Expression and specificity of a chitin deacetylase from the nematophagous fungus Pochonia chlamydosporia potentially involved in pathogenicity

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Title: Expression and specificity of a chitin deacetylase from the nematophagous fungus Pochonia chlamydosporia potentially involved in pathogenicity
Authors: Aranda-Martínez, Almudena | Grifoll-Romero, Laia | Aragunde, Hugo | Sancho-Vaello, Enea | Biarnés, Xevi | Lopez-Llorca, Luis Vicente | Planas, Antoni
Research Group/s: Fitopatología
Center, Department or Service: Universidad de Alicante. Departamento de Ciencias del Mar y Biología Aplicada | Universidad de Alicante. Instituto Multidisciplinar para el Estudio del Medio "Ramón Margalef"
Keywords: Chitin deacetylases | Chitosans | Nematophagous fungus | Pochonia chlamydosporia | Pathogenicity
Knowledge Area: Botánica
Issue Date: 1-Feb-2018
Publisher: Springer Nature
Citation: Scientific Reports. 2018, 8: 2170. doi:10.1038/s41598-018-19902-0
Abstract: Chitin deacetylases (CDAs) act on chitin polymers and low molecular weight oligomers producing chitosans and chitosan oligosaccharides. Structurally-defined, partially deacetylated chitooligosaccharides produced by enzymatic methods are of current interest as bioactive molecules for a variety of applications. Among Pochonia chlamydosporia (Pc) annotated CDAs, gene pc_2566 was predicted to encode for an extracellular CE4 deacetylase with two CBM18 chitin binding modules. Chitosan formation during nematode egg infection by this nematophagous fungus suggests a role for their CDAs in pathogenicity. The P. chlamydosporia CDA catalytic domain (PcCDA) was expressed in E. coli BL21, recovered from inclusion bodies, and purified by affinity chromatography. It displays deacetylase activity on chitooligosaccharides with a degree of polymerization (DP) larger than 3, generating mono- and di-deacetylated products with a pattern different from those of closely related fungal CDAs. This is the first report of a CDA from a nematophagous fungus. On a DP5 substrate, PcCDA gave a single mono-deacetylated product in the penultimate position from the non-reducing end (ADAAA) which was then transformed into a di-deacetylated product (ADDAA). This novel deacetylation pattern expands our toolbox of specific CDAs for biotechnological applications, and will provide further insights into the determinants of substrate specificity in this family of enzymes.
Sponsor: This work was supported by the European Commission NANO3BIO project, grant agreement n° 613931 (to A.P.), and grants BFU2016–77427-C2-1-R (to A.P.) and AGL2015-66833-R (to L.L.) from MINECO, Spain. Pre-doctoral contracts are acknowledged to Generalitat Valenciana (to A.A.), Generalitat de Catalunya (to H.A.), and European Commission NANO3BIO project (to L.G.).
URI: http://hdl.handle.net/10045/73297
ISSN: 2045-2322
DOI: 10.1038/s41598-018-19902-0
Language: eng
Type: info:eu-repo/semantics/article
Rights: Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
Peer Review: si
Publisher version: http://dx.doi.org/10.1038/s41598-018-19902-0
Appears in Collections:INV - Fitopatología - Artículos de Revistas
Research funded by the EU

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