Characterization of a Glycoside Hydrolase Family 157 Endo-β-1,3-Glucanase That Displays Antifungal Activity against Phytopathogens

Qin, Zhen; Yu, Sainan; Zhang, Kemin; Wei, Xingmei; Li, Junjie; Zhang, Zheyi; Wan, Sibao; Gao, Haiyan

doi:10.1021/acs.jafc.3c02083

Cited by 5 publications

(2 citation statements)

References 38 publications

(97 reference statements)

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“…For example, some b-1,3-glucanase are pathogenesis-related proteins (PRs), thus could be used as antifungal agents to destroy the cell wall of pathogenic organisms or as resistance gene in plant disease resistance in agriculture field [6,7]. In food and feed industries, b-1,3-glucanases can be used to produce b-1,3-glucan oligomers, which have been reported to possess series biological functions, such as increasing immune resistance in humans and animals, regulating intestinal flora balance, and inducing the antipathogen responses in plants [8].…”

Section: Introductionmentioning

confidence: 99%

Structural and functional analysis of SpGlu64A: a novel glycoside hydrolase family 64 laminaripentaose‐producing β‐1,3‐glucanase from Streptomyces pratensis

Ma,

Jiang,

Yan

et al. 2024

The FEBS Journal

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Laminaripentaose (L5)‐producing β‐1,3‐glucanases can preferentially cleave the triple‐helix curdlan into β‐1,3‐glucooligosaccharides, especially L5. In this study, a newly identified member of the glycoside hydrolase family 64, β‐1,3‐glucanase from Streptomyces pratensis (SpGlu64A), was functionally and structurally characterized. SpGlu64A shared highest identity (30%) with a β‐1,3‐glucanase from Streptomyces matensis. The purified SpGlu64A showed maximal activity at pH 7.5 and 50 °C, and exhibited strict substrate specificity toward curdlan (83.1 U·mg−1). It efficiently hydrolyzed curdlan to produce L5 as the end product. The overall structure of SpGlu64A consisted of a barrel domain and a mixed (α/β) domain, which formed an unusually wide groove with a crescent‐like structure. In the two complex structures (SpGlu64A–L3 and SpGlu64A–L4), two oligosaccharide chains were captured and the triple‐helical structure was relatively compatible with the wide groove, which suggested the possibility of binding to the triple‐helical β‐1,3‐glucan. A catalytic framework (β6–β9–β10) and the steric hindrance formed by the side chains of residues Y161, N163, and H393 in the catalytic groove were predicted to complete the exotype‐like cleavage manner. On the basis of the structure, a fusion protein with the CBM56 domain (SpGlu64A–CBM) and a mutant (Y161F; by site‐directed mutation) were obtained, with 1.2‐ and 1.7‐fold increases in specific activity, respectively. Moreover, the combined expression of SpGlu64A–CBM and ‐Y161F improved the enzyme activity by 2.63‐fold. The study will not only be helpful in understanding the reaction mechanism of β‐1,3‐glucanases but will also provide a basis for further enzyme engineering.

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Section: Introductionmentioning

confidence: 99%

Structural and functional analysis of SpGlu64A: a novel glycoside hydrolase family 64 laminaripentaose‐producing β‐1,3‐glucanase from Streptomyces pratensis

Ma,

Jiang,

Yan

et al. 2024

The FEBS Journal

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“…Based on the Carbohydrate-Active enZymes (CAZymes) Database (http://www.cazy.org), β-1,3glucanases belong to the glycoside hydrolase (GH) family 17. They are classi ed into two types, i.e., endo-β-1,3-glucanases (EC 3.2.1.39) that cleave the β-1,3-linkages inside the β-glucan chain at random sites, while exo-β-1,3-glucanases (EC 3.2.1.58) cleave the β-1,3-linkages from the nonreducing end of the β-glucan chain (Rajninec et al, 2021;Qin et al, 2023). Both endoand exo-acting β-1,3-glucanases degrade β-1,3-glucan e ciently, which regulates callose accumulation in the resistant cultivar.…”

Section: Introductionmentioning

confidence: 99%

Functional characterization of cell wall-associated β-glucanases and peroxidase induced during wheat-Diuraphis noxia inteactions.

