An anti-infective synthetic peptide with dual antimicrobial and immunomodulatory activities

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Silva, O N ^a,b   De La Fuente Nunez C ^c,d,e,f,g   Haney, E F ^h   Fensterseifer, I C M ^i,j   Ribeiro, S M ^b   Porto, W F ^j   Brown, P ^c   Faria Junior, C ^j   Rezende, T M B ^i,j   Moreno, S E ^b   Lu, T K ^c,d,e,f,g   Hancock, R E W ^h   Franco, O L ^a,b,i,j  

^a FEDERAL UNIVERSITY OF JUIZ DE FORA   (Brazil)

^b UNIVERSIDADE CATÓLICA DOM BOSCO   (Brazil)

^c Massachusetts Institute of Technology Cambridge   (United States)

^d MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^e Department of Electrical Engineering and Computer Science   (United States)

^f BROAD INSTITUTE OF MIT AND HARVARD   (United States)

^g HARVARD UNIVERSITY   (United States)

^h UNIVERSITY OF BRITISH COLUMBIA   (Canada)

ⁱ UNIVERSIDADE CATÓLICA DE BRASÍLIA   (Brazil)

^j UNIVERSITY OF BRASILIA   (Brazil)

more..

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; CLAVANIN A; IMMUNOLOGIC FACTOR; PEPTIDE; PLASMA PROTEIN;

ANIMAL; BACTERIAL INFECTION; C57BL MOUSE; CHEMISTRY; DISEASE MODEL; DRUG EFFECTS; FEMALE; HEK293 CELL LINE; HUMAN; IMMUNOMODULATION; INNATE IMMUNITY; MICROBIAL SENSITIVITY TEST; MOUSE; RAW 264.7 CELL LINE;

ANIMALS; ANTI-BACTERIAL AGENTS; BACTERIAL INFECTIONS; BLOOD PROTEINS; DISEASE MODELS, ANIMAL; FEMALE; HEK293 CELLS; HUMANS; IMMUNITY, INNATE; IMMUNOLOGIC FACTORS; IMMUNOMODULATION; MICE; MICE, INBRED C57BL; MICROBIAL SENSITIVITY TESTS; PEPTIDES; RAW 264.7 CELLS;

EID: 84994591102     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep35465     Document Type: Article

References (57)

