Parasitic dodder expresses an arsenal of secreted cellulases with multi-substrate specificity during host invasion

Copyright © 2024 The Authors. Published by Elsevier Masson SAS.. All rights reserved.

Détails bibliographiques
Publié dans:Plant physiology and biochemistry : PPB. - 1991. - 210(2024) vom: 01. Mai, Seite 108633
Auteur principal: Edema, Hilary (Auteur)
Autres auteurs: Bawin, Thomas, Olsen, Stian, Krause, Kirsten, Karppinen, Katja
Format: Article en ligne
Langue:English
Publié: 2024
Accès à la collection:Plant physiology and biochemistry : PPB
Sujets:Journal Article Cuscuta campestris Endoglucanase Glycoside hydrolase family 9 (GH9) Haustorium Host infection Parasitic plant Plant cell wall Cellulases EC 3.2.1.- Plant Proteins
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520 |a Cuscuta campestris is a common and problematic parasitic plant which relies on haustoria to connect to and siphon nutrients from host plants. Glycoside hydrolase family 9 (GH9) cellulases (EC 3.2.1.4) play critical roles in plant cell wall biosynthesis and disassembly, but their roles during Cuscuta host invasion remains underexplored. In this study, we identified 22 full-length GH9 cellulase genes in C. campestris genome, which encoded fifteen secreted and seven membrane-anchored cellulases that showed distinct phylogenetic relationships. Expression profiles suggested that some of the genes are involved in biosynthesis and remodeling of the parasite's cell wall during haustoriogenesis, while other genes encoding secreted B- and C-type cellulases are tentatively associated with degrading host cell walls during invasion. Transcriptomic data in a host-free system and in the presence of susceptible or partially resistant tomato hosts, showed for especially GH9B7, GH9B11 and GH9B12 a shift in expression profiles in the presence of hosts, being more highly expressed during host attachment, indicating that Cuscuta can tune cellulase expression in response to a host. Functional analyses of recombinant B- and C-type cellulases showed endoglucanase activities over wide pH and temperature conditions, and activities towards multiple cellulose and hemicellulose substrates. These findings improve our understanding of host cell wall disassembly by Cuscuta, and cellulase activity towards broad substrate range potentially explain its wide host range. This is the first study to provide a broad biochemical insight into Cuscuta GH9 cellulases, which based on our study may have potential applications in industrial bioprocessing 
650 4 |a Journal Article 
650 4 |a Cuscuta campestris 
650 4 |a Endoglucanase 
650 4 |a Glycoside hydrolase family 9 (GH9) 
650 4 |a Haustorium 
650 4 |a Host infection 
650 4 |a Parasitic plant 
650 4 |a Plant cell wall 
650 7 |a Cellulases  |2 NLM 
650 7 |a EC 3.2.1.-  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
700 1 |a Bawin, Thomas  |e verfasserin  |4 aut 
700 1 |a Olsen, Stian  |e verfasserin  |4 aut 
700 1 |a Krause, Kirsten  |e verfasserin  |4 aut 
700 1 |a Karppinen, Katja  |e verfasserin  |4 aut 
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773 1 8 |g volume:210  |g year:2024  |g day:01  |g month:05  |g pages:108633 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2024.108633  |3 Volltext 
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