Polimiksinlere ve Fosfomisine Direnç Mekanizmaları

AINSWORTH GC, BROWN AM, BROWNLEE G. (1947). Aerosporin, an antibiotic produced by Bacillus aerosporus Greer. Nature, 159(4060), 263. https://doi.org/10.1038/160263a0

BENEDICT RG & LANGLYKKE AF. (1947). Antibiotic activity of Bacillus polymyxa. Journal of bacteriology, 54(1), 24.

STANSLY PG, SHEPHERD RG & WHITE HJ. (1947). Polymyxin: a new chemotherapeutic agent. Bulletin of the Johns Hopkins Hospital, 81(1), 43–54.

WILKINSON S. (1963). Identity of colistin and polymyxin E. Lancet (London, England), 1(7287), 922–923. https://doi.org/10.1016/s0140-6736(63)91694-5

Wolinsky E, Hines JD. (1962). Neurotoxic and nephrotoxic effects of colistin in patients with renal disease. The New England journal of medicine, 266, 759–762. https://doi.org/10.1056/NEJM196204122661505

Falagas ME, Rafailidis PI, Matthaiou DK. (2010). Resistance to polymyxins: Mechanisms, frequency and treatment options. Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy, 13(4-5), 132–138.

Olaitan AO, Morand S, Rolain JM. (2014). Mechanisms of polymyxin resistance: acquired and intrinsic resistance in bacteria. Frontiers in microbiology, 5, 643. https://doi.org/10.3389/fmicb.2014.00643

Nikaido H. (2003). Molecular basis of bacterial outer membrane permeability revisited. Microbiology and molecular biology reviews : MMBR, 67(4), 593–656. https://doi.org/10.1128/MMBR.67.4.593-656.2003

Raetz CR & Whitfield C. (2002). Lipopolysaccharide endotoxins. Annual review of biochemistry, 71, 635–700. https://doi.org/10.1146/annurev.biochem.71.110601.135414

Koebnik R, Locher KP & Van Gelder P. (2000). Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Molecular microbiology, 37(2), 239–253. https://doi.org/10.1046/j.1365-2958.2000.01983.x

Deris ZZ, Akter J, Sivanesan S et al. (2014). A secondary mode of action of polymyxins against Gram-negative bacteria involves the inhibition of NADH-quinone oxidoreductase activity. The Journal of antibiotics, 67(2), 147–151. .

Deris ZZ, Swarbrick JD, Roberts KD, et al. (2014). Probing the penetration of antimicrobial polymyxin lipopeptides into gram-negative bacteria. Bioconjugate chemistry, 25(4), 750–760. . https://doi.org/10.1021/bc500094d

Lerner S. A, Ouellette M, Sobel, J. D. (2017). Antimicrobial drug resistance; Mechanisms of Drug Resistance, Volume 1( pp. 333-336) D. L. Mayers (Ed.). New York: Humana press.

Chen HD & Groisman EA. (2013). The biology of the PmrA/PmrB two-component system: the major regulator of lipopolysaccharide modifications. Annual review of microbiology, 67, 83–112. https://doi.org/10.1146/annurev-micro-092412-155751

Gunn JS, Ernst RK, McCoy AJ, et al. (2000). Constitutive mutations of the Salmonella enterica serovar Typhimurium transcriptional virulence regulator phoP. Infection and immunity, 68(6), 3758–3762. https://doi.org/10.1128/IAI.68.6.3758-3762.2000

Gunn JS, Ryan SS, Van Velkinburgh JC, et al. (2000). Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium. Infection and immunity, 68(11), 6139–6146. https://doi.org/10.1128/IAI.68.11.6139-6146.2000

Kox LF, Wösten MM & Groisman EA. (2000). A small protein that mediates the activation of a two-component system by another two-component system. The EMBO journal, 19(8), 1861–1872. https://doi.org/10.1093/emboj/19.8.1861

Bader MW, Sanowar S, Daley ME, et al. (2005). Recognition of antimicrobial peptides by a bacterial sensor kinase. Cell, 122(3), 461–472. https://doi.org/10.1016/j.cell.2005.05.030

Johnson L, Horsman SR, Charron-Mazenod L, et al. (2013). Extracellular DNA-induced antimicrobial peptide resistance in Salmonella enterica serovar Typhimurium. BMC microbiology, 13, 115. https://doi.org/10.1186/1471-2180-13-115

