Characterization and affinity applications of cellulose-binding domains

Tomme, Peter; Boraston, A.B.; McLean, Bradley W.; Kormos, J.; Creagh, A. Louise; Sturch, K.; Gilkes, Neil R.; Haynes, Charles A.; Warren, R. A. J.; Kilburn, Douglas G.

doi:10.1016/s0378-4347(98)00053-x

Cited by 194 publications

(149 citation statements)

References 52 publications

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“…Thus CBMs are excellent model systems for studying the mechanism of protein-carbohydrate recognition. Furthermore, this diversity in ligand specificity underpins the exploitation of these protein modules in numerous biotechnological applications [18].…”

Section: Introductionmentioning

confidence: 99%

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Boraston

Bolam

Gilbert

et al. 2004

Biochemical Journal

1,799

1,724

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The enzymic degradation of insoluble polysaccharides is one of the most important reactions on earth. Despite this, glycoside hydrolases attack such polysaccharides relatively inefficiently as their target glycosidic bonds are often inaccessible to the active site of the appropriate enzymes. In order to overcome these problems, many of the glycoside hydrolases that utilize insoluble substrates are modular, comprising catalytic modules appended to one or more non-catalytic CBMs (carbohydrate-binding modules). CBMs promote the association of the enzyme with the substrate. In view of the central role that CBMs play in the enzymic hydrolysis of plant structural and storage polysaccharides, the ligand specificity displayed by these protein modules and the mechanism by which they recognize their target carbohydrates have received considerable attention since their discovery almost 20 years ago. In the last few years, CBM research has harnessed structural, functional and bioinformatic approaches to elucidate the molecular determinants that drive CBM-carbohydrate recognition. The present review summarizes the impact structural biology has had on our understanding of the mechanisms by which CBMs bind to their target ligands.

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Section: Introductionmentioning

confidence: 99%

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Boraston

Bolam

Gilbert

et al. 2004

Biochemical Journal

1,799

1,724

View full text Add to dashboard Cite

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“…This CBP exhibited a relatively high affinity for cellulose and was found to be essential for the degradation of crystalline cellulose (Goldstein et al, 1993). It is thought that CBD determines the efficiency of degradation of insoluble cellulose by concentrating cellulase catalytic domains on the surface of the insoluble cellulose substrate (Tomme et al, 1998;Carrard et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Cellulose Binding Protein from the Parasitic Nematode Heterodera schachtii Interacts with Arabidopsis Pectin Methylesterase: Cooperative Cell Wall Modification during Parasitism

et al. 2008

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Plant-parasitic cyst nematodes secrete a complex of cell wall-digesting enzymes, which aid in root penetration and migration. The soybean cyst nematode Heterodera glycines also produces a cellulose binding protein (Hg CBP) secretory protein. To determine the function of CBP, an orthologous cDNA clone (Hs CBP) was isolated from the sugar beet cyst nematode Heterodera schachtii, which is able to infect Arabidopsis thaliana. CBP is expressed only in the early phases of feeding cell formation and not during the migratory phase. Transgenic Arabidopsis expressing Hs CBP developed longer roots and exhibited enhanced susceptibility to H. schachtii. A yeast two-hybrid screen identified Arabidopsis pectin methylesterase protein 3 (PME3) as strongly and specifically interacting with Hs CBP. Transgenic plants overexpressing PME3 also produced longer roots and exhibited increased susceptibility to H. schachtii, while a pme3 knockout mutant showed opposite phenotypes. Moreover, CBP overexpression increases PME3 activity in planta. Localization studies support the mode of action of PME3 as a cell wall-modifying enzyme. Expression of CBP in the pme3 knockout mutant revealed that PME3 is required but not the sole mechanism for CBP overexpression phenotype. These data indicate that CBP directly interacts with PME3 thereby activating and potentially targeting this enzyme to aid cyst nematode parasitism.

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“…Recombinant cells with surface-expressed CBD or hybrid enzymes/proteins containing CBD are easily and reliably bound to cellulose supports, thus providing a very simple and economical way of whole-cell or protein immobilization [14,[21][22][23]. On the other hand, use of CBD families, which reversibly bind to cellulose, in protein engineering provide specific tags for bioseparation on cellulose matrix by affinity chromatography [24].…”

Section: Introductionmentioning

confidence: 99%

Atomic force microscopy study of cellulose surface interaction controlled by cellulose binding domains

Nigmatullin

Lovitt

Wright

et al. 2004

Colloids and Surfaces B: Biointerfaces

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Colloidal probe microscopy has been used to study the interaction between model cellulose surfaces and the role of cellulose binding domain (CBD), peptides specifically binding to cellulose, in interfacial interaction of cellulose surfaces modified with CBDs.The interaction between pure cellulose surfaces in aqueous electrolyte solution is dominated by double layer repulsive forces with the range and magnitude of the net force dependent on electrolyte concentration. AFM imaging reveals agglomeration of CBD adsorbed on cellulose surface. Despite an increase in surface charge owing to CBD binding to cellulose surface, force profiles are less repulsive for interactions involving, at least, one modified surface. Such changes are attributed to irregularity of the topography of protein surface and non-uniform distribution of surface charges on the surface of modified cellulose.Binding double CBD hybrid protein to cellulose surfaces causes adhesive forces at retraction, whereas separation curves obtained with cellulose modified with single CBD show small adhesion only at high ionic strength. This is possibly caused by the formation of the cross-links between cellulose surfaces in the case of double CBD.

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Characterization and affinity applications of cellulose-binding domains

Cited by 194 publications

References 52 publications

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Cellulose Binding Protein from the Parasitic Nematode Heterodera schachtii Interacts with Arabidopsis Pectin Methylesterase: Cooperative Cell Wall Modification during Parasitism

Atomic force microscopy study of cellulose surface interaction controlled by cellulose binding domains

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