Biofilm inhibitors that target amyloid proteins

Chemistry and Biology

Volumn 20, Issue 1, 2013, Pages 102-110

  Romero, Diego ^a   Sanabria Valentín, Edgardo ^a   Vlamakis, Hera ^a   Kolter, Roberto ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; BIOFILM INHIBITOR; DOCEBENONE; FUNGAL PROTEIN; NEW1 PROTEIN; PARTHENOLIDE; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS CEREUS; BACILLUS SUBTILIS; BIOFILM; CELL SURFACE; CONTROLLED STUDY; ESCHERICHIA COLI; FLOW CYTOMETRY; GENE EXPRESSION; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN POLYMERIZATION; PROTEIN TARGETING;

AMYLOIDOGENIC PROTEINS; ANTI-BACTERIAL AGENTS; BACILLUS CEREUS; BACILLUS SUBTILIS; BACTERIAL PROTEINS; BENZOQUINONES; BIOFILMS; ESCHERICHIA COLI; HUMANS; SESQUITERPENES;

EID: 84872966256     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2012.10.021     Document Type: Article

References (39)

1. H. Amijee, J. Madine, D.A. Middleton, and A.J. Doig Inhibitors of protein aggregation and toxicity Biochem. Soc. Trans. 37 2009 692 696
2. M.P. Badtke, N.D. Hammer, and M.R. Chapman Functional amyloids signal their arrival Sci. Signal. 2 2009 pe43
3. L.P. Blanco, M.L. Evans, D.R. Smith, M.P. Badtke, and M.R. Chapman Diversity, biogenesis and function of microbial amyloids Trends Microbiol. 20 2012 66 73
4. S.S. Branda, J.E. González-Pastor, S. Ben-Yehuda, R. Losick, and R. Kolter Fruiting body formation by Bacillus subtilis Proc. Natl. Acad. Sci. USA 98 2001 11621 11626 (Pubitemid 32928778)
5. S.S. Branda, J.E. González-Pastor, E. Dervyn, S.D. Ehrlich, R. Losick, and R. Kolter Genes involved in formation of structured multicellular communities by Bacillus subtilis J. Bacteriol. 186 2004 3970 3979 (Pubitemid 38746073)
6. S.S. Branda, S. Vik, L. Friedman, and R. Kolter Biofilms: the matrix revisited Trends Microbiol. 13 2005 20 26 (Pubitemid 40082393)
7. S.S. Branda, F. Chu, D.B. Kearns, R. Losick, and R. Kolter A major protein component of the Bacillus subtilis biofilm matrix Mol. Microbiol. 59 2006 1229 1238
8. L. Cegelski, J.S. Pinkner, N.D. Hammer, C.K. Cusumano, C.S. Hung, E. Chorell, V. Aberg, J.N. Walker, P.C. Seed, and F. Almqvist Small-molecule inhibitors target Escherichia coli amyloid biogenesis and biofilm formation Nat. Chem. Biol. 5 2009 913 919
9. M.R. Chapman, L.S. Robinson, J.S. Pinkner, R. Roth, J. Heuser, M. Hammar, S. Normark, and S.J. Hultgren Role of Escherichia coli curli operons in directing amyloid fiber formation Science 295 2002 851 855 (Pubitemid 34118365)
10. D. Claessen, H.A. Wösten, G. van Keulen, O.G. Faber, A.M. Alves, W.G. Meijer, and L. Dijkhuizen Two novel homologous proteins of Streptomyces coelicolor and Streptomyces lividans are involved in the formation of the rodlet layer and mediate attachment to a hydrophobic surface Mol. Microbiol. 44 2002 1483 1492 (Pubitemid 34639427)
11. C.M. Dobson Principles of protein folding, misfolding and aggregation Semin. Cell Dev. Biol. 15 2004 3 16 (Pubitemid 38177363)
12. M.S. Dueholm, S.V. Petersen, M. Sønderkær, P. Larsen, G. Christiansen, K.L. Hein, J.J. Enghild, J.L. Nielsen, K.L. Nielsen, P.H. Nielsen, and D.E. Otzen Functional amyloid in Pseudomonas Mol. Microbiol. 77 2010 1009 1020
13. B.Y. Feng, B.H. Toyama, H. Wille, D.W. Colby, S.R. Collins, B.C. May, S.B. Prusiner, J. Weissman, and B.K. Shoichet Small-molecule aggregates inhibit amyloid polymerization Nat. Chem. Biol. 4 2008 197 199 (Pubitemid 351264126)
14. D.M. Fowler, A.V. Koulov, W.E. Balch, and J.W. Kelly Functional amyloid - from bacteria to humans Trends Biochem. Sci. 32 2007 217 224 (Pubitemid 46694328)
15. S.J. Garrity, V. Sivanathan, J. Dong, S. Lindquist, and A. Hochschild Conversion of a yeast prion protein to an infectious form in bacteria Proc. Natl. Acad. Sci. USA 107 2010 10596 10601
16. L. Gasparini, L. Rusconi, H. Xu, P. del Soldato, and E. Ongini Modulation of beta-amyloid metabolism by non-steroidal anti-inflammatory drugs in neuronal cell cultures J. Neurochem. 88 2004 337 348 (Pubitemid 38084550)
