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Amyloid fibers provide structural integrity to Bacillus subtilis biofilms
Open accessAbstract
Bacillus subtilis forms biofilms whose constituent cells are held together by an extracellular matrix. Previous studies have shown that the protein TasA and an exopolysaccharide are the main components of the matrix. Given the importance of TasA in biofilm formation, we characterized the physicochemical properties of this protein. We report that purified TasA forms fibers of variable length and 10–15 nm in width. Biochemical analyses, in combination with the use of specific dyes and microscopic analyses, indicate that TasA forms amyloid fibers. Consistent with this hypothesis, TasA fibers required harsh treatments (e.g., formic acid) to be depolymerized. When added to a culture of a tasA mutant, purified TasA restored wild-type biofilm morphology, indicating that the purified protein retained biological activity. We propose that TasA forms amyloid fibers that bind cells together in the biofilm.
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365
Fruiting body formation by Bacillus subtilis
Branda, S. S., González-Pastor, J. E., Ben-Yehuda, S., Losick, R., & Kolter, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191384198 · Cited by 1,129
Self-citationClaessen, D., Rink, R., de Jong, W., Siebring, J., de Vreugd, P., Boersma, F. G. H., Dijkhuizen, L., & Wösten, H. A. B. (2003) · Genes & Development · doi:10.1101/gad.264303 · Cited by 327
Research works printed but not linked: 37
- 10.1146/annurev.micro.54.1.49 · DOI · Paper page
- 10.1016/j.tim.2004.11.006 · DOI · Paper page
- 10.1128/JB.01920-07 · DOI · Paper page
- 10.1016/S1438-4221(00)80102-2 · DOI · Paper page
- 10.1016/j.resmic.2005.11.003 · DOI · Paper page
- KP Lemon, AM Earl, HC Vlamakis, C Aguilar, R Kolter, Biofilm development with an emphasis on Bacillus subtilis . Curr Top Microbiol Immunol 322, 1–16 (2008).
- 10.1128/AEM.71.1.247-254.2005 · DOI · Paper page
- 10.1046/j.1365-2958.2001.02337.x · DOI · Paper page
- 10.1111/j.1462-5822.2008.01148.x · DOI
- 10.1126/science.1067484 · DOI · Paper page
- 10.1016/S0076-6879(99)09019-9 · DOI · Paper page
- 10.1006/jmbi.1997.1348 · DOI · Paper page
- 10.1016/S0076-6879(99)09022-9 · DOI · Paper page
- 10.1038/nrmicro1127 · DOI · Paper page
- 10.1016/j.tibs.2007.03.003 · DOI · Paper page
- 10.1074/jbc.M602576200 · DOI
- 10.1073/pnas.0602304104 · DOI · Paper page
- W de Jong, HA Wosten, L Dijkhuizen, D Claessen, Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae that are anchored to the cell surface via cellulose. Mol Microbiol 73, 1128–1140 (2009).
- 10.1016/S0304-4157(00)00002-2 · DOI · Paper page
- 10.1016/j.femsre.2005.01.004 · DOI · Paper page
- 10.1111/j.1462-2920.2007.01418.x · DOI · Paper page
- 10.1101/gad.1645008 · DOI · Paper page
- 10.1111/j.1365-2958.2005.05020.x · DOI · Paper page
- 10.1128/JB.181.12.3632-3643.1999 · DOI
- 10.1128/JB.181.5.1664-1672.1999 · DOI
- 10.1074/jbc.M011499200 · DOI · Paper page
- 10.1111/j.1365-2958.2004.04440.x · DOI · Paper page
- 10.1074/jbc.M205570200 · DOI · Paper page
- 10.1111/j.1742-4658.2009.07250.x · DOI
- 10.1146/annurev.micro.60.080805.142106 · DOI · Paper page
- 10.1074/jbc.M609228200 · DOI · Paper page
- 10.1016/S0021-9258(18)47347-4 · DOI
- 10.1038/nsmb.1617 · DOI
- 10.1128/jb.175.1.12-18.1993 · DOI
- 10.1529/biophysj.108.130997 · DOI · Paper page
- 10.1073/pnas.0802593105 · DOI · Paper page
- 10.1016/S0076-6879(99)09021-7 · DOI · Paper page
Cited by
The antimicrobial activity of nanoparticles: present situation and prospects for the future
Wang, L., Hu, C., & Shao, L. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s121956 · Cited by 4,062
Hyldgaard, M., Mygind, T., & Meyer, R. L. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00012 · Cited by 2,191
Strategies for combating bacterial biofilm infections
Wu, H., Moser, C., Wang, H.-Z., Høiby, N., & Song, Z.-J. (2015) · International Journal of Oral Science · doi:10.1038/ijos.2014.65 · Cited by 925
d -Amino Acids Trigger Biofilm Disassembly
Kolodkin-Gal, I., Romero, D., Cao, S., Clardy, J., Kolter, R., & Losick, R. (2010) · Science · doi:10.1126/science.1188628 · Cited by 874
Self-citationHobley, L., Harkins, C., MacPhee, C. E., & Stanley-Wall, N. R. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv015 · Cited by 581
“The production and assembly of amyloid-like fibres in the B. subtilis biofilm matrix is accomplished by the proteins encoded within the tapA-sipW-tasA operon (Branda et al. 2006; Romero et al. 2010) (Fig.”
BackgroundMethodInfluential
Metadata
- Authors
- Romero, D., Aguilar, C., Losick, R., & Kolter, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-01-13
- Volume
- 107
- Issue
- 5
- Pages
- 2230-2234
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2086603752
- Cited by
- 792
- References
- 5
- FWCI
- 15.01
- Type
- journal article
- Language
- en
- Open access
- green
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- Romero, D., Aguilar, C., Losick, R., & Kolter, R. (2010). Amyloid fibers provide structural integrity to Bacillus subtilis biofilms. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0910560107
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