Identification of an amyloidogenic peptide from the bap protein of Staphylococcus epidermidis

Protein and Peptide Letters

Volumn 21, Issue 1, 2014, Pages 75-79

  Lembré, Pierre ^a   Vendrely, Charlotte ^a   Di Martino, Patrick ^a  

^a UNIVERSITÉ DE CERGY PONTOISE   (France)

Author keywords

Amyloid; Bap; Biofilm; Peptide; Staphylococcus epidermidis

Indexed keywords

AMYLOID; AMYLOID PROTEIN; BAP PROTEIN; PROTEIN; THIOFLAVINE; UNCLASSIFIED DRUG;

ACINETOBACTER BAUMANNII; AGGRESCAN SOFTWARE; AMINO ACID SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; BETA SHEET; BIOFILM; COMPUTER PROGRAM; ESCHERICHIA COLI; INFRARED SPECTROSCOPY; NONHUMAN; NUCLEOTIDE SEQUENCE; PASTA SOFTWARE; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; SALMONELLA ENTERICA; STAPHYLOCOCCUS EPIDERMIDIS; TANGO SOFTWARE;

AMYLOIDOGENIC PROTEINS; BACTERIAL PROTEINS; BIOFILMS; MEMBRANE PROTEINS; MICROSCOPY, ATOMIC FORCE; SPECTROPHOTOMETRY, INFRARED; STAPHYLOCOCCUS EPIDERMIDIS; THIAZOLES;

EID: 84891468157     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/09298665113209990072     Document Type: Article

References (37)