Fernández L, Gooderham WJ, Bains M, et al. Adaptive resistance to the "last hope" antibiotics polymyxin B and colistin in Pseudomonas aeruginosa is mediated by the novel two-component regulatory system ParR-ParS. Antimicrobial agents and chemotherapy, 54(8), 3372–3382. https://doi.org/10.1128/AAC.00242-10

Fernández L, Jenssen H, Bains M, et al. (2012). The two-component system CprRS senses cationic peptides and triggers adaptive resistance in Pseudomonas aeruginosa independently of ParRS. Antimicrobial agents and chemotherapy, 56(12), 6212–6222

https://doi.org/10.1128/AAC.01530-12

Moskowitz SM, Ernst RK & Miller SI. (2004). PmrAB, a two-component regulatory system of Pseudomonas aeruginosa that modulates resistance to cationic antimicrobial peptides and addition of aminoarabinose to lipid A. Journal of bacteriology, 186(2), 575–579.

https://doi.org/10.1128/JB.186.2.575-579.2004

Muller C, Plésiat P, Jeannot K. (2011). A two-component regulatory system interconnects resistance to polymyxins, aminoglycosides, fluoroquinolones, and β-lactams in Pseudomonas aeruginosa. Antimicrobial agents and chemotherapy, 55(3), 1211–1221. https://doi.org/10.1128/AAC.01252-10

Macfarlane EL, Kwasnicka A, Ochs MM, et al. (1999). PhoP-PhoQ homologues in Pseudomonas aeruginosa regulate expression of the outer-membrane protein OprH and polymyxin B resistance. Molecular microbiology, 34(2), 305–316.

https://doi.org/10.1046/j.1365-2958.1999.01600.x

Poirel L, Jayol A, Bontron S, et al. (2015). The mgrB gene as a key target for acquired resistance to colistin in Klebsiella pneumoniae. The Journal of antimicrobial chemotherapy, 70(1), 75–80. https://doi.org/10.1093/jac/dku323

Lee H, Hsu FF, Turk J, et al. (2004). The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica. Journal of bacteriology, 186(13), 4124–4133. https://doi.org/10.1128/JB.186.13.4124-4133.2004

Kato A, Chen HD, Latifi T, et al. (2012). Reciprocal control between a bacterium's regulatory system and the modification status of its lipopolysaccharide. Molecular cell, 47(6), 897–908. https://doi.org/10.1016/j.molcel.2012.07.017

Veldman K, van Essen-Zandbergen A, Rapallini M, et al. (2016). Location of colistin resistance gene mcr-1 in Enterobacteriaceae from livestock and meat. The Journal of antimicrobial chemotherapy, 71(8), 2340–2342. https://doi.org/10.1093/jac/dkw181

Liu YY, Wang Y, Walsh TR, et al. (2016). Emergence of plasmid-mediated colistin resistance mechanism MCR-1 in animals and human beings in China: a microbiological and molecular biological study. The Lancet. Infectious diseases, 16(2), 161–168. https://doi.org/10.1016/S1473-3099(15)00424-7

Rhouma M, Beaudry F & Letellier A. (2016). Resistance to colistin: what is the fate for this antibiotic in pig production? . International journal of antimicrobial agents, 48(2), 119–126. https://doi.org/10.1016/j.ijantimicag.2016.04.008

Schwarz S & Johnson AP. (2016). Transferable resistance to colistin: a new but old threat. The Journal of antimicrobial chemotherapy, 71(8), 2066–2070. https://doi.org/10.1093/jac/dkw274

Skov RL & Monnet DL. (2016). Plasmid-mediated colistin resistance (mcr-1 gene): three months later, the story unfolds. Euro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin, 21(9), 30155. https://doi.org/10.2807/1560-7917.ES.2016.21.9.30155

Giamarellou H. (2016). Epidemiology of infections caused by polymyxin-resistant pathogens. International journal of antimicrobial agents, 48(6), 614–621. https://doi.org/10.1016/j.ijantimicag.2016.09.025

Xavier BB, Lammens C, Ruhal R, et al. (2016). Identification of a novel plasmid-mediated colistin-resistance gene, mcr-2, in Escherichia coli, Belgium, June 2016. Euro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin, 21(27), 10.2807/1560-7917.ES.2016.21.27.30280. https://doi.org/10.2807/1560-7917.ES.2016.21.27.30280

