Partial characterization of lectin binding sites of retinal photoreceptor outer segments and interphotoreceptor matrix

1984 ◽  
Vol 228 (2) ◽  
pp. 299-307 ◽  
Author(s):  
John G. Wood ◽  
Joseph C. Besharse ◽  
Lynda Napier-Marshall
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Partial Characterization ◽  
Photoreceptor Outer Segments ◽  
Outer Segments ◽  
Retinal Photoreceptor ◽  
Interphotoreceptor Matrix ◽  
Lectin Binding Sites

Characterization of Lectin-Binding Sites on Human Spermatozoa

1987 ◽  
Vol 137 (6) ◽  
Author(s):  
Markus Gotwald ◽  
Peter Oefner ◽  
Pia Dejaco
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Human Spermatozoa ◽  
Lectin Binding Sites

scholarly journals Comprehensive analysis of lectin-glycan interactions reveals determinants of lectin specificity

2021 ◽  
Author(s):  
Daniel E Mattox ◽  
Chris Bailey-Kellogg
Keyword(s):  
Protein Trafficking ◽  
Binding Sites ◽  
Lectin Binding ◽  
Novel Approach ◽  
Wide Range ◽  
Generalized Patterns ◽  
Lectin Specificity ◽  
Positively Charged ◽  
Lectin Binding Sites

Lectin-glycan interactions facilitate inter- and intracellular communication in many processes including protein trafficking, host-pathogen recognition, and tumorigenesis promotion. Specific recognition of glycans by lectins is also the basis for a wide range of applications in areas including glycobiology research, cancer screening, and antiviral therapeutics. To provide a better understanding of the determinants of lectin-glycan interaction specificity and support such applications, this study comprehensively investigates specificity-conferring features of all available lectin-glycan complex structures. Systematic characterization, comparison, and predictive modeling of a set of 221 complementary physicochemical and geometric features representing these interactions highlighted specificity-conferring features with potential mechanistic insight. Univariable comparative analyses with weighted Wilcoxon-Mann-Whitney tests revealed strong statistical associations between binding site features and specificity that are conserved across unrelated lectin binding sites. Multivariable modeling with random forests demonstrated the utility of these features for predicting the identity of bound glycans based on generalized patterns learned from non-homologous lectins. These analyses revealed global determinants of lectin specificity, such as sialic acid glycan recognition in deep, concave binding sites enriched for positively charged residues, in contrast to high mannose glycan recognition in fairly shallow but well-defined pockets enriched for non-polar residues. Focused analysis of hemagglutinin interactions with human-like and avian-like glycans uncovered features representing both known and novel mutations related to shifts in influenza tropism from avian to human tissues. The presented systematic characterization of lectin binding sites provides a novel approach to studying lectin specificity and is a step towards confidently predicting new lectin-glycan interactions.

scholarly journals Differential effects of protease digestion on photoreceptor lectin binding sites.

1985 ◽  
Vol 33 (7) ◽  
pp. 642-646 ◽  
Author(s):  
J G Wood ◽  
L Napier-Marshall
Keyword(s):  
Binding Sites ◽  
Outer Segment ◽  
Lectin Binding ◽  
Rod Outer Segments ◽  
Proteolytic Digestion ◽  
Experimental Conditions ◽  
Intense Staining ◽  
Outer Segments ◽  
Intracellular Compartments ◽  
Lectin Binding Sites

The use of lectin cytochemistry together with proteolytic digestion techniques to partially characterize lectin binding sites of several intracellular compartments in frog photoreceptors was studied. Uniform access of reagents to all intracellular compartments was obtained by performing the experiments directly on semithin sections of retinal tissue embedded in a hydrophilic plastic resin. Protease pretreatment of sections of Xenopus laevis eyecup leads to a loss of wheat germ agglutinin (WGA) binding sites from most of the rod outer segment. Under experimental conditions used here, cone outer segment WGA binding sites are resistant to proteolytic digestion. Another major difference between rod and cone under segments is that rod outer segments are heavily labeled with succinylated WGA, whereas cone outer segments are barely labeled except for a region of intense staining thought to be at the connecting cilium. WGA binding sites in the shed outer segment tip (phagosome) are also relatively resistant to proteolytic digestion, as is the tip region of a few rod outer segments. This difference in lectin binding properties between the bulk of the outer segment membrane and the shed outer segment membrane is the only distinction we have observed between the two compartments in terms of their glycoconjugates. These results may be useful in terms of designing experiments to isolate cone and rod outer segments separately. They indicate that a change in outer segment glycoconjugates may accompany the shedding and phagocytosis events, as previously suggested, but this change does not necessarily involve the addition of saccharides to outer segment glycoproteins.

scholarly journals Comprehensive analysis of lectin-glycan interactions reveals determinants of lectin specificity

2021 ◽  
Vol 17 (10) ◽  
pp. e1009470
Author(s):  
Daniel E. Mattox ◽  
Chris Bailey-Kellogg
Keyword(s):  
Protein Trafficking ◽  
Binding Sites ◽  
Lectin Binding ◽  
Structural Data ◽  
Novel Approach ◽  
Wide Range ◽  
Generalized Patterns ◽  
Lectin Specificity ◽  
Lectin Binding Sites

Lectin-glycan interactions facilitate inter- and intracellular communication in many processes including protein trafficking, host-pathogen recognition, and tumorigenesis promotion. Specific recognition of glycans by lectins is also the basis for a wide range of applications in areas including glycobiology research, cancer screening, and antiviral therapeutics. To provide a better understanding of the determinants of lectin-glycan interaction specificity and support such applications, this study comprehensively investigates specificity-conferring features of all available lectin-glycan complex structures. Systematic characterization, comparison, and predictive modeling of a set of 221 complementary physicochemical and geometric features representing these interactions highlighted specificity-conferring features with potential mechanistic insight. Univariable comparative analyses with weighted Wilcoxon-Mann-Whitney tests revealed strong statistical associations between binding site features and specificity that are conserved across unrelated lectin binding sites. Multivariable modeling with random forests demonstrated the utility of these features for predicting the identity of bound glycans based on generalized patterns learned from non-homologous lectins. These analyses revealed global determinants of lectin specificity, such as sialic acid glycan recognition in deep, concave binding sites enriched for positively charged residues, in contrast to high mannose glycan recognition in fairly shallow but well-defined pockets enriched for non-polar residues. Focused fine specificity analysis of hemagglutinin interactions with human-like and avian-like glycans uncovered features representing both known and novel mutations related to shifts in influenza tropism from avian to human tissues. As the approach presented here relies on co-crystallized lectin-glycan pairs for studying specificity, it is limited in its inferences by the quantity, quality, and diversity of the structural data available. Regardless, the systematic characterization of lectin binding sites presented here provides a novel approach to studying lectin specificity and is a step towards confidently predicting new lectin-glycan interactions.

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