Induced bacterial cross-resistance toward host antimicrobial peptides: A worrying phenomenon

Frontiers in Microbiology

Volumn 7, Issue MAR, 2016, Pages

  Fleitas, Osmel ^a,b   Franco, Octávio L ^a,b,c  

^a UNIVERSITY OF BRASILIA   (Brazil)

^b UNIVERSIDADE CATÓLICA DE BRASÍLIA   (Brazil)

^c UNIVERSIDADE CATÓLICA DOM BOSCO   (Brazil)

Author keywords

Antibiotics; Antimicrobial peptides; Bacterial infection; Cross resistance

Indexed keywords

AMPICILLIN; BETA LACTAM; COLISTIN; DEFENSIN; PEXIGANAN; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; VANCOMYCIN;

ACINETOBACTER BAUMANNII; ANTIBIOTIC RESISTANCE; ENTEROBACTER CLOACAE; INNATE IMMUNITY; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; MINIMUM INHIBITORY CONCENTRATION; SALMONELLA ENTERICA SEROVAR TYPHIMURIUM; SHORT SURVEY; SINGLE NUCLEOTIDE POLYMORPHISM; STAPHYLOCOCCUS AUREUS; VIBRIO CHOLERAE;

EID: 84964397435     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2016.00381     Document Type: Short Survey

References (28)