Yang YQ, Li YX, Lei CW, et al. (2018). Novel plasmid-mediated colistin resistance gene mcr-7.1 in Klebsiella pneumoniae. The Journal of antimicrobial chemotherapy, 73(7), 1791–1795. https://doi.org/10.1093/jac/dky111

Carroll LM, Gaballa A, Guldimann C, et al. (2019). Identification of Novel Mobilized Colistin Resistance Gene mcr-9 in a Multidrug-Resistant, Colistin-Susceptible Salmonella enterica Serotype Typhimurium Isolate. mBio, 10(3), e00853-19. https://doi.org/10.1128/mBio.00853-19

Moffatt JH, Harper M, Harrison P, et al. (2010). Colistin resistance in Acinetobacter baumannii is mediated by complete loss of lipopolysaccharide production. Antimicrobial agents and chemotherapy, 54(12), 4971–4977. https://doi.org/10.1128/AAC.00834-10

Moffatt JH, Harper M, Adler B, et al. (2011). Insertion sequence ISAba11 is involved in colistin resistance and loss of lipopolysaccharide in Acinetobacter baumannii. Antimicrobial agents and chemotherapy, 55(6), 3022–3024. https://doi.org/10.1128/AAC.01732-10

García-Quintanilla M, Pulido MR, Moreno-Martínez P, et al. (2014). Activity of host antimicrobials against multidrug-resistant Acinetobacter baumannii acquiring colistin resistance through loss of lipopolysaccharide. Antimicrobial agents and chemotherapy, 58(5), 2972–2975. https://doi.org/10.1128/AAC.02642-13

Srinivasan VB, Singh BB, Priyadarshi N, et al. (2014). Role of novel multidrug efflux pump involved in drug resistance in Klebsiella pneumoniae. PloS one, 9(5), e96288. https://doi.org/10.1371/journal.pone.0096288

Tzeng YL, Ambrose KD, Zughaier S, et al. (2005). Cationic antimicrobial peptide resistance in Neisseria meningitidis. Journal of bacteriology, 187(15), 5387–5396. . https://doi.org/10.1128/JB.187.15.5387-5396.2005

Mathur J & Waldor MK. (2004). The Vibrio cholerae ToxR-regulated porin OmpU confers resistance to antimicrobial peptides. Infection and immunity, 72(6), 3577–3583. https://doi.org/10.1128/IAI.72.6.3577-3583.2004

Mathur J, Davis BM, & Waldor MK. (2007). Antimicrobial peptides activate the Vibrio cholerae sigmaE regulon through an OmpU-dependent signalling pathway. Molecular microbiology, 63(3), 848–858. https://doi.org/10.1111/j.1365-2958.2006.05544.x

Bengoechea JA & Skurnik M. (2000). Temperature-regulated efflux pump/potassium antiporter system mediates resistance to cationic antimicrobial peptides in Yersinia. Molecular microbiology, 37(1), 67–80. https://doi.org/10.1046/j.1365-2958.2000.01956.x

Campos MA, Vargas MA, Regueiro V, et al. (2004). Capsule polysaccharide mediates bacterial resistance to antimicrobial peptides. Infection and immunity, 72(12), 7107–7114. https://doi.org/10.1046/j.1365-2958.2000.01956.x

Llobet E, Tomás JM & Bengoechea JA. (2008). Capsule polysaccharide is a bacterial decoy for antimicrobial peptides. Microbiology (Reading, England), 154(Pt 12), 3877–3886. https://doi.org/10.1099/mic.0.2008/022301-0

Muyembe T, Vandepitte J & Desmyter J. (1973). Natural colistin resistance in Edwardsiella tarda. Antimicrobial agents and chemotherapy, 4(5), 521–524. . https://doi.org/10.1128/AAC.4.5.521

Rózalski A, Sidorczyk Z & Kotełko K. (1997). Potential virulence factors of Proteus bacilli. Microbiology and molecular biology reviews: MMBR, 61(1), 65–89. https://doi.org/10.1128/mmbr.61.1.65-89.1997

Loutet SA & Valvano MA. (2011). Extreme antimicrobial peptide and polymyxin B resistance in the genus Burkholderia. Frontiers in cellular and infection microbiology, 1, 6. https://doi.org/10.3389/fcimb.2011.00006

Biswas S, Brunel JM, Dubus JC, et al. (2012). Colistin: an update on the antibiotic of the 21st century. Expert review of anti-infective therapy, 10(8), 917–934. https://doi.org/10.1586/eri.12.78

