Lysozyme activity of the Ruminococcus champanellensis cellulosome

Sarah Moraïs, Darrell W Cockburn, Yonit Ben-David, Nicole M Koropatkin, Eric C Martens, Sylvia H Duncan, Harry J Flint, Itzhak Mizrahi, Edward A Bayer

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Ruminococcus champanellensis is a keystone species in the human gut that produces an intricate cellulosome system of various architectures. A variety of cellulosomal enzymes have been identified, which exhibit a range of hydrolytic activities on lignocellulosic substrates. We describe herein a unique R. champanellensis scaffoldin, ScaK, which is expressed during growth on cellobiose and comprises a cohesin module and a family 25 glycoside hydrolase (GH25). The GH25 is non-autolytic and exhibits lysozyme-mediated lytic activity against several bacterial species. Despite the narrow acidic pH curve, the enzyme is active along a temperature range from 2 to 85°C and is stable at very high temperatures for extended incubation periods. The ScaK cohesin was shown to bind selectively to the dockerin of a monovalent scaffoldin (ScaG), thus enabling formation of a cell-free cellulosome, whereby ScaG interacts with a divalent scaffodin (ScaA) that bears the enzymes either directly or through additional monovalent scaffoldins (ScaC and ScaD). The ScaK cohesin also interacts with the dockerin of a protein comprising multiple Fn3 domains that can potentially promote adhesion to carbohydrates and the bacterial cell surface. A cell-free cellulosomal GH25 lysozyme may provide a bacterial strategy to both hydrolyze lignocellulose and repel eventual food competitors and/or cheaters. This article is protected by copyright.

Original languageEnglish
Pages (from-to)5112–5122
Number of pages11
JournalEnvironmental Microbiology
Volume18
Issue number12
Early online date23 Aug 2016
DOIs
Publication statusPublished - Dec 2016

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cellulosome
Cellulosomes
Ruminococcus
Muramidase
lysozyme
enzyme
Enzymes
enzymes
Cellobiose
keystone species
lignocellulose
cellobiose
Temperature
Glycoside Hydrolases
cells
hydrolases
adhesion
glycosides
carbohydrate
temperature

Cite this

Moraïs, S., Cockburn, D. W., Ben-David, Y., Koropatkin, N. M., Martens, E. C., Duncan, S. H., ... Bayer, E. A. (2016). Lysozyme activity of the Ruminococcus champanellensis cellulosome. Environmental Microbiology, 18(12), 5112–5122. https://doi.org/10.1111/1462-2920.13501

Lysozyme activity of the Ruminococcus champanellensis cellulosome. / Moraïs, Sarah; Cockburn, Darrell W; Ben-David, Yonit; Koropatkin, Nicole M; Martens, Eric C; Duncan, Sylvia H; Flint, Harry J; Mizrahi, Itzhak; Bayer, Edward A.

In: Environmental Microbiology, Vol. 18, No. 12, 12.2016, p. 5112–5122.

Research output: Contribution to journalArticle

Moraïs, S, Cockburn, DW, Ben-David, Y, Koropatkin, NM, Martens, EC, Duncan, SH, Flint, HJ, Mizrahi, I & Bayer, EA 2016, 'Lysozyme activity of the Ruminococcus champanellensis cellulosome', Environmental Microbiology, vol. 18, no. 12, pp. 5112–5122. https://doi.org/10.1111/1462-2920.13501
Moraïs S, Cockburn DW, Ben-David Y, Koropatkin NM, Martens EC, Duncan SH et al. Lysozyme activity of the Ruminococcus champanellensis cellulosome. Environmental Microbiology. 2016 Dec;18(12):5112–5122. https://doi.org/10.1111/1462-2920.13501
Moraïs, Sarah ; Cockburn, Darrell W ; Ben-David, Yonit ; Koropatkin, Nicole M ; Martens, Eric C ; Duncan, Sylvia H ; Flint, Harry J ; Mizrahi, Itzhak ; Bayer, Edward A. / Lysozyme activity of the Ruminococcus champanellensis cellulosome. In: Environmental Microbiology. 2016 ; Vol. 18, No. 12. pp. 5112–5122.
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abstract = "Ruminococcus champanellensis is a keystone species in the human gut that produces an intricate cellulosome system of various architectures. A variety of cellulosomal enzymes have been identified, which exhibit a range of hydrolytic activities on lignocellulosic substrates. We describe herein a unique R. champanellensis scaffoldin, ScaK, which is expressed during growth on cellobiose and comprises a cohesin module and a family 25 glycoside hydrolase (GH25). The GH25 is non-autolytic and exhibits lysozyme-mediated lytic activity against several bacterial species. Despite the narrow acidic pH curve, the enzyme is active along a temperature range from 2 to 85°C and is stable at very high temperatures for extended incubation periods. The ScaK cohesin was shown to bind selectively to the dockerin of a monovalent scaffoldin (ScaG), thus enabling formation of a cell-free cellulosome, whereby ScaG interacts with a divalent scaffodin (ScaA) that bears the enzymes either directly or through additional monovalent scaffoldins (ScaC and ScaD). The ScaK cohesin also interacts with the dockerin of a protein comprising multiple Fn3 domains that can potentially promote adhesion to carbohydrates and the bacterial cell surface. A cell-free cellulosomal GH25 lysozyme may provide a bacterial strategy to both hydrolyze lignocellulose and repel eventual food competitors and/or cheaters. This article is protected by copyright.",
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N1 - Acknowledgements This research was supported by a grant to EAB, NMK and ECM from the United States-Israel Binational Science. Foundation (BSF), Jerusalem, Israel and by a grant (No.1349) to EAB from the Israel Science Foundation (ISF). Additional support was obtained from the establishment of an Israeli Center of Research Excellence (I-CORE Center No.152/11) managed by the Israel Science Foundation. The authors also appreciate the support of the European Union, Area NMP.2013.1.1-2: Self-assembly of naturally occurring nanosystems: CellulosomePlus Project number: 604530. HJF and SHD acknowledge financial support from the Scottish Government Rural and Environmental Sciences and Analytical Services (SG-RESAS) and from BBSRC grant no BB/L009951/1. EAB is the incumbent of The Maynard I. and Elaine Wishner Chair of Bio-organic Chemistry.

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N2 - Ruminococcus champanellensis is a keystone species in the human gut that produces an intricate cellulosome system of various architectures. A variety of cellulosomal enzymes have been identified, which exhibit a range of hydrolytic activities on lignocellulosic substrates. We describe herein a unique R. champanellensis scaffoldin, ScaK, which is expressed during growth on cellobiose and comprises a cohesin module and a family 25 glycoside hydrolase (GH25). The GH25 is non-autolytic and exhibits lysozyme-mediated lytic activity against several bacterial species. Despite the narrow acidic pH curve, the enzyme is active along a temperature range from 2 to 85°C and is stable at very high temperatures for extended incubation periods. The ScaK cohesin was shown to bind selectively to the dockerin of a monovalent scaffoldin (ScaG), thus enabling formation of a cell-free cellulosome, whereby ScaG interacts with a divalent scaffodin (ScaA) that bears the enzymes either directly or through additional monovalent scaffoldins (ScaC and ScaD). The ScaK cohesin also interacts with the dockerin of a protein comprising multiple Fn3 domains that can potentially promote adhesion to carbohydrates and the bacterial cell surface. A cell-free cellulosomal GH25 lysozyme may provide a bacterial strategy to both hydrolyze lignocellulose and repel eventual food competitors and/or cheaters. This article is protected by copyright.

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