studies of Lathyrus ochrus isolectin I with Di- and trisaccharides, and a biantennary octosaccharide

Bourne, Yves; Anguille, Christelle; Fontecilla-Camps, J C; Rougé, Pierre; Cambillau, Christian

doi:10.1016/s0022-2836(05)80180-9

Cited by 9 publications

(2 citation statements)

References 7 publications

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“…The gradients were collected, the protein bands identified by R-SDS-PAGE, and the sedimentation coefficients determined as described under Materials and Methods. and Yarwood et al, 1985;Bourne et al, 1990Bourne et al, a, 1990b. Considering this information, how can the presence of only two polypeptides (20 and 24 kDa) in the γ-lathyrin fraction be explained?…”

Section: Resultsmentioning

confidence: 99%

Storage Proteins from Lathyrus sativus Seeds

Rosa

Ferreira

Teixeira

2000

J. Agric. Food Chem.

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The proteins from Lathyrus sativus Linn. (chickling vetch or grass pea) seeds were investigated. Protein constitutes approximately 20% of the seed dry weight, >60% of which is composed by globulins and 30% by albumins. A single, 24 kDa polypeptide comprises more than half of the protein present in the albumin fraction. The globulins may be fractionated into three main components, which were named alpha-lathyrin (the major globulin), beta-lathyrin, and gamma-lathyrin. alpha-Lathyrin, with a sedimentation coefficient of approximately 18S, is composed of three main types of unglycosylated subunits (50-66 kDa), each of which produce, upon reduction, a heavy and a light polypeptide chain, by analogy with 11S. beta-Lathyrin, with a sedimentation coefficient of 13S, is composed by a relatively large number of subunits (8-66 kDa). Two major polypeptides are glycosylated and exhibit structural similarity with beta-conglutin from Lupinus albus. One of these possesses an internal disulfide bond. gamma-Lathyrin, with a sedimentation coefficient of approximately 5S, contains two interacting, unglycosylated polypeptides, with no disulfide bonds: the major 24 kDa albumin and the heavier (20 kDa) polypeptide chain of La. sativus lectin.

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Section: Resultsmentioning

confidence: 99%

Storage Proteins from Lathyrus sativus Seeds

Rosa

Ferreira

Teixeira

2000

J. Agric. Food Chem.

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“…Even though they constitute a disparate group of proteins poorly related by their phylogenetic relationship and structural features, they share a very common property to specifically recognize Man and their derivatives, including mannosides, oligomannosides, and high-mannose glycans [ 20 ]. This specific recognition also concerns other Man-containing glycans like the complex N -glycans which are built around a trimannosyl Manα1,3Manα1,6Man core, readily recognized by Man-specific legume lectins [ 21 , 22 ]. As shown for plant lectins, the differences observed in the specific recognition of Man-containing glycans, essentially depend on both the axial position of the hydroxyl group at C2 in Man which is more or less strictly recognized by the carbohydrate-binding sites (CBSs) of lectins, and the type of glycosidic bonds α1,2, α1,3 or α1,6, and their internal or external position in the glycan chain, recognized by lectins [ 23 ].…”

Section: Introductionmentioning

confidence: 99%

Man-Specific Lectins from Plants, Fungi, Algae and Cyanobacteria, as Potential Blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) Coronaviruses: Biomedical Perspectives

Barre

Damme

Simplicien

et al. 2021

Cells

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Betacoronaviruses, responsible for the “Severe Acute Respiratory Syndrome” (SARS) and the “Middle East Respiratory Syndrome” (MERS), use the spikes protruding from the virion envelope to attach and subsequently infect the host cells. The coronavirus spike (S) proteins contain receptor binding domains (RBD), allowing the specific recognition of either the dipeptidyl peptidase CD23 (MERS-CoV) or the angiotensin-converting enzyme ACE2 (SARS-Cov, SARS-CoV-2) host cell receptors. The heavily glycosylated S protein includes both complex and high-mannose type N-glycans that are well exposed at the surface of the spikes. A detailed analysis of the carbohydrate-binding specificity of mannose-binding lectins from plants, algae, fungi, and bacteria, revealed that, depending on their origin, they preferentially recognize either complex type N-glycans, or high-mannose type N-glycans. Since both complex and high-mannose glycans substantially decorate the S proteins, mannose-specific lectins are potentially useful glycan probes for targeting the SARS-CoV, MERS-CoV, and SARS-CoV-2 virions. Mannose-binding legume lectins, like pea lectin, and monocot mannose-binding lectins, like snowdrop lectin or the algal lectin griffithsin, which specifically recognize complex N-glycans and high-mannose glycans, respectively, are particularly adapted for targeting coronaviruses. The biomedical prospects of targeting coronaviruses with mannose-specific lectins are wide-ranging including detection, immobilization, prevention, and control of coronavirus infection.

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Data bank of three-dimensional structures of disaccharides: Part II,N-acetyllactosaminic type N-glycans. Comparison with the crystal structure of a biantennary octasaccharide

et al. 1991

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Conformational energy maps and descriptions of structures at the local minima are presented for the following fragments found in N-acetyllactosaminic type glycans of N-glycoproteins: GlcNAc beta(1-2)Man, GlcNAc beta(1-4)Man, GlcNAc beta(1-6)Man, Gal beta(1-4)GlcNAc, GlcNAc beta(1-3)Gal, Fuc alpha(1-6)GlcNAc, Fuc alpha(1-3)GlcNAc, Xyl beta(1-2)Man, Gal beta(1-3)GlcNAc and GlcNAc beta(1-6)Gal. These results are the second part of a data bank on glycoprotein moieties; five disaccharides found in oligomannose type N-glycans were analysed earlier (Imberty et al., 1990, Glycoconjugate J 7:27-54). In the present study, three to seven minima are found for each dimer. Conformations of disaccharide fragments found in the crystal structure of the complex of a biantennary octasaccharide with Lathyrus ochrus lectin are plotted on these energy maps. While the observed conformations are at predicted minima, they are not always at the minimum predicted to have the lowest energy. Further, not all observed conformations are stabilized by the exo-anomeric effect. We conclude that these oligosaccharides are highly flexible.

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Co-crystallization and preliminary X-ray diffraction studies of Lathyrus ochrus isolectin I with Di- and trisaccharides, and a biantennary octosaccharide

Cited by 9 publications

References 7 publications

Storage Proteins from Lathyrus sativus Seeds

Storage Proteins from Lathyrus sativus Seeds

Man-Specific Lectins from Plants, Fungi, Algae and Cyanobacteria, as Potential Blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) Coronaviruses: Biomedical Perspectives

Data bank of three-dimensional structures of disaccharides: Part II,N-acetyllactosaminic type N-glycans. Comparison with the crystal structure of a biantennary octasaccharide

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