Samonis G, Korbila IP, Maraki S, et al. (2014). Trends of isolation of intrinsically resistant to colistin Enterobacteriaceae and association with colistin use in a tertiary hospital. European journal of clinical microbiology & infectious diseases: official publication of the European Society of Clinical Microbiology, 33(9), 1505–1510. https://doi.org/10.1007/s10096-014-2097-8

Basu S, Radziejewska-Lebrecht J & Mayer H. (1986). Lipopolysaccharide of Providencia rettgeri. Chemical studies and taxonomical implications. Archives of microbiology, 144(3), 213–218.

https://doi.org/10.1007/BF00410949

Boll M, Radziejewska-Lebrecht J, Warth C, et al. (1994). 4-Amino-4-deoxy-L-arabinose in LPS of enterobacterial R-mutants and its possible role for their polymyxin reactivity. FEMS immunology and medical microbiology, 8(4), 329–341. https://doi.org/10.1111/j.1574-695X.1994.tb00460.x

Vinogradov E, Lindner B, Seltmann G, et al. (2006). Lipopolysaccharides from Serratia marcescens possess one or two 4-amino-4-deoxy-L-arabinopyranose 1-phosphate residues in the lipid A and D-glycero-D-talo-oct-2-ulopyranosonic acid in the inner core region. Chemistry (Weinheim an der Bergstrasse, Germany), 12(25), 6692–6700. https://doi.org/10.1002/chem.200600186

Sidorczyk Z, Zähringer U & Rietschel ET. (1983). Chemical structure of the lipid A component of the lipopolysaccharide from a Proteus mirabilis Re-mutant. European journal of biochemistry, 137(1-2), 15–22. https://doi.org/10.1111/j.1432-1033.1983.tb07789.x

Kaca W, Radziejewska-Lebrecht J, Bhat UR. (1990). Effect of polymyxins on the lipopolysaccharide-defective mutants of Proteus mirabilis. Microbios, 61(246), 23–32.

McCoy AJ, Liu H, Falla TJ, et al. (2001). Identification of Proteus mirabilis mutants with increased sensitivity to antimicrobial peptides. Antimicrobial agents and chemotherapy, 45(7), 2030–2037. https://doi.org/10.1128/AAC.45.7.2030-2037.2001

Aquilini E, Merino S, Knirel YA, et al. (2014). Functional identification of Proteus mirabilis eptC gene encoding a core lipopolysaccharide phosphoethanolamine transferase. International journal of molecular sciences, 15(4), 6689–6702. https://doi.org/10.3390/ijms15046689

Olaitan AO, Diene SM, Gupta SK, et al. (2014). Genome analysis of NDM-1 producing Morganella morganii clinical isolate. Expert review of anti-infective therapy, 12(10), 1297–1305. https://doi.org/10.1586/14787210.2014.944504

Lin QY, Tsai YL, Liu MC, et al. (2014). Serratia marcescens arn, a PhoP-regulated locus necessary for polymyxin B resistance. Antimicrobial agents and chemotherapy, 58(9), 5181–5190. https://doi.org/10.1128/AAC.00013-14

Isshiki Y, Kawahara K & Zähringer U. (1998). Isolation and characterisation of disodium (4-amino-4-deoxy-beta-L- arabinopyranosyl)-(1-->8)-(D-glycero-alpha-D-talo-oct-2-ulopyranosylona te)- (2-->4)-(methyl 3-deoxy-D-manno-oct-2-ulopyranosid)onate from the lipopolysaccharide of Burkholderia cepacia. Carbohydrate research, 313(1), 21–27. https://doi.org/10.1016/s0008-6215(98)00179-7

Ortega XP, Cardona ST, Brown AR, et al. (2007). A putative gene cluster for aminoarabinose biosynthesis is essential for Burkholderia cenocepacia viability. Journal of bacteriology, 189(9), 3639–3644. . https://doi.org/10.1128/JB.00153-07

European Centre for Disease Prevention and Control. Antimicrobial Resistance Surveillance in Europe 2016; Annual Report of the European Antimicrobial Resistance Surveillance Network (EARS-Net); European Centre for Disease Prevention and Control: Solna, Sweden, 2017.

European Centre for Disease Prevention and Control. Surveillance of antimicrobial resistance in Europe Annual report of the European Antimicrobial Resistance Surveillance Network (EARS-Net) 2017. In ECDC: Surveillance Report; European Centre for Disease Prevention and Control: Solna, Sweden, 2018.