1. Boucher, H. W., et al. Bad bugs, no drugs: no ESKAPE An update from the Infectious Diseases Society of America. Clin. Infect. Dis. 48, 1-12 (2009
2. London, R. on A. R., & Grande-Bretagne. Antimicrobial Resistance: Tackling a Crisis for the Health and Wealth of Nations. at https://books.google.com.br/books/about/Antimicrobial-Resistance.html?id=poAFrgEACAAJ& pgis=1 (2014
3. Fjell, C. D., Hiss, J. A., Hancock, R. E. W., & Schneider, G. Designing antimicrobial peptides: form follows function. Nat. Rev. Drug Discov. 11, 37-51 (2011
4. Hancock, R. E. W., & Sahl, H.-G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24, 1551-1557 (2006
5. Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 415, 389-395 (2002
6. De La Fuente-Núñez, C., Reffuveille, F., Haney, E. F., Straus, S. K., & Hancock, R. E. W. Broad-spectrum anti-biofilm peptide that targets a cellular stress response. PLoS Pathog. 10, e1004152 (2014
7. Hilchie, A. L., Wuerth, K., & Hancock, R. E. W. Immune modulation by multifaceted cationic host defense (antimicrobial) peptides. Nat. Chem. Biol. 9, 761-768 (2013
8. Galdino, A. S., et al. Biochemical and Structural Characterization of Amy1: An Alpha-Amylase from Cryptococcus flavus Expressed in Saccharomyces cerevisiae. Enzyme Res. 2011, 157294 (2011
9. Lee, I. H., Cho, Y., & Lehrer, R. I. Effects of pH and salinity on the antimicrobial properties of clavanins. Infect. Immun. 65, 2898-2903 (1997
10. Lee, I. H., et al. Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes. FEBS Lett. 400, 158-162 (1997
11. Lehrer, R. I., Lee, I. H., Menzel, L., Waring, A., & Zhao, C. Clavanins and styelins, alpha-helical antimicrobial peptides from the hemocytes of Styela clava. Adv. Exp. Med. Biol. 484, 71-76 (2001
12. Silva, O. N., et al. Clavanin A improves outcome of complications from different bacterial infections. Antimicrob. Agents Chemother. 59, 1620-1626 (2015
13. Saúde, A. C. M., et al. Clavanin bacterial sepsis control using a novel methacrylate nanocarrier. Int. J. Nanomedicine 9, 5055-5069 (2014
14. Silva, O. N., et al. Structural Studies of a Lipid-Binding Peptide from Tunicate Hemocytes with Anti-Biofilm Activity. Sci. Rep. 6, 27128 (2016
15. De La Fuente-Núñez, C., et al. D-enantiomeric peptides that eradicate wild-type and multidrug-resistant biofilms and protect against lethal Pseudomonas aeruginosa infections. Chem. Biol. 22, 196-205 (2015
16. Reffuveille, F., De La Fuente-Núñez, C., Mansour, S., & Hancock, R. E. W. A broad-spectrum antibiofilm peptide enhances antibiotic action against bacterial biofilms. Antimicrob. Agents Chemother. 58, 5363-5371 (2014
17. van Kan, E. J. M., Demel, R. A., van der Bent, A., & De Kruijff, B. The role of the abundant phenylalanines in the mode of action of the antimicrobial peptide clavanin. Biochim. Biophys. Acta 1615, 84-92 (2003
18. Haney, E. F., Mansour, S. C., Hilchie, A. L., De La Fuente-Núñez, C., & Hancock, R. E. W. High throughput screening methods for assessing antibiofilm and immunomodulatory activities of synthetic peptides. Peptides 71, 276-285 (2015
19. Mansour, S. C., De La Fuente-Núñez, C., & Hancock, R. E. W. Peptide IDR-1018: modulating the immune system and targeting bacterial biofilms to treat antibiotic-resistant bacterial infections. J. Pept. Sci. 21, 323-329 (2015
20. Nijnik, A., & Hancock, R. E. W. The roles of cathelicidin LL-37 in immune defences and novel clinical applications. Curr. Opin. Hematol. 16, 41-47 (2009
21. De Yang, et al. LL-37, the neutrophil granule-and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 192, 1069-1074 (2000
22. Nijnik, A., et al. Synthetic cationic peptide IDR-1002 provides protection against bacterial infections through chemokine induction and enhanced leukocyte recruitment. J. Immunol. 184, 2539-2550 (2010
23. Prins, J. M., Kuijper, E. J., Mevissen, M. L., Speelman, P., & van Deventer, S. J. Release of tumor necrosis factor alpha and interleukin 6 during antibiotic killing of Escherichia coli in whole blood: influence of antibiotic class, antibiotic concentration, and presence of septic serum. Infect. Immun. 63, 2236-2242 (1995
24. Bishop, R. E., Penfold, S. S., Frost, L. S., Höltje, J. V., & Weiner, J. H. Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins. J. Biol. Chem. 270, 23097-23103 (1995
25. Peitsch, M. C., & Boguski, M. S. Is apolipoprotein D a mammalian bilin-binding protein? New Biol. 2, 197-206 (1990
26. Huber, R., et al. Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 A resolution. J. Mol. Biol. 198, 499-513 (1987