1. Bayer, A. S., Mishra, N. N., Chen, L., Kreiswirth, B. N., Rubio, A., and Yang, J. S. (2015). Frequency and distribution of single-nucleotide polymorphisms within mprf in methicillin-resistant Staphylococcus aureus clinical isolates: role in cross-resistance between daptomycin and host defense antimicrobial peptides. Antimicrob. Agents Chemother. 59, 4930-4937. doi: 10.1128/AAC.00970-15
2. Bayer, A. S., Mishra, N. N., Sakoulas, G., Nonejuie, P., Nast, C. C., and Pogliano, J. (2014). Heterogeneity of mprF sequences in methicillin-resistant Staphylococcus aureus clinical isolates: role in cross-resistance between daptomycin and host defense antimicrobial peptides. Antimicrob. Agents Chemother. 58, 7462-7467. doi: 10.1128/AAC.03422-14
3. Bell, G., and Gouyon, P. H. (2003). Arming the enemy: the evolution of resistance to self-proteins. Microbiology 149, 1367-1375. doi: 10.1099/mic.0.26265-0
4. Chen, H. D., and Groisman, E. A. (2013). The biology of the PmrA/PmrB two component system: the major regulator of lipopolysaccharide modifications. Annu. Rev. Microbiol. 67, 83-112. doi: 10.1146/annurev-micro-092412-155751
5. Chernysh, S., Gordya, N., and Suborova, T. (2015). Insect antimicrobial peptide complexes prevent resistance development in bacteria. PLoS ONE 10:e0130788. doi: 10.1371/journal.pone.0130788
6. Dobson, A. J., Purves, J., Kamysz, W., and Rolff, J. (2013). Comparing selection on S. aureus between antimicrobial peptides and common antibiotics. PLoS ONE 8:e76521. doi: 10.1371/journal.pone.0076521
7. Dobson, A. J., Purves, J., and Rolff, J. (2014). Increased survival of experimentally evolved antimicrobial peptide-resistant Staphylococcus aureus in an animal host. Evol. Appl. 7, 905-912. doi: 10.1111/eva.12184
8. Duperthuy, M., Sjöström, A. E., Sabharwal, D., Damghani, F., Uhlin, B. E., and Wai, S. N. (2014). Role of the Vibrio cholerae matrix protein Bap 1 in cross-resistance to antimicrobial peptides. PLoS Pathog. 9:e1003620. doi: 10.1371/journal.ppat.1003620
9. Ernst, C. M., and Peschel, A. (2011). Broad-spectrum antimicrobial peptide resistance by MprF-mediated aminoacylation and flipping of phospholipids. Mol. Microbiol. 80, 290-299. doi: 10.1111/j.1365-2958.2011.07576.x
10. Guilhelmelli, F., Vilela, N., Albuquerque, P., Derengowski Lda, S., Silva-Pereira, I., and Kway, C. M. (2013). Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance. Front. Microbiol. 4:353. doi: 10.3389/fmicb.2013.00353
11. Habets, M. G., and Brockhurst, M. A. (2012). Therapeutic antimicrobial peptides may compromise natural immunity. Biol. Lett. 8, 416-418. doi: 10.1098/rsbl.2011.1203
12. Hindler, A. J., Wong-Beringer, A., Charlton, C. L., Miller, S. A, Kelesidis, T., Carvalho, M. et al. (2015). In vitro activity of daptomycin in combination with ß-lactams, gentamicin, rifampin, and tigecycline against daptomycin-nonsusceptible enterococci. Antimicrob. Agents Chemother. 59, 4279-4288. doi: 10.1128/AAC.05077-14
13. Jenssen, H., Hamill, P., and Hancock, R. E. (2006). Peptide antimicrobial agents. Clin. Microbiol. Rev. 19, 491-511. doi: 10.1128/CMR.00056-05
14. Lofton, H., Anwar, N., Rhen, M., and Andersson, D. I. (2015). Fitness of Salmonella mutants resistant to antimicrobial peptides. J. Antimicrob Chemother. 70, 432-440. doi: 10.1093/jac/dku423
15. Lofton, H., Pränting, M., Thulin, E., and Andersson, D. I. (2013). Mechanisms and fitness costs of resistance to antimicrobial peptides LL-37, CNY-100HL and wheat germ histones. PLoS ONE 8:e68875. doi: 10.1371/journal.pone.0068875
16. Manning, A. J., and Kuehn, M. J. (2011). Contribution of bacterial outer membrane vesicles to innate bacterial defense. BMC Microbiol. 11:258. doi: 10.1186/1471-2180-11-258
17. Maria-Neto, S., de Almeida, K. C., Macedo, M. L., and Franco, O. L. (2015). Understanding bacterial resistance to antimicrobial peptides: from the surface to deep inside. Biochim. Biophys. Acta. 1848, 3078-3088. doi: 10.1016/j.bbamem.2015.02.017
18. Mishra, N. N., Bayer, A. S., Moise, P. A., Yeaman, M. R., and Sakoulas, G. (2012). Reduced susceptibility to host-defense cationics peptides and daptomycin coemerge in methicillin-resistant Staphylococcus aureus from daptomycin-naïve bacteremic patients. J. Infect. Dis. 206, 1160-1167. doi: 10.1093/infdis/jis482
19. Mishra, N. N., Bayer, A. S., Weidenmaier, C., Grau, T., Wanner, S., Stefani, S., et al. (2014). Phenotypic and genotypic characterization of daptomycin-resistant methicillin-resistant Staphylococcus aureus strains: relative roles of mprF and dlt operons. PLoS ONE 9:e107426. doi: 10.1371/journal.pone.0107426
20. Mishra, N. N., Yang, S. J., Chen, L., Muller, C., Saleh-Mghir, A., Kuhn, S., et al. (2013). Emergence of daptomycin resistance in daptomycin-naïve rabbits with methicillin-resistant Staphylococcus aureus prosthetic joint infection is associated with resistance to host defense cationic peptides and mrpF polymorphisms. PLoS ONE 8:e71151. doi: 10.1371/journal.pone.0071151
21. Napier, B. A., Band, V., Burd, E. M., and Weiss, D. S. (2014). Colistin heteroresistance in Enterobacter cloacae is associated with cross-resistance to the host antimicrobial lysozyme. Antimicrob. Agents Chemother. 58, 5594-5597. doi: 10.1128/AAC.02432-14
22. Napier, B. A., Burd, E. M., Satola, S. W., Cagle, S. M., Ray, S. M., McGann, P., et al. (2013). Clinical use of colistin induces cross-resistance to host antimicrobials in Acinetobacter baumannii. MBio 4:e00021-00013. doi: 10.1128/mBio.00021-13
23. Narayanan, S., Modak, J. K., Ryan, C. S., Garcia-Bustos, J., Davies, J. K., and Roujeinikova, A. (2014). Mechanism of Escherichia coli resistance to Pyrrhocoricin. Antimicrob. Agents Chemother. 58, 2754-2762. doi: 10.1128/AAC.02565-13
24. Pränting, M., Negrea, A., Rhen, M., and Andersson, D. I. (2008). Mechanism and fitness costs of PR-39 resistance in Salmonella enterica serovar Typhimurium LT2. Antimicrob. Agents Chemother. 52, 2734-2741. doi: 10.1128/AAC.00205-08
25. Saga, T., and Yamaguchi, K. (2009). History of antimicrobial agents and resistant bacteria. JMAJ 52, 103-108.
26. Sakoulas, G., Bayer, A. S., Pogliano, J., Tsuji, B. T., Yang, S. J., Mishra, N. N., et al. (2012). Ampicillin enhances daptomycin-and cationic host defense peptide-mediated killing of ampicillin-and vancomycin-resistant Enterococcus faecium. Antimicrob. Agents Chemother. 56, 838-844. doi: 10.1128/AAC.05551-11
27. Saleh-Mghir, A., Muller-Serieys, C., Dinh, A., Massias, L., and Crémieux, A. C. (2011). Adjunctive rifampim is crucial to optimizing daptomycin efficacy against rabbit prosthetic joint infection due to methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 55, 4589-4593. doi: 10.1128/AAC.00675-11
28. Zasloff, M. (2002). Antimicrobial peptides of multicellular organisms. Nature 415, 389-395. doi: 10.1038/415389a