Hendlin D, Stapley EO, Jackson M, et al. (1969). Phosphonomycin, a new antibiotic produced by strains of streptomyces. Science (New York, N.Y.), 166(3901), 122–123. https://doi.org/10.1126/science.166.3901.122

Karageorgopoulos DE, Wang R, Yu XH, et al. (2012). Fosfomycin: evaluation of the published evidence on the emergence of antimicrobial resistance in Gram-negative pathogens. The Journal of antimicrobial chemotherapy, 67(2), 255–268. https://doi.org/10.1093/jac/dkr466

Suárez JE & Mendoza MC. (1991). Plasmid-encoded fosfomycin resistance. Antimicrobial agents and chemotherapy, 35(5), 791–795.

https://doi.org/10.1128/AAC.35.5.791

McCoy AJ, Sandlin RC & Maurelli AT. (2003). In vitro and in vivo functional activity of Chlamydia MurA, a UDP-N-acetylglucosamine enolpyruvyl transferase involved in peptidoglycan synthesis and fosfomycin resistance. Journal of bacteriology, 185(4), 1218–1228. https://doi.org/10.1128/JB.185.4.1218-1228.2003

De Smet KAL, Kempsell KE, Gallagher A, et al. (1999). Alteration of a single amino acid residue reverses fosfomycin resistance of recombinant MurA from Mycobacterium tuberculosis. Microbiology (Reading, England), 145 ( Pt 11), 3177–3184. https://doi.org/10.1099/00221287-145-11-3177

Kumar S, Parvathi A, Hernandez RL, et al. (2009). Identification of a novel UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) from Vibrio fischeri that confers high fosfomycin resistance in Escherichia coli. Archives of microbiology, 191(5), 425–429. https://doi.org/10.1007/s00203-009-0468-9

Gisin J, Schneider A, Nägele B, et al. (2013). A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis. Nature chemical biology, 9(8), 491–493. https://doi.org/10.1038/nchembio.1289

Tsuruoka T, Miyata A, & Yamada Y. (1978). Two kinds of mutants defective in multiple carbohydrate utilization isolated from in vitro fosfomycin-resistant strains of Escherichia coli K--12. The Journal of antibiotics, 31(3), 192–201. . https://doi.org/10.7164/antibiotics.31.192

Takahata S, Ida T, Hiraishi T, et al. (2010). Molecular mechanisms of fosfomycin resistance in clinical isolates of Escherichia coli. International journal of antimicrobial agents, 35(4), 333–337. https://doi.org/10.1016/j.ijantimicag.2009.11.011

Horii T, Kimura T, Sato K, et al. (1999). Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing Escherichia coli O26. Antimicrobial agents and chemotherapy, 43(4), 789–793. https://doi.org/10.1128/AAC.43.4.789

Díez-Aguilar M & Cantón R. (2019). New microbiological aspects of fosfomycin. Revista espanola de quimioterapia : publicacion oficial de la Sociedad Espanola de Quimioterapia, 32 Suppl 1(Suppl 1), 8–18.

Nilsson AI, Berg OG, Aspevall O, et al. (2003). Biological costs and mechanisms of fosfomycin resistance in Escherichia coli. Antimicrobial agents and chemotherapy, 47(9), 2850–2858. https://doi.org/10.1128/AAC.47.9.2850-2858.2003

Venkateswaran PS & Wu HC. (1972). Isolation and characterization of a phosphonomycin-resistant mutant of Escherichia coli K-12. Journal of bacteriology, 110(3), 935–944. https://doi.org/10.1128/jb.110.3.935-944.1972

Woodyer RD, Shao Z, Thomas PM, et al. (2006). Heterologous production of fosfomycin and identification of the minimal biosynthetic gene cluster. Chemistry & biology, 13(11), 1171–1182.

