Proposal of a New Hydrogen‐Bonding Form to Maintain Curdlan Triple Helix

Miyoshi, Keita; Uezu, Kazuya; Sakurai, Kazuo; Shinkai, Seiji

doi:10.1002/cbdv.200490073

Cited by 89 publications

(67 citation statements)

References 16 publications

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“…To investigate the ␤-1,3-glucanrecognition mechanism by ␤GRP N102, the surface plasmon resonance (SPR) data were first analyzed. In aqueous solution, ␤-1,3-glucan forms a stable triple-helical structure and is known to be converted into a random coil or a single helix by chemical or physical treatments (18)(19)(20). Previous studies have shown that NaOH treatment alters the structure of laminaran (soluble ␤-1,3-glucan) from a triple-helical structure into a partially opened triple-helical structure, and it was indicated that even after neutralization, the partially opened structure was maintained for up to 20 days (21,22).…”

Section: Resultsmentioning

confidence: 99%

“…This result is consistent with the notion of the non-aromatic platform binding of ␤GRP. In the triple-helical structure, each of the chains is stabilized via inter-chain hydrogen bonds between the OH (2) groups but the OH (4) and OH (6) groups are exposed on the surface of the structure (19). Thus, the triple-helical structure does not exhibit the sugar rings on the surface and the hydrophobic interaction mediated by the aromatic platform and the sugar ring is not necessary to recognize the triple-helical structure of ␤-1,3-glucan (Fig.…”

Section: Discussionmentioning

confidence: 99%

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Solution structure of the silkworm βGRP/GNBP3 N-terminal domain reveals the mechanism for β-1,3-glucan-specific recognition

Takahasi

Ochiai

Horiuchi

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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The ␤-1,3-glucan recognition protein (␤GRP)/Gram-negative bacteriabinding protein 3 (GNBP3) is a crucial pattern-recognition receptor that specifically binds ␤-1,3-glucan, a component of fungal cell walls. It evokes innate immunity against fungi through activation of the prophenoloxidase (proPO) cascade and Toll pathway in invertebrates. The ␤GRP consists of an N-terminal ␤-1,3-glucan-recognition domain and a C-terminal glucanase-like domain, with the former reported to be responsible for the proPO cascade activation. This report shows the solution structure of the N-terminal ␤-1,3-glucan recognition domain of silkworm ␤GRP. Although the N-terminal domain of ␤GRP has a ␤-sandwich fold, often seen in carbohydrate-binding modules, both NMR titration experiments and mutational analysis showed that ␤GRP has a binding mechanism which is distinct from those observed in previously reported carbohydarate-binding domains. Our results suggest that ␤GRP is a ␤-1,3-glucan-recognition protein that specifically recognizes a triple-helical structure of ␤-1,3-glucan.phenol oxidase ͉ innate immunity ͉ pattern recognition

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Solution structure of the silkworm βGRP/GNBP3 N-terminal domain reveals the mechanism for β-1,3-glucan-specific recognition

Takahasi

Ochiai

Horiuchi

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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“…The modeled b-1,3-galactan was flexible in water, undergoing repeated minor conformational changes. Although the modeled structure did not reveal a specific binding site for b-Yarivs, the inside of the helix is relatively hydrophobic, because, as is the case for the b-1,3-glucan helix, OH groups of galactosyl residues other than C-2 OH are facing outward in water (Miyoshi et al, 2004;Sletmoen and Stokke, 2008).…”

Section: Computational Modeling Of B-13-galactanmentioning

confidence: 92%

β-Galactosyl Yariv Reagent Binds to the β-1,3-Galactan of Arabinogalactan Proteins

et al. 2013

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Yariv phenylglycosides [1,3,5-tri(p-glycosyloxyphenylazo)-2,4,6-trihydroxybenzene] are a group of chemical compounds that selectively bind to arabinogalactan proteins (AGPs), a type of plant proteoglycan. Yariv phenylglycosides are widely used as cytochemical reagents to perturb the molecular functions of AGPs as well as for the detection, quantification, purification, and staining of AGPs. However, the target structure in AGPs to which Yariv phenylglycosides bind has not been determined. Here, we identify the structural element of AGPs required for the interaction with Yariv phenylglycosides by stepwise trimming of the arabinogalactan moieties using combinations of specific glycoside hydrolases. Whereas the precipitation with Yariv phenylglycosides (Yariv reactivity) of radish (Raphanus sativus) root AGP was not reduced after enzyme treatment to remove a-L-arabinofuranosyl and b-glucuronosyl residues and b-1,6-galactan side chains, it was completely lost after degradation of the b-1,3-galactan main chains. In addition, Yariv reactivity of gum arabic, a commercial product of acacia (Acacia senegal) AGPs, increased rather than decreased during the repeated degradation of b-1,6-galactan side chains by Smith degradation. Among various oligosaccharides corresponding to partial structures of AGPs, b-1,3-galactooligosaccharides longer than b-1,3-galactoheptaose exhibited significant precipitation with Yariv in a radial diffusion assay on agar. A pull-down assay using oligosaccharides cross linked to hydrazine beads detected an interaction of b-1,3-galactooligosaccharides longer than b-1,3-galactopentaose with Yariv phenylglycoside. To the contrary, no interaction with Yariv was detected for b-1,6-galactooligosaccharides of any length. Therefore, we conclude that Yariv phenylglycosides should be considered specific binding reagents for b-1,3-galactan chains longer than five residues, and seven residues are sufficient for cross linking, leading to precipitation of the Yariv phenylglycosides.Arabinogalactan proteins (AGPs) are a type of plant proteoglycans consisting of a Hyp-rich core protein and large arabinogalactan (AG) moieties (Fincher et al., 1983;Nothnagel, 1997). Although there are many molecular species of AGP differentiated by their core proteins, the AG moieties commonly comprise b-1,3-galactan main chains and b-1,6-galactan side chains, to which L-Ara and other auxiliary sugars, such as GlcA, 4-O-methyl-GlcA, L-Fuc, L-Rha, and Xyl, are attached (Fincher et al., 1983;Nothnagel, 1997;Seifert and Roberts, 2007). A commercial product of AGPs prepared from the acacia (Acacia senegal) tree is known as gum arabic and utilized as a food stabilizer. In the Japanese herbal remedy Juzen-Taiho-To, AGs from Astragalus membranaceus are the active ingredient (Majewska-Sawka and Nothnagel, 2000;Kiyohara et al., 2002). In intact plants, AGPs are implicated in various physiological events and serve as extracellular constituents and signaling molecules. For instance, an AGP from stylar transmitting tissue attracts pollen tub...

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“…The different structures are illustrated in Figure 1. It is demonstrated that this alternate structure provides a more stable structure of curdlan and hence is likely to have higher population [25]. 1,3--glucans have also been complexed with nucleotides to form crystalline structures.…”

Section: Crystallinity Of 13-β-glucansmentioning

confidence: 99%