1. Lasa, I.; Penades, J.R. Bap: a family of surface proteins involved in biofilm formation. Res. Microbiol., 2006, 157, 99-107.
2. Cucarella, C.; Solano, C.; Valle, J.; Amorena, B.; Lasa, I.I.; Penades, J.R. Bap, a Staphylococcus aureus surface protein involved in biofilm formation. J. Bacteriol., 2001, 183, 2888-2896.
3. Tormo, M.A.; Knecht, E.; Gotz, F.; Lasa, I.; Penades, J.R. Bapdependent biofilm formation by pathogenic species of Staphylococcus: evidence of horizontal gene transfer? Microbiology, 2005, 151, 2465-2475.
4. Bowden, M.G.; Chen, W.; Singvall, J.; Xu Y.; Peacock, S.J.; Valtulina, V.; Speziale, P.; Höök, M. Identification and preliminary characterization of cell-wall-anchored proteins of Staphylococcus epidermidis. Microbiology, 2005, 151, 1453-1464.
5. Foster, T.J.; Hook, M. Surface protein adhesins of Staphylococcus aureus. Trends Microbiol., 1998, 6, 484-488.
6. Rich, R.L.; Demeler, B.; Ashby, K.; Deivanayagam, C.C.; Petrich, J.W.; Patti, J.M.; Narayana, S.V.; Hook, M. Domain structure of the Staphylococcus aureus collagen adhesion. Biochemistry, 1998, 37, 15423-15433.
7. Callebaut, I.; Gilges, D.; Vigon, I.; Mornon, J.P. HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold. Protein Sci., 2000, 9, 1382-1390.
8. Josefsson, E.; McCrea, K.W.; Ni Eidhin, D.; O'Connell, D.; Cox, J.; Hook, M.; Foster, T.J. Three new members of the serineaspartate repeat protein multigene family of Staphylococcus aureus. Microbiology, 1998, 144, 3387-3395.
9. Larsen, P.; Nielsen, J.L.; Dueholm, M.S.; Wetzel, R.; Otzen, D.; Nielsen, P.H. Amyloid adhesins are abundant in natural biofilms. Environ. Microbiol., 2007, 9, 3077-3090.
10. Larsen, P.; Nielsen, J.L.; Otzen, D.; Nielsen, P.H. Amyloid-like adhesins produced by floc-forming and filamentous bacteria in activated sludge. Appl. Environ. Microbiol., 2008, 74, 1517-1526.
11. Maltsev, A.V.; Bystryak, S.; Galzitskaya, O.V. The role of β-amyloid peptide in neurodegenerative diseases. Ageing Res. Rev., 2011, 10, 440-452.
12. Ramsook, C.B.; Tan, C.; Garcia, M.C.; Fung, R.; Soybelman, G.; Henry, R.; Litewka, A.; O'Meally, S.; Otoo, H.N.; Khalaf, R.A.; Dranginis, A.M.; Gaur, N.K.; Klotz, S.A.; Rauceo, J.M.; Jue, C.K.; Lipke, P.N. Yeast cell adhesion molecules have functional amyloid-forming sequences. Eukaryot. Cell, 2010, 9, 393-404.
13. Sunde, M.; Serpell, L.C.; Bartlam, M.; Fraser, P.E.; Pepys, M.B.; Blake, C.C. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol., 1997, 273, 729-739.
14. LeVine, H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci., 1993, 2, 404-410.
15. Inouye, H.; Kirschner, D.A. X-Ray fiber and powder diffraction of PrP prion peptides. Adv. Protein Chem., 2006, 73, 181-215.
16. Sawaya, M.R.; Sambashivan, S.; Nelson, R.; Ivanova, M.I.; Sievers, S.A.; Apostol, M.I.; Thompson, M.J.; Balbirnie, M.; Wiltzius, J.J.; Mcfarlane, H.T. Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature, 2007, 447, 453-457.
17. Sanchez De Groot, N.; Pallares, I.; Aviles, F.X.; Vendrell, J.; Ventura, S. Prediction of "hot spots" of aggregation in diseaselinked polypeptides. BMC Struct. Biol., 2005, 5, 18.
18. Olsen, A.; Jonsson, A.; Normark, S. Fibronectin binding mediated by a novel class of surface organelles on Escherichia coli. Nature, 1989, 338, 652-655.
19. Van Houdt, R.; Michiels, C. Role of bacterial cell surface structures in Escherichia coli biofilm formation. Res. Microbiol., 2005, 156, 626-633.
20. Wang, X.; Chapman, M.R. Curli provide the template for understanding controlled amyloid propagation. Prion, 2008, 2, 57-60.
21. Vidal, O.; Longin, R.; Prigent-Combaret, C.; Dorel, C.; Hooreman, M.; Lejeune, P. Isolation of an Escherichia coli K-12 mutant strain able to form biofilms on inert surfaces: involvement of a new ompR allele that increases curli expression. J. Bacteriol., 1998, 180, 2442-2449.
22. Barnhart, M. M.; Chapman, M. R. Curli biogenesis and function. Annu. Rev. Microbiol., 2006, 60, 131-147.
23. Wang, X.; Chapman, M.R. Sequence determinants of bacterial amyloid formation. J. Mol. Biol., 2008, 380, 570-580.
24. Cherny, I.; Rockah, L.; Levy-Nissenbaum, O.; Gophna, U.; Ron E. Z.; Gazit, E. The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats. J. Mol. Biol., 2005, 352, 245-252.
25. Wang, X.; Smith, D.R.; Jones, J.W.; Chapman, M.R. In vitro polymerization of a functional Escherichia coli amyloid protein. J. Biol. Chem., 2007, 282, 3713-3719.
26. Lembre, P.; Vendrely, C.; Di Martino, P. Amyloid Fiber Formation by Synthetic Peptides Derived from the Sequence of the Protein CsgA of Escherichia coli. Protein Pept. Lett., 2013, 20, 942-946
27. Latasa, C.; Roux, A.; Toledo-Arana, A.; Ghigo, J.M.; Gamazo, C.; Penades, J. R.; Lasa, I. BapA, a large secreted protein required for biofilm formation and host colonization of Salmonella enterica serovar Enteritidis. Mol. Microbiol., 2005, 58, 1322-1339.
28. Conchillo-Solé, O.; de Groot, N.S.; Avilés, F.X.; Vendrell, J.; Daura, X.; Ventura, S. AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC Bioinformatics, 2007, 8, 65.
29. Trovato, A.; Seno, F.; Tosatto, S.C. The PASTA server for protein aggregation prediction. Protein Eng. Des. Sel., 2007, 20, 521-523.
30. Fernandez-Escamilla, A.M.; Rousseau, F.; Schymkowitz, J.; Serrano, L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol., 2004, 22, 1302-1306.
31. Ahmed, A.B.; Kajava, A.V. Breaking the amyloidogenicity code: methods to predict amyloids from amino acid sequence. FEBS Lett., 2013, 587,1089-1095.
32. Cucarella, C.; Tormo, M.A.; Ubeda, C.; Trotonda, M.P.; Monzon, M.; Peris, C.; Amorena, B.; Lasa, I.; Penades, J.R. Role of biofilmassociated protein bap in the pathogenesis of bovine Staphylococcus aureus. Infect. Immun., 2004, 72, 2177-2185.
33. Arrizubieta, M.J.; Toledo-Arana, A.; Amorena, B.; Penades, J.R.; Lasa, I. Calcium inhibits bap-dependent multicellular behavior in Staphylococcus aureus. J. Bacteriol., 2004, 186, 7490-7498.
34. Lopez de la Paz, M.; Serrano L. Sequence determinants of amyloid fibril formation. Proc. Natl. Acad. Sci. USA, 2004, 101, 87-92.
35. Lu, Y.; Derreumaux, P.; Guo, Z.; Mousseau, N.; Wei, G. Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent. Proteins, 2009, 75, 954-963.
36. Loehfelm, T.W.; Luke, N.R.; Campagnari, A.A. Identification and characterization of an Acinetobacter baumannii biofilm-associated protein. J. Bacteriol., 2008, 190, 1036-1044.
37. Tzotzos, S.; Doig, A.J. Amyloidogenic sequences in native protein structures. Protein Sci., 2010, 19, 327-348.