Cross-Linking Activities of Galectins and Other Multivalent Lectins.

Brewer, C. Fred; 洋一郎, 荒田

doi:10.4052/tigg.9.155

Cited by 33 publications

(15 citation statements)

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“…Based on the non-antibacterial nature of the BjCHI1 derivatives lacking chitin-binding domains, the bivalent structure of the carbohydrate-binding domains in BjCHI1 now appears especially significant in defence against bacteria. Molecular and structural studies have shown that cross-linking interactions between certain bivalent and multivalent lectins result in the formation of unique two- and three-dimensional supermolecular assemblies ( Brewer, 1997 ). Mobile infecting bacterial cells could be immobilized and inhibited by such supermolecular assemblies as a result of BjCHI1 binding bacterial cells.…”

Section: Discussionmentioning

confidence: 99%

Brassica juncea chitinase BjCHI1 inhibits growth of fungal phytopathogens and agglutinates Gram-negative bacteria

Guan

Ramalingam

Nagegowda

et al. 2008

Journal of Experimental Botany

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Brassica juncea BjCHI1 is a plant chitinase with two chitin-binding domains. Its expression, induced in response to wounding, methyl jasmonate treatment, Aspergillus niger infection, and caterpillar Pieris rapae feeding, suggests that it plays a role in defence. In this study, to investigate the potential of using BjCHI1 in agriculture, Pichia-expressed BjCHI1 and its deletion derivatives that lack one or both chitin-binding domains were tested against phytopathogenic fungi and bacteria. Transplastomic tobacco expressing BjCHI1 was also generated and its extracts assessed. In radial growth-inhibition assays, BjCHI1 and its derivative with one chitin-binding domain showed anti-fungal activities against phytopathogens, Colletotrichum truncatum, C. acutatum, Botrytis cinerea, and Ascochyta rabiei. BjCHI1 also inhibited spore germination of C. truncatum. Furthermore, BjCHI1, but not its derivatives lacking one or both domains, inhibited the growth of Gram-negative bacteria (Escherichia coli, Ralstonia solanacearum, Pseudomonas aeruginosa) more effectively than Gram-positive bacteria (Micrococcus luteus and Bacillus megaterium), indicating that the duplicated chitin-binding domain, uncommon in chitinases, is essential for bacterial agglutination. Galactose, glucose, and lactose relieved agglutination, suggesting that BjCHI1 interacts with the carbohydrate components of the Gram-negative bacterial cell wall. Retention of chitinase and bacterial agglutination activities in transplastomic tobacco extracts implicates that BjCHI1 is potentially useful against both fungal and bacterial phytopathogens in agriculture.

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Section: Discussionmentioning

confidence: 99%

Brassica juncea chitinase BjCHI1 inhibits growth of fungal phytopathogens and agglutinates Gram-negative bacteria

Guan

Ramalingam

Nagegowda

et al. 2008

Journal of Experimental Botany

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“…Galectin-1 Induces Cross-linking of LRP1 and Galectin-3 Induces Cross-linking of LRP1 and PDGFRB, Including ITGB1 on the Surface of Retinal Pigment Epithelial Cells-It is known that Gal-1 and Gal-3 can cross-link and cluster transmembrane glycoproteins and additionally reduce their mobility (11,14,15). Dynamic lattices on the cell surface are built, and several cellular processes can be influenced (14,15). To check whether Gal-1 and Gal-3 are able to cross-link with LRP1 and PDGFRB as well as with the known galectin interactor ITGB1, mesenchymal human RPE cells were treated with biotinylated Gal-1 or Gal-3 for 30 min before fixation.…”

Section: Galectin-3 Revealed More Interacting Binding Partners Thanmentioning

confidence: 99%

Proteome-wide Identification of Glycosylation-dependent Interactors of Galectin-1 and Galectin-3 on Mesenchymal Retinal Pigment Epithelial (RPE) Cells

Obermann

Priglinger

Merl-Pham

et al. 2017

Molecular & Cellular Proteomics

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Identification of interactors is a major goal in cell biology. Not only protein-protein but also protein-carbohydrate interactions are of high relevance for signal transduction in biological systems. Here, we aim to identify novel interacting binding partners for the β-galactoside-binding proteins galectin-1 (Gal-1) and galectin-3 (Gal-3) relevant in the context of the eye disease proliferative vitreoretinopathy (PVR). PVR is one of the most common failures after retinal detachment surgeries and is characterized by the migration, adhesion, and epithelial-to-mesenchymal transition of retinal pigment epithelial cells (RPE) and the subsequent formation of sub- and epiretinal fibrocellular membranes. Gal-1 and Gal-3 bind in a dose- and carbohydrate-dependent manner to mesenchymal RPE cells and inhibit cellular processes like attachment and spreading. Yet knowledge about glycan-dependent interactors of Gal-1 and Gal-3 on RPE cells is very limited, although this is a prerequisite for unraveling the influence of galectins on distinct cellular processes in RPE cells. We identify here 131 Gal-3 and 15 Gal-1 interactors by galectin pulldown experiments combined with quantitative proteomics. They mainly play a role in multiple binding processes and are mostly membrane proteins. We focused on two novel identified interactors of Gal-1 and Gal-3 in the context of PVR: the low-density lipoprotein receptor LRP1 and the platelet-derived growth factor receptor β PDGFRB. Addition of exogenous Gal-1 and Gal-3 induced cross-linking with LRP1/PDGFRB and integrin-β1 (ITGB1) on the cell surface of human RPE cells and induced ERK/MAPK and Akt signaling. Treatment with kifunensine, an inhibitor of complex-type -glycosylation, weakened the binding of Gal-1 and Gal-3 to these interactors and prevented lattice formation. In conclusion, the identified specific glycoprotein ligands shed light into the highly specific binding of galectins to dedifferentiated RPE cells and the resulting prevention of PVR-associated cellular events.

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“…2 the carbohydrate-binding domains in BjCHI1 appears essential in defense against bacteria. The formation of two-and three-dimensional supermolecular assemblies 13 from the interaction of the lipopolysaccharide components, present on the outer membranes of bacterial cell walls, in conjunction with BjCHI1, would immobilize bacteria. Further, the second chitin-binding domain may confer a synergistic effect on BjCHI1 with other chitinases, as well as in enhancing its own ability to access reactive sites on fungal hyphae.…”

Section: An Unusual Chimera Consisting Of Two Chitin-binding Domains mentioning

confidence: 99%

ABrassica junceachitinase with two-chitin binding domains show anti-microbial properties against phytopathogens and gram-negative bacteria

Guan

Chye

2008

Plant Signaling & Behavior

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Cross-Linking Activities of Galectins and Other Multivalent Lectins.

Cited by 33 publications

References 0 publications

Brassica juncea chitinase BjCHI1 inhibits growth of fungal phytopathogens and agglutinates Gram-negative bacteria

Brassica juncea chitinase BjCHI1 inhibits growth of fungal phytopathogens and agglutinates Gram-negative bacteria

Proteome-wide Identification of Glycosylation-dependent Interactors of Galectin-1 and Galectin-3 on Mesenchymal Retinal Pigment Epithelial (RPE) Cells

ABrassica junceachitinase with two-chitin binding domains show anti-microbial properties against phytopathogens and gram-negative bacteria

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