Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds

ACS Chemical Biology

Volumn 9, Issue 9, 2014, Pages 1997-2002

  Wang, Guangshun ^a   Hanke, Mark L ^a   Mishra, Biswajit ^a   Lushnikova, Tamara ^a   Heim, Cortney E ^a   Thomas, Vinai Chittezham ^a   Bayles, Kenneth W ^a   Kielian, Tammy ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

17BIPHE PEPTIDE; 17BIPHE2 PEPTIDE; 17F NAPH PEPTIDE; 17F2 PEPTIDE; 17MF F PEPTIDE; 17MF NAPH PEPTIDE; 17NAPH MF PEPTIDE; BACTERIAL DNA; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; CAP18 LIPOPOLYSACCHARIDE-BINDING PROTEIN;

ACINETOBACTER BAUMANNII; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIBACTERIAL ACTIVITY; ARTICLE; BACTERIAL MEMBRANE; BIOFILM; CATHETER INFECTION; CONTROLLED STUDY; DRUG CYTOTOXICITY; DRUG DNA BINDING; DRUG EFFICACY; DRUG POTENCY; DRUG SCREENING; DRUG SELECTIVITY; DRUG STABILITY; DRUG STRUCTURE; ENTEROBACTER; ENTEROCOCCUS FAECIUM; ESCHERICHIA COLI; HUMAN; HUMAN CELL; HYDROPHOBICITY; IN VITRO STUDY; IN VIVO STUDY; KLEBSIELLA PNEUMONIAE; MALE; MEMBRANE DAMAGE; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; MINIMUM INHIBITORY CONCENTRATION; MOUSE; NONHUMAN; PEPTIDE LIBRARY; PSEUDOMONAS AERUGINOSA; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS INFECTION; AMINO ACID SEQUENCE; ANIMAL; C57BL MOUSE; CATHETER-RELATED INFECTIONS; CHEMICAL PHENOMENA; CHEMISTRY; DISEASE MODEL; DRUG DESIGN; DRUG EFFECTS; MICROBIAL SENSITIVITY TEST; MICROBIOLOGY; MOLECULAR GENETICS; PATHOGENICITY; STAPHYLOCOCCAL INFECTIONS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; CATHETER-RELATED INFECTIONS; DISEASE MODELS, ANIMAL; DRUG DESIGN; ENTEROCOCCUS FAECIUM; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MALE; METHICILLIN-RESISTANT STAPHYLOCOCCUS AUREUS; MICE, INBRED C57BL; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PSEUDOMONAS AERUGINOSA; STAPHYLOCOCCAL INFECTIONS; STAPHYLOCOCCUS AUREUS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84912095002     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500475y     Document Type: Article

References (29)

