Curing bacterial infections with protein aggregates

Molecular Microbiology

Volumn 99, Issue 5, 2016, Pages 827-830

  Ventura, Salvador ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT; ANTIINFECTIVE AGENT; PEPTIDE; PROTEIN AGGREGATE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL INFECTION; BACTERICIDAL ACTIVITY; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN HOMEOSTASIS; PROTEIN STRUCTURE; ANIMAL; BACTERIUM; METABOLISM;

ANIMALS; ANTI-BACTERIAL AGENTS; BACTERIA; BACTERIAL INFECTIONS; HUMANS; PEPTIDES; PROTEIN AGGREGATES;

EID: 84961711999     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.13293     Document Type: Article

References (31)

1. Bednarska, N.G., Van Eldere, J., Gallardo, R., Ganesan, A., Ramakers, M., Vogel, I., et al. (2015) Protein aggregation as an antibiotic design strategy. Mol. Microbiol 99: 849-865.
2. Berke, S.J., and Paulson, H.L. (2003) Protein aggregation and the ubiquitin proteasome pathway: gaining the UPPer hand on neurodegeneration. Curr. Opin. Genet. Dev 13: 253-261.
3. Buell, A.K., Dobson, C.M., and Knowles, T.P. (2014) The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation. Essays Biochem 56: 11-39.
4. Castillo, V., Grana-Montes, R., Sabate, R., and Ventura, S. (2011) Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes. Biotechnol J 6: 674-685.
5. Chiti, F., and Dobson, C.M. (2006) Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75: 333-366.
6. Dobson, C.M. (2004) Principles of protein folding, misfolding and aggregation. Semin. Cell Dev Biol 15: 3-16.
7. Dovidchenko, N.V., and Galzitskaya, O.V. (2015) Computational Approaches to Identification of Aggregation Sites and the Mechanism of Amyloid Growth. Adv Exp Med Biol 855: 213-239.
8. Eisenberg, D., and Jucker, M. (2012) The amyloid state of proteins in human diseases. Cell 148: 1188-1203.
9. Ellis, R.J. (2001) Macromolecular crowding: obvious but underappreciated. Trends Biochem Sci 26: 597-604.
10. Fowler, D.M., Koulov, A.V., Balch, W.E., and Kelly, J.W. (2007) Functional amyloid-from bacteria to humans. Trends Biochem Sci 32: 217-224.
11. Gidalevitz, T., Kikis, E.A., and Morimoto, R.I. (2010) A cellular perspective on conformational disease: the role of genetic background and proteostasis networks. Curr Opin Struct Biol 20: 23-32.
12. Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis. Nature 475: 324-332.
13. Invernizzi, G., Papaleo, E., Sabate, R., and Ventura, S. (2012) Protein aggregation: mechanisms and functional consequences. Int J Biochem Cell Biol 44: 1541-1554.
14. Jahn, T.R., and Radford, S.E. (2005) The Yin and Yang of protein folding. FEBS J 272: 5962-5970.
15. Jahn, T.R., and Radford, S.E. (2008) Folding versus aggregation: polypeptide conformations on competing pathways. Arch Biochem Biophys 469: 100-117.
16. Karran, E., Mercken, M., and De Strooper, B. (2011) The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics. Nat Rev Drug Discov 10: 698-712.
17. Kim, Y.E., Hipp, M.S., Bracher, A., Hayer-Hartl, M., and Hartl, F.U. (2013) Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem 82: 323-355.
18. Last, N.B., and Miranker, A.D. (2013) Common mechanismunites membrane poration by amyloid and antimicrobial peptides. Proc Natl Acad Sci USA 110: 6382-6387.
19. Linding, R., Schymkowitz, J., Rousseau, F., Diella, F., and Serrano, L. (2004) A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins. J Mol Biol 342: 345-353.
20. Martin, L., van Meegern, A., Doemming, S., and Schuerholz, T. (2015) Antimicrobial peptides in human sepsis. Front Immunol 6: 404.
21. Morales, R., Moreno-Gonzalez, I., and Soto, C. (2013) Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases. PLoS Pathog 9: e1003537.
22. Pastor, M.T., Esteras-Chopo, A., and Serrano, L. (2007) Hacking the code of amyloid formation: the amyloid stretch hypothesis. Prion 1: 9-14.
23. Reumers, J., Maurer-Stroh, S., Schymkowitz, J., and Rousseau, F. (2009) Protein sequences encode safeguards against aggregation. Hum. Mutat. 30: 431-437.
24. Rousseau, F., Serrano, L., and Schymkowitz, J.W. (2006) How evolutionary pressure against protein aggregation shaped chaperone specificity. J Mol Biol 355: 1037-1047.
25. Sanchez de Groot, N., Torrent, M., Villar-Pique, A., Lang, B., Ventura, S., Gsponer, J., and Babu, M.M. (2012) Evolutionary selection for protein aggregation. Biochem Soc Trans 40: 1032-1037.
26. Selkoe, D.J. (2003) Folding proteins in fatal ways. Nature 426: 900-904.
27. Soscia, S.J., Kirby, J.E., Washicosky, K.J., Tucker, S.M., Ingelsson, M., Hyman, B., et al. (2010) The Alzheimer's disease-associated amyloid beta-protein is an antimicrobial peptide. PLoS One 5: e9505.
28. Torrent, M., Pulido, D., Nogues, M.V., and Boix, E. (2012) Exploring new biological functions of amyloids: bacteria cell agglutination mediated by host protein aggregation. PLoS Pathog. 8: e1003005.
29. Torrent, M., Valle, J., Nogues, M.V., Boix, E., and Andreu, D. (2011) The generation of antimicrobial peptide activity: a trade-off between charge and aggregation? Angew Chem Int Ed Engl 50: 10686-10689.
30. Uversky, V.N., and Fink A.L. (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 1698: 131-153.
31. Ventura, S., Zurdo, J., Narayanan, S., Parreno, M., Mangues, R., Reif, B., et al. (2004) Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proc Natl Acad Sci USA 101: 7258-7263.