Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/145843
Title: Phase transitions by an abundant protein in the anammox extracellular matrix mediate cell-to-cell aggregation and biofilm formation
Authors: Seviour, Thomas
Wong, Lan Li
Lu, Yang
Mugunthan, Sudarsan
Yang, Qiaohui
Chanda Segaran, Uma Shankari
Bessarab, Irina
Liebl, David
Williams, Rohan B. H.
Law, Yingyu
Kjelleberg, Staffan
Keywords: Science::Biological sciences
Issue Date: 2020
Source: Seviour, T., Wong, L. L., Lu, Y., Chanda Segaran, U. S., Bessarab, I., Liebl, D., . . . Kjelleberg, S. (2020). Phase transitions by an abundant protein in the anammox extracellular matrix mediate cell-to-cell aggregation and biofilm formation. mBio, 11(5), e02052-20-. doi:10.1128/mBio.02052-20
Journal: mBio 
Abstract: This study describes the first direct functional assignment of a highly abundant extracellular protein from a key environmental and biotechnological biofilm performing an anaerobic ammonium oxidation (anammox) process. Expression levels of Brosi_A1236, belonging to a class of proteins previously suggested to be cell surface associated, were in the top one percentile of all genes in the "Candidatus Brocadia sinica"-enriched biofilm. The Brosi_A1236 structure was computationally predicted to consist of immunoglobulin-like anti-parallel β-strands, and circular dichroism conducted on the isolated surface protein indicated that β-strands are the dominant higher-order structure. The isolated protein was stained positively by the β-sheet-specific stain thioflavin T, along with cell surface- and matrix-associated regions of the biofilm. The surface protein has a large unstructured content, including two highly disordered domains at its C terminus. The disordered domains bound to the substratum and thereby facilitated the adhesion of negatively charged latex microspheres, which were used as a proxy for cells. The disordered domains and isolated whole surface protein also underwent liquid-liquid phase separation to form liquid droplets in suspension. Liquid droplets of disordered protein wet the surfaces of microspheres and bacterial cells and facilitated their coalescence. Furthermore, the surface layer protein formed gels as well as ordered crystalline structures. These observations suggest that biophysical remodeling through phase transitions promotes aggregation and biofilm formation. Importance: By employing biophysical and liquid-liquid phase separation concepts, this study revealed how a highly abundant extracellular protein enhances the key environmental and industrial bioprocess of anaerobic ammonium oxidation (anammox). Extracellular proteins of environmental biofilms are understudied and poorly annotated in public databases. Understanding the function of extracellular proteins is also increasingly important for improving bioprocesses and resource recovery. Here, protein functions were assessed based on theoretical predictions of intrinsically disordered domains, known to promote adhesion and liquid-liquid phase separation, and available surface layer protein properties. A model is thus proposed to explain how the protein promotes aggregation and biofilm formation by extracellular matrix remodeling and phase transitions. This work provides a strong foundation for functional investigations of extracellular proteins involved in biofilm development.
URI: https://hdl.handle.net/10356/145843
ISSN: 2161-2129
DOI: 10.1128/mBio.02052-20
Rights: © 2020 Seviour et al. This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SCELSE Journal Articles

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