1. Boucher, H. W., Talbot, G. H., Bradley, J. S., Edwards, J. E., Gilbert, D., Rice, L. B., Scheld, M., Spellberg, B., and Bartlett, J. (2009) Bad bugs, no drugs: no ESKAPE! An update from the Infectious Diseases Society of America. Clin. Infect. Dis. 48, 1-12.
2. Klevens, R. M., Morrison, M. A., Nadle, J., Petit, S., Gershman, K., Ray, S., Harrison, L. H., Lynfield, R., Dumyati, G., Townes, J. M., Craig, A. S., Zell, E. R., Fosheim, G. E., McDougal, L. K., Carey, R. B., and Fridkin, S. K. (2007) Invasive methicillin-resistant Staphylococcus aureus infections in the United States. J. Am. Med. Assoc. 298, 1763-1771.
3. Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature 415, 389-395.
4. Lai, Y., and Gallo, R. L. (2009) AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 30, 131-141.
5. Hancock, R. E., and Sahl, H. G. (2013) New strategies and compounds for anti-infective treatment. Curr. Opin. Microbiol. 16, 519-521.
6. van der Does, A. M., Bergman, P., Agerberth, B., and Lindbom, L. (2012) Induction of the human cathelicidin LL-37 as a novel treatment against bacterial infections. J. Leukocyte Biol. 92, 735-742.
7. Putsep, K., Carsson, G., Boman, H. G., and Andersson, M. (2002) Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 360, 1144-1149.
8. Chromek, M., Slamová, Z., Bergman, P., Kovács, L., Podracká, L., Ehrén, I., Hökfelt, T., Gudmundsson, G. H., Gallo, R. L., Agerberth, B., and Brauner, A. (2006) The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection. Nat. Med. 12, 636-641.
9. Nakatsuj, T., and Gallo, R. L. (2012) Antimicrobial peptides: old molecules with new ideas. J. Invest. Dermatol. 132, 887-895.
10. Wang, G. (2008) Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J. Biol. Chem. 283, 32637-32643.
11. Oren, Z., Lerman, J. C., Gudmundsson, G. H., Agerberth, B., and Shai, Y. (1999) Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 341 (Pt 3), 501-513.
12. Wang, G., Mishra, B., Epand, R. F., and Epand, R. M. (2014) High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments. Biochim. Biophys. Acta 1838, 2160-2172.
13. Braff, M. H., Hawkins, M. A., Di Nardo, A., Lopez-Garcia, B., Howell, M. D., Wong, C., Lin, K., Streib, J. E., Dorschner, R., Leung, D. Y., and Gallo, R. L. (2005) Structure-function relationships among human cathelicidin peptides: dissociation of antimicrobial properties from host immunostimulatory activities. J. Immunol. 174, 4271-4278.
14. Nagaoka, I., Kuwahara-Arai, K., Tamura, H., Hiramatsu, K., and Hirata, M. (2005) Augmentation of the bactericidal activities of human cathelicidin CAP18/LL-37-derived antimicrobial peptides by amino acid substitutions. Infammation. Res. 54, 66-73.
15. Li, X., Li, Y., Han, H., Miller, D. W., and Wang, G. (2006) Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. J. Am. Chem. Soc. 128, 5776-5785.
16. Papo, N., and Shai, Y. (2003) New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells. Biochemistry 42, 9346-9354.
17. Epand, R. F., Wang, G., Berno, B., and Epand, R. M. (2009) Lipid segregation explains selective toxicity of a series of fragments derived from the human cathelicidin LL-37. Antimicrob. Agents Chemother. 53, 3705-3714.
18. Wang, G., Epand, R. F., Mishra, B., Lushnikova, T., Thomas, V. C., Bayles, K. W., and Epand, R. M. (2012) Decoding the functional roles of cationic side chains of the major antimicrobial region of human cathelicidin LL-37. Antimicrob. Agents Chemother. 56, 845-856.
19. Mishra, B., and Wang, G. (2012) Ab initio design of potent anti-MRSA peptides based on database filtering technology. J. Am. Chem. Soc. 134, 12426-12429.
20. Park, C. B., Kim, H. S., and Kim, S. C. (1998) Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 244, 253-257.
21. Menousek, J., Mishra, B., Hanke, M. L., Heim, C. E., Kielian, T., and Wang, G. (2012) Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300. Int. J. Antimicrob. Agents 39, 402-406.
22. Cassat, J. E., Lee, C. Y., and Smeltzer, M. S. (2007) formation in clinical isolates of Staphylococcus aureus. Methods Mol. Biol. 391, 127-144.
23. Heim, C. E., Hanke, M. L., and Kielian, T. (2014) A mouse model of Staphylococcus catheter-associated biofilm infection. Methods Mol. Biol. 1106, 183-191.
24. Thurlow, L. R., Hanke, M. L., Fritz, T., Angle, A., Aldrich, A., Williams, S. H., Engebretsen, I. L., Bayles, K. W., Horswill, A. R., and Kielian, T. (2011) Staphylococcus aureus biofilms prevent macrophage phagocytosis and attenuate inflammation in vivo. J. Immunol. 186, 6585-6596.
25. Wang, G., Elliott, M., Cogen, A. L., Ezell, E. L., Gallo, R. L., and Hancock, R. E. W. (2012) Structure, dynamics, and antimicrobial and immune modulatory activities of human LL-23 and its single-residue variants mutated on the basis of homologous primate cathelicidins. Biochemistry 51, 653-664.
26. Yung, S. C., Parenti, D., and Murphy, P. M. (2011) Host chemokines bind to Staphylococcus aureus and stimulate protein A release. J. Biol. Chem. 286, 5069-5077.
27. Yang, D., Chen, Q., Hoover, D. M., Staley, P., Tucker, K. D., Lubkowski, J., and Oppenheim, J. J. (2003) Many chemokines including CCL20/MIP-3alpha display antimicrobial activity. J. Leukocyte Biol. 74, 448-455.
28. Darouiche, R. O. (2004) Treatment of infections associated with surgical implants. N. Engl. J. Med. 350, 1422-1429.
29. Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55.