27. Jiang, Z., et al. Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alphahelical cationic antimicrobial peptides. Biopolymers 90, 369-383 (2008
28. Mahalka, A. K., & Kinnunen, P. K. J. Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L. Biochim. Biophys. Acta 1788, 1600-1609 (2009
29. Zhu, X., et al. Design of imperfectly amphipathic a -helical antimicrobial peptides with enhanced cell selectivity. Acta Biomater. 10, 244-257 (2014
30. Turner-Brannen, E., et al. Modulation of interleukin-1β -induced inflammatory responses by a synthetic cationic innate defence regulator peptide, IDR-1002, in synovial fibroblasts. Arthritis Res. Ther. 13, R129 (2011
31. Soehnlein, O., et al. Neutrophil secretion products pave the way for inflammatory monocytes. Blood 112, 1461-1471 (2008
32. Mookherjee, N., et al. Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37. J. Immunol. 176, 2455-2464 (2006
33. Niyonsaba, F., et al. A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis. Immunology 106, 20-26 (2002
34. Maggiora, L. L., Smith, C. W., & Zhang, Z. Y. A general method for the preparation of internally quenched fluorogenic protease substrates using solid-phase peptide synthesis. J. Med. Chem. 35, 3727-3730 (1992
35. Mandal, S. M., et al. Controlling resistant bacteria with a novel class of β -lactamase inhibitor peptides: from rational design to in vivo analyses. Sci. Rep. 4, 6015 (2014
36. Kokai-Kun, J. F., Chanturiya, T., & Mond, J. J. Lysostaphin as a treatment for systemic Staphylococcus aureus infection in a mouse model. J. Antimicrob. Chemother. 60, 1051-1059 (2007
37. Wiegand, I., Hilpert, K., & Hancock, R. E. W. Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances. Nat. Protoc. 3, 163-175 (2008
38. De Almeida, K. C., et al. Investigating specific bacterial resistance to AMPs by using a magainin I-resistant Escherichia coli model. J. Antibiot. (Tokyo). 67, 681-687 (2014
39. Dathe, M., et al. Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35, 12612-12622 (1996
40. Lima, T. B., et al. A Kunitz proteinase inhibitor from corms of Xanthosoma blandum with bactericidal activity. J. Nat. Prod. 74, 969-975 (2011
41. Silva, O. N., et al. Cn-AMP1: a new promiscuous peptide with potential for microbial infections treatment. Biopolymers 98, 322-331 (2012
42. Malik, U., et al. In vivo efficacy of anuran trypsin inhibitory peptides against staphylococcal skin infection and the impact of peptide cyclization. Antimicrob. Agents Chemother. 59, 2113-2121 (2015
43. Qiu, X., et al. [A case-control study on the risk factor of perinatals? congenital malformations in seven cities of Guangxi]. Zhonghua Liu Xing Bing Xue Za Zhi 24, 512-515 (2003
44. Pini, A., et al. A novel tetrabranched antimicrobial peptide that neutralizes bacterial lipopolysaccharide and prevents septic shock in vivo. FASEB J. 24, 1015-1022 (2010
45. Ray, A., & Dittel, B. N. Isolation of mouse peritoneal cavity cells. J. Vis. Exp. e1488 (2010). doi: 10.3791/1488
46. Moreno, S. E., et al. IL-12, but Not IL-18, Is Critical to Neutrophil Activation and Resistance to Polymicrobial Sepsis Induced by Cecal Ligation and Puncture. J. Immunol. 177, 3218-3224 (2006
47. Xu, D., & Zhang, Y. Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field. Proteins 80, 1715-1735 (2012
48. Eswar, N., et al. Comparative protein structure modeling using MODELLER. Curr. Protoc. Protein Sci. Chapter 2, Unit 2.9 (2007
49. Wiederstein, M., & Sippl, M. J. ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res. 35, W407-W410 (2007
50. Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993
51. Wu, E. L., et al. CHARMM-GUI Membrane Builder toward realistic biological membrane simulations. J. Comput. Chem. 35, 1997-2004 (2014
52. Berger, O., Edholm, O., & Jähnig, F. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys. J. 72, 2002-2013 (1997
53. Hess, B., Kutzner, C., van der Spoel, D., & Lindahl, E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J. Chem. Theory Comput. 4, 435-447 (2008
54. Miyamoto, S., & Kollman, P. A. Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models. J. Comput. Chem. 13, 952-962 (1992
55. Hess, B., Bekker, H., Berendsen, H. J. C., & Fraaije, J. G. E. M. LINCS: A linear constraint solver for molecular simulations. J. Comput. Chem. 18, 1463-1472 (1997
56. Darden, T., York, D., & Pedersen, L. Particle mesh Ewald: An N log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089 (1993
57. Van Gunsteren, W. F., & Berendsen, H. J. C. A Leap-frog Algorithm for Stochastic Dynamics. Mol. Simul. 1, 173-185 (1988