Bernat BA, Laughlin LT & Armstrong RN. (1997). Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases. Biochemistry, 36(11), 3050–3055. https://doi.org/10.1021/bi963172a

Fillgrove KL, Pakhomova S, Newcomer ME, et al. (2003). Mechanistic diversity of fosfomycin resistance in pathogenic microorganisms. Journal of the American Chemical Society, 125(51), 15730–15731 https://doi.org/10.1021/ja039307z

Arca P, Reguera G & Hardisson C. (1997). Plasmid-encoded fosfomycin resistance in bacteria isolated from the urinary tract in a multicentre survey. The Journal of antimicrobial chemotherapy, 40(3), 393–399. https://doi.org/10.1093/jac/40.3.393

Arca P, Hardisson C, Suárez JE. (1990). Purification of a glutathione S-transferase that mediates fosfomycin resistance in bacteria. Antimicrobial agents and chemotherapy, 34(5), 844–848. https://doi.org/10.1128/AAC.34.5.844

Ma Y, Xu X, Guo Q, et al. (2015). Characterization of fosA5, a new plasmid-mediated fosfomycin resistance gene in Escherichia coli. Letters in applied microbiology, 60(3), 259–264. https://doi.org/10.1111/lam.12366

Wachino J, Yamane K, Suzuki S, et al. (2010). Prevalence of fosfomycin resistance among CTX-M-producing Escherichia coli clinical isolates in Japan and identification of novel plasmid-mediated fosfomycin-modifying enzymes. Antimicrobial agents and chemotherapy, 54(7), 3061–3064. https://doi.org/10.1128/AAC.01834-09

Xu H, Miao V, Kwong W, et al. (2011). Identification of a novel fosfomycin resistance gene (fosA2) in Enterobacter cloacae from the Salmon River, Canada. Letters in applied microbiology, 52(4), 427–429. https://doi.org/10.1111/j.1472-765X.2011.03016.x

Qu TT, Shi KR, Ji JS, et al. (2014). Fosfomycin resistance among vancomycin-resistant enterococci owing to transfer of a plasmid harbouring the fosB gene. International journal of antimicrobial agents, 43(4), 361–365.

Cao M, Bernat BA, Wang Z, et al. (2001). FosB, a cysteine-dependent fosfomycin resistance protein under the control of sigma(W), an extracytoplasmic-function sigma factor in Bacillus subtilis. Journal of bacteriology, 183(7), 2380–2383.

Etienne J, Gerbaud G, Fleurette J, et al. (1991). Characterization of staphylococcal plasmids hybridizing with the fosfomycin resistance gene fosB. FEMS microbiology letters, 68(1), 119–122. https://doi.org/10.1016/0378-1097(91)90406-z

Lerner S. A, Ouellette M, Sobel, J. D. (2017). Antimicrobial drug resistance; Mechanisms of Drug Resistance, Volume 1( pp. 99-100) D. L. Mayers (Ed.). New York: Humana press.

Fillgrove KL, Pakhomova S, Schaab, et al. (2007). Structure and mechanism of the genomically encoded fosfomycin resistance protein, FosX, from Listeria monocytogenes. Biochemistry, 46(27), 8110–8120. https://doi.org/10.1021/bi700625p

García P, Arca P, Evaristo Suárez J. (1995). Product of fosC, a gene from Pseudomonas syringae, mediates fosfomycin resistance by using ATP as cosubstrate. Antimicrobial agents and chemotherapy, 39(7), 1569–1573. https://doi.org/10.1128/AAC.39.7.1569

Duez JM, Mousson C, Siebor E, et al. 2011. Fosfomycin and its application in the treatment of multidrug-resistant Enterobacteriaceae infections. Clin Med Rev Ther 3:123–142.

Thompson MK, Keithly ME, Goodman, MC, et al. (2014). Structure and function of the genomically encoded fosfomycin resistance enzyme, FosB, from Staphylococcusaureus. Biochemistry, 53(4), 755–765. https://doi.org/10.1021/bi4015852

Engel H, Gutiérrez-Fernández J, Flückiger C, et al. (2013). Heteroresistance to fosfomycin is predominant in Streptococcus pneumoniae and depends on the murA1 gene. Antimicrobial agents and chemotherapy, 57(6), 2801–2808.

Walsh CC, McIntosh MP, Peleg AY, et al. (2015). In vitro pharmacodynamics of fosfomycin against clinical isolates of Pseudomonas aeruginosa. The Journal of antimicrobial chemotherapy, 70(11), 3042–3050. https://doi.org/10.1093/jac/dkv221

Ho PL, Chan J, Lo WU, et al. (2013). Dissemination of plasmid-mediated fosfomycin resistance fosA3 among multidrug-resistant Escherichia coli from livestock and other animals. Journal of applied microbiology, 114(3), 695–702. https://doi.org/10.1111/jam.12099