메뉴 건너뛰기




Volumn 62, Issue 3, 2018, Pages

Cystatins 9 and C as a novel immunotherapy treatment that protects against multidrug-resistant New Delhi metallo-beta-lactamase-1-producing klebsiella pneumoniae

Author keywords

Antimicrobial; Cystatin 9; Cystatin C; Immunomodulation; Immunotherapy; Inflammation; Multidrug resistant; New Delhi metallo beta lactamase 1 producing K. pneumoniae; Pneumonia

Indexed keywords

ANTIINFECTIVE AGENT; COLISTIN; CYSTATIN; CYSTATIN 9; CYSTATIN C; UNCLASSIFIED DRUG; BETA LACTAMASE; BETA-LACTAMASE NDM-1;

EID: 85042416881     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01900-17     Document Type: Article
Times cited : (15)

References (42)
  • 1
    • 79960153872 scopus 로고    scopus 로고
    • Series “matrix metalloproteinases in lung health and disease”: Biological role of matrix metalloproteinases: A critical balance
    • Loffek S, Schilling O, Franzke CW. 2011. Series “matrix metalloproteinases in lung health and disease”: biological role of matrix metalloproteinases: a critical balance. Eur Respir J 38:191–208. https://doi.org/10.1183/09031936.00146510.
    • (2011) Eur Respir J , vol.38 , pp. 191-208
    • Loffek, S.1    Schilling, O.2    Franzke, C.W.3
  • 2
    • 42549100331 scopus 로고    scopus 로고
    • Cystatin protease inhibitors and immune functions
    • Zavasnik-Bergant T. 2008. Cystatin protease inhibitors and immune functions. Front Biosci 13:4625–4637. https://doi.org/10.2741/3028.
    • (2008) Front Biosci , vol.13 , pp. 4625-4637
    • Zavasnik-Bergant, T.1
  • 4
    • 0026806875 scopus 로고
    • Cystatins—inhibitors of cysteine proteinases
    • Bobek LA, Levine MJ. 1992. Cystatins—inhibitors of cysteine proteinases. Crit Rev Oral Biol Med 3:307–332. https://doi.org/10.1177/10454411920030040101.
    • (1992) Crit Rev Oral Biol Med , vol.3 , pp. 307-332
    • Bobek, L.A.1    Levine, M.J.2
  • 5
    • 33750984761 scopus 로고    scopus 로고
    • The role of cystatins in cells of the immune system
    • Kopitar-Jerala N. 2006. The role of cystatins in cells of the immune system. FEBS Lett 580:6295–6301. https://doi.org/10.1016/j.febslet.2006.10.055.
    • (2006) FEBS Lett , vol.580 , pp. 6295-6301
    • Kopitar-Jerala, N.1
  • 7
    • 0036709877 scopus 로고    scopus 로고
    • Immunomodulatory properties of cystatins
    • Vray B, Hartmann S, Hoebeke J. 2002. Immunomodulatory properties of cystatins. Cell Mol Life Sci 59:1503–1512. https://doi.org/10.1007/s00018-002-8525-4.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1503-1512
    • Vray, B.1    Hartmann, S.2    Hoebeke, J.3
  • 8
  • 10
    • 84864015486 scopus 로고    scopus 로고
    • Cystatin C in Alzheimer’s disease
    • Kaur G, Levy E. 2012. Cystatin C in Alzheimer’s disease. Front Mol Neurosci 5:79. https://doi.org/10.3389/fnmol.2012.00079.
    • (2012) Front Mol Neurosci , vol.5 , pp. 79
    • Kaur, G.1    Levy, E.2
  • 11
    • 25444494315 scopus 로고    scopus 로고
    • Late stage inhibition of hematogenous melanoma metastasis by cystatin C over-expression
    • Ervin H, Cox JL. 2005. Late stage inhibition of hematogenous melanoma metastasis by cystatin C over-expression. Cancer Cell Int 5:14. https://doi.org/10.1186/1475-2867-5-14.
    • (2005) Cancer Cell Int , vol.5 , pp. 14
    • Ervin, H.1    Cox, J.L.2
  • 12
    • 77953370520 scopus 로고    scopus 로고
    • Preclinical efficacy of cystatin C to target the oncogenic activity of transforming growth factor in breast cancer
    • Tian M, Schiemann WP. 2009. Preclinical efficacy of cystatin C to target the oncogenic activity of transforming growth factor in breast cancer. Transl Oncol 2:174–183. https://doi.org/10.1593/tlo.09145.
    • (2009) Transl Oncol , vol.2 , pp. 174-183
    • Tian, M.1    Schiemann, W.P.2
  • 13
    • 84881288420 scopus 로고    scopus 로고
    • Cystatins in immune system
    • Magister Š, Kos J. 2013. Cystatins in immune system. J Cancer 4:45–56. https://doi.org/10.7150/jca.5044.
    • (2013) J Cancer , vol.4 , pp. 45-56
    • Magister, Š.1    Kos, J.2
  • 14
    • 84905669507 scopus 로고    scopus 로고
    • Macrophage derived cystatin B/cathepsin B in HIV replication and neuropathogenesis
    • Rivera LE, Colón K, Cantres-Rosario YM, Zenón FM, Meléndez LM. 2014. Macrophage derived cystatin B/cathepsin B in HIV replication and neuropathogenesis. Curr HIV Res 12:111–120. https://doi.org/10.2174/1570162X12666140526120249.
    • (2014) Curr HIV Res , vol.12 , pp. 111-120
    • Rivera, L.E.1    Colón, K.2    Cantres-Rosario, Y.M.3    Zenón, F.M.4    Meléndez, L.M.5
  • 16
    • 85020226465 scopus 로고    scopus 로고
    • Emergence of multidrug-resistant New Delhi metallo--lactamase-1-producing Klebsiella pneumoniae in Egypt
    • Khalil MAF, Elgaml A, El-Mowafy M. 2017. Emergence of multidrug-resistant New Delhi metallo--lactamase-1-producing Klebsiella pneumoniae in Egypt. Microb Drug Resist 23:480–487. https://doi.org/10.1089/mdr.2016.0003.
    • (2017) Microb Drug Resist , vol.23 , pp. 480-487
    • Khalil, M.A.F.1    Elgaml, A.2    El-Mowafy, M.3
  • 17
    • 85018162548 scopus 로고    scopus 로고
    • Structure, genetics and worldwide spread of New Delhi metallo--lactamase (NDM): A threat to public health
    • Khan AU, Maryam L, Zarrilli R. 2017. Structure, genetics and worldwide spread of New Delhi metallo--lactamase (NDM): a threat to public health. BMC Microbiol 17:101. https://doi.org/10.1186/s12866-017-1012-8.
    • (2017) BMC Microbiol , vol.17 , pp. 101
    • Khan, A.U.1    Maryam, L.2    Zarrilli, R.3
  • 18
    • 84860117465 scopus 로고    scopus 로고
    • A case of New Delhi metallo--lactamase 1 (NDM-1)-producing Klebsiella pneumoniae with putative secondary transmission from the Balkan Region in the Netherlands
    • Halaby T, Reuland AE, Naiemi N, Potron A, Savelkoul PH, Vanenbrouke-