17. M.F. Gebbink, D. Claessen, B. Bouma, L. Dijkhuizen, and H.A. Wösten Amyloids - a functional coat for microorganisms Nat. Rev. Microbiol. 3 2005 333 341 (Pubitemid 40443726)
18. I. Horvath, C.F. Weise, E.K. Andersson, E. Chorell, M. Sellstedt, C. Bengtsson, A. Olofsson, S.J. Hultgren, M. Chapman, and M. Wolf-Watz Mechanisms of protein oligomerization: inhibitor of functional amyloids templates α-synuclein fibrillation J. Am. Chem. Soc. 134 2012 3439 3444
19. I. Kolodkin-Gal, D. Romero, S. Cao, J. Clardy, R. Kolter, and R. Losick D-amino acids trigger biofilm disassembly Science 328 2010 627 629
20. J. Li, M. Zhu, S. Rajamani, V.N. Uversky, and A.L. Fink Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils Chem. Biol. 11 2004 1513 1521 (Pubitemid 39527278)
21. D. López, H. Vlamakis, R. Losick, and R. Kolter Cannibalism enhances biofilm development in Bacillus subtilis Mol. Microbiol. 74 2009 609 618
22. V.B. Mathema, Y.S. Koh, B.C. Thakuri, and M. Sillanpää Parthenolide, a sesquiterpene lactone, expresses multiple anti-cancer and anti-inflammatory activities Inflammation 35 2012 560 565
23. C.P. Maury The emerging concept of functional amyloid J. Intern. Med. 265 2009 329 334
24. R.M. Murphy Peptide aggregation in neurodegenerative disease Annu. Rev. Biomed. Eng. 4 2002 155 174 (Pubitemid 35217418)
25. Q. Nie, X.G. Du, and M.Y. Geng Small molecule inhibitors of amyloid β peptide aggregation as a potential therapeutic strategy for Alzheimer's disease Acta Pharmacol. Sin. 32 2011 545 551
26. G.A. O'Toole, and R. Kolter Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis Mol. Microbiol. 28 1998 449 461 (Pubitemid 28218392)
27. G. O'Toole, H.B. Kaplan, and R. Kolter Biofilm formation as microbial development Annu. Rev. Microbiol. 54 2000 49 79
28. B.E. Roberts, M.L. Duennwald, H. Wang, C. Chung, N.P. Lopreiato, E.A. Sweeny, M.N. Knight, and J. Shorter A synergistic small-molecule combination directly eradicates diverse prion strain structures Nat. Chem. Biol. 5 2009 936 946
29. D. Romero, and R. Kolter Will biofilm disassembly agents make it to market? Trends Microbiol. 19 2011 304 306
30. D. Romero, C. Aguilar, R. Losick, and R. Kolter Amyloid fibers provide structural integrity to Bacillus subtilis biofilms Proc. Natl. Acad. Sci. USA 107 2010 2230 2234
31. D. Romero, H. Vlamakis, R. Losick, and R. Kolter An accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms Mol. Microbiol. 80 2011 1155 1168
32. C.A. Szekely, and P.P. Zandi Non-steroidal anti-inflammatory drugs and Alzheimer's disease: the epidemiological evidence CNS Neurol. Disord. Drug Targets 9 2010 132 139
33. E. Titos, J. Clària, A. Planagumà, M. López-Parra, N. Villamor, M. Párrizas, A. Carrió, R. Miquel, W. Jiménez, and V. Arroyo Inhibition of 5-lipoxygenase induces cell growth arrest and apoptosis in rat Kupffer cells: implications for liver fibrosis FASEB J. 17 2003 1745 1747
34. T. Tomiyama, H. Kaneko, K. Kataoka, S. Asano, and N. Endo Rifampicin inhibits the toxicity of pre-aggregated amyloid peptides by binding to peptide fibrils and preventing amyloid-cell interaction Biochem. J. 322 1997 859 865 (Pubitemid 27135636)
35. H. Vlamakis, C. Aguilar, R. Losick, and R. Kolter Control of cell fate by the formation of an architecturally complex bacterial community Genes Dev. 22 2008 945 953 (Pubitemid 351482847)
36. S. Weggen, J.L. Eriksen, P. Das, S.A. Sagi, R. Wang, C.U. Pietrzik, K.A. Findlay, T.E. Smith, M.P. Murphy, and T. Bulter A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity Nature 414 2001 212 216 (Pubitemid 33051236)
37. H.A. Wösten, and M.L. de Vocht Hydrophobins, the fungal coat unravelled Biochim. Biophys. Acta 1469 2000 79 86
38. R.E. Yasbin, and F.E. Young Transduction in Bacillus subtilis by bacteriophage SPP1 J. Virol. 14 1974 1343 1348
39. T. Yoshimoto, C. Yokoyama, K. Ochi, S. Yamamoto, Y. Maki, Y. Ashida, S. Terao, and M. Shiraishi 2,3,5-Trimethyl-6-(12-hydroxy-5,10-dodecadiynyl)-1,4- benzoquinone (AA861), a selective inhibitor of the 5-lipoxygenase reaction and the biosynthesis of slow-reacting substance of anaphylaxis Biochim. Biophys. Acta 713 1982 470 473 (Pubitemid 13222960)