Role and significance of lytic polysaccharide monooxygenases (LPMOs) in lignocellulose deconstruction

Singhania, Reeta Rani; Dixit, Pooja; Patel, Anil Kumar; Giri, Balendu Shekher; Kuo, Chia‐Hung; Chen, Chiu-Wen; Dong, Cheng-Di

doi:10.1016/j.biortech.2021.125261

Cited by 56 publications

(26 citation statements)

References 92 publications

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“…They catalyze the oxidative cleavage of glycosidic bonds in polysaccharides such as chitin and cellulose, hemicellulose or starch and their discovery has revolutionized our understanding of enzymatic biomass conversion (Manavalan et al, 2021;Wang et al, 2021). Lytic polysaccharide monooxygenases require oxygen and partners to donate electrons during catalytic action on the cellulose backbone which must be present in the cell wall and released into the apoplastic space (Rani Singhania et al, 2021). Due to their enormous potential for application in agricultural waste decomposition, the current research focusses on biochemical application.…”

Section: Classification Of Secreted Fungal Proteinsmentioning

confidence: 99%

Comparative Secretome Analyses of Trichoderma/Arabidopsis Co-cultures Identify Proteins for Salt Stress, Plant Growth Promotion, and Root Colonization

Rouina

Tseng

Nataraja³

et al. 2022

Front. Ecol. Evol.

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Numerous Trichoderma strains are beneficial for plants, promote their growth, and confer stress tolerance. A recently described novel Trichoderma strain strongly promotes the growth of Arabidopsis thaliana seedlings on media with 50 mM NaCl, while 150 mM NaCl strongly stimulated root colonization and induced salt-stress tolerance in the host without growth promotion. To understand the dynamics of plant-fungus interaction, we examined the secretome from both sides and revealed a substantial change under different salt regimes, and during co-cultivation. Stress-related proteins, such as a fungal cysteine-rich Kp4 domain-containing protein which inhibits plant cell growth, fungal WSC- and CFEM-domain-containing proteins, the plant calreticulin, and cell-wall modifying enzymes, disappear when the two symbionts are co-cultured under high salt concentrations. In contrast, the number of lytic polysaccharide monooxygenases increases, which indicates that the fungus degrades more plant lignocellulose under salt stress and its lifestyle becomes more saprophytic. Several plant proteins involved in plant and fungal cell wall modifications and root colonization are only found in the co-cultures under salt stress, while the number of plant antioxidant proteins decreased. We identified symbiosis- and salt concentration-specific proteins for both partners. The Arabidopsis PYK10 and a fungal prenylcysteine lyase are only found in the co-culture which promoted plant growth. The comparative analysis of the secretomes supports antioxidant enzyme assays and suggests that both partners profit from the interaction under salt stress but have to invest more in balancing the symbiosis. We discuss the role of the identified stage- and symbiosis-specific fungal and plant proteins for salt stress, and conditions promoting root colonization and plant growth.

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Section: Classification Of Secreted Fungal Proteinsmentioning

confidence: 99%

Comparative Secretome Analyses of Trichoderma/Arabidopsis Co-cultures Identify Proteins for Salt Stress, Plant Growth Promotion, and Root Colonization

Rouina

Tseng

Nataraja³

et al. 2022

Front. Ecol. Evol.

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“…The LPMOs are oxidative enzymes, require an external electron donor (in this case lignin) and molecular oxygen or hydrogen peroxide for their catalytic activity, and elevate the hydrolytic potentiality of glycoside hydrolases (GHs) in the course of the depolymerization of recalcitrant polysaccharides, such as cellulosic biomass. [ 18 ]. Commercial cellulase preparations currently include LPMOs as their presence reasonably minimizes enzyme loading [ 19 ].…”

Section: Functional Properties Of Cellulasesmentioning

confidence: 99%

Tailoring in fungi for next generation cellulase production with special reference to CRISPR/CAS system

Mondal

Halder

Mondal

2021

Syst Microbiol and Biomanuf

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Cellulose is the utmost plenteous source of biopolymer in our earth, and fungi are the most efficient and ubiquitous organism in degrading the cellulosic biomass by synthesizing cellulases. Tailoring through genetic manipulation has played a substantial role in constructing novel fungal strains towards improved cellulase production of desired traits. However, the traditional methods of genetic manipulation of fungi are time-consuming and tedious. With the availability of the full-genome sequences of several industrially relevant filamentous fungi, CRISPR-CAS (clustered regularly interspaced short palindromic repeats/CRISPR-associated protein) technology has come into the focus for the proficient development of manipulated strains of filamentous fungi. This review summarizes the mode of action of cellulases, transcription level regulation for cellulase expression, various traditional strategies of genetic manipulation with CRISPR-CAS technology to develop modified fungal strains for a preferred level of cellulase production, and the futuristic trend in this arena of research.

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“…While the catalytic activity of LPMOs is driving technological advances in biomass degradation (Harris et al ., 2010; Arfi et al ., 2014; Horn et al ., 2012; Rani Singhania et al ., 2021), their role in virulence has been less thoroughly investigated. LPMOs play a role in virulence (Wong et al ., 2012; Loose et al ., 2014; Chiu et al ., 2015; Sabbadin et al ., 2021; Agostoni et al ., 2017) and are upregulated in pathogenic bacteria when exposed to human tissues (Vebø et al ., 2009, 2010).…”

Section: Introductionmentioning

confidence: 99%

CbpD crystal structure adds intrigue to substrate-specificity motifs in chitin-active lytic polysaccharide monooxygenases

Dade

Douzi

Cambillau

et al. 2022

Preprint

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Pseudomonas aeruginosa secretes diverse proteins via its Type 2 Secretion System, including a 39 KDa Chitin-Binding Protein, CbpD. CbpD was recently shown to be a lytic polysaccharide monooxygenase active on chitin, and to contribute substantially to virulence. To-date no structure of this virulence factor has been reported. Its first two domains are homologous to those found in the crystal structure of Vibrio cholerae GbpA, while the third domain is homologous to the NMR structure of the Cellvibrio japonicus CjLPMO10A CBM73 domain. We report the 3.0 Å resolution crystal structure of CbpD solved by molecular replacement, which required ab initio models of each CbpD domain generated by the artificial intelligence deep learning structure prediction algorithm RoseTTAFold. The structure of CbpD confirms previously postulated chitin-specific motifs in the AA10 domain while challenging the deterministic effects of other postulated substrate specificity motifs. Additionally, the structure of CbpD shows that post translational modifications occur on the chitin binding surface. Moreover, the structure raises interesting possibilities about how type 2 secretion system substrates may interact with the secretion machinery and demonstrates the utility of new artificial intelligence protein structure prediction algorithms in making challenging structural targets tractable.

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Role and significance of lytic polysaccharide monooxygenases (LPMOs) in lignocellulose deconstruction

Cited by 56 publications

References 92 publications

Comparative Secretome Analyses of Trichoderma/Arabidopsis Co-cultures Identify Proteins for Salt Stress, Plant Growth Promotion, and Root Colonization

Comparative Secretome Analyses of Trichoderma/Arabidopsis Co-cultures Identify Proteins for Salt Stress, Plant Growth Promotion, and Root Colonization

Tailoring in fungi for next generation cellulase production with special reference to CRISPR/CAS system

CbpD crystal structure adds intrigue to substrate-specificity motifs in chitin-active lytic polysaccharide monooxygenases

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