Zondo,

Mohase,

Tolmay

et al. 2024

Preprint

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Wheat plants infested by Russian wheat aphids (RWA) induce a cascade of defence responses, which include increased activity of β-1,3-glucanase and peroxidase (POD). There is a lack of information regarding β-1,3-glucanase and POD synergistic effects on the plant cell wall modification and characterisation during wheat-RWA infestation. This study aimed to characterise the physicochemical properties of the cell wall-bound POD and β-1,3-glucanase during RWA-wheat interaction. The susceptible Tugela, moderately resistant Tugela Dn1, and resistant Tugela Dn5 cultivars were planted in a glasshouse to a seedling stage before being infested with RWASA2 for 14 days. The findings showed a significant increase in β-1,3-glucanase and POD activities in the infested Tugela Dn5 and Tugela-Dn1 cultivars over the 14 days. However, in the Tugela enzymes were repressed. In addition, it was shown for the first time that β-1,3-1,4-glucanase activity specific toward mixed-linked glucan was significant in the resistant cultivar over 14 days. β-1,3-glucanase, β-1,3-1,4-glucanase and POD displayed optimum at pH 5. β-1,3-glucanase and POD displayed temperature optimum at 40 and 50°C, respectively. However, β-1,3-1,4-glucanase had temperature optimum at 25°C. β-1,3-glucanase and POD had a thermo-stability at 37°C followed by about 80% relative activity at 70°C, but β-1,3-1,4-glucanase displayed thermostability at 25°C and retained more than 75% at 70°C, confirming that β-1,3-1,4-glucanase and β-1,3-glucanase induced in the resistant cultivars cell wall were two different enzymes. Mechanism of actions and oligosaccharide displayed that β-1,3-glucanase was highly active against β-1,3-glucan and required a triose and higher oligosaccharide to be active. Our findings demonstrated cell-wall bound POD and β-1,3-glucanase activities significantly increased in wheat after RWASA2 infestation, revealing they acted synergistically to reinforce the cell wall to deter RWASA2 feeding in resistant cultivars.

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Functional characterisation of cell wall-associated β-glucanases and peroxidase induced during wheat-Diuraphis noxia interactions

Zondo,

Mohase,

Tolmay

et al. 2024

Biologia

View full text Add to dashboard Cite

Wheat plants infested by Russian wheat aphids (RWA) induce a cascade of defence responses, which include increased activity of β-1,3-glucanase and peroxidase (POD). There is a lack of information regarding β-1,3-glucanase and POD synergistic effects on the plant cell wall modification and characterisation during wheat-RWA infestation. This study aimed to characterise the physicochemical properties of the cell wall-bound POD and β-1,3-glucanase during RWA-wheat interaction. The susceptible Tugela, moderately resistant Tugela-Dn1, and resistant Tugela-Dn5 cultivars were planted in a glasshouse to a seedling stage before being infested with RWASA2 for 14 days. The findings showed a significant increase in β-1,3-glucanase and POD activities in the infested Tugela-Dn5 and Tugela-Dn1 cultivars over the 14 days. However, in the Tugela enzymes were repressed. In addition, it was shown for the first time that β-1,3 − 1,4-glucanase activity specific toward mixed-linked glucan was significant in the resistant cultivar over 14 days. β-1,3-glucanase, β-1,3 − 1,4-glucanase and POD displayed optimum at pH 5. β-1,3-glucanase and POD displayed temperature optimum at 40 and 50 °C, respectively. However, β-1,3 − 1,4-glucanase had temperature optimum at 25 °C. β-1,3-glucanase and POD had a thermo-stability at 37 °C followed by about 80% relative activity at 70 °C, but β-1,3 − 1,4-glucanase displayed thermostability at 25 °C and retained more than 75% at 70 °C, confirming that β-1,3 − 1,4-glucanase and β-1,3-glucanase induced in the resistant cultivars cell wall were two different enzymes. Mechanism of actions and oligosaccharide displayed that β-1,3-glucanase was highly active against β-1,3-glucan and required a triose and higher oligosaccharide to be active. Our findings demonstrated cell-wall bound POD and β-1,3-glucanase activities significantly increased in wheat after RWASA2 infestation, revealing they acted synergistically to reinforce the cell wall to deter RWASA2 feeding in resistant cultivars.

show abstract

Characterization of a Glycoside Hydrolase Family 157 Endo-β-1,3-Glucanase That Displays Antifungal Activity against Phytopathogens

Cited by 5 publications

References 38 publications

Structural and functional analysis of SpGlu64A: a novel glycoside hydrolase family 64 laminaripentaose‐producing β‐1,3‐glucanase from Streptomyces pratensis

Structural and functional analysis of SpGlu64A: a novel glycoside hydrolase family 64 laminaripentaose‐producing β‐1,3‐glucanase from Streptomyces pratensis

Functional characterization of cell wall-associated β-glucanases and peroxidase induced during wheat-Diuraphis noxia inteactions.

Functional characterisation of cell wall-associated β-glucanases and peroxidase induced during wheat-Diuraphis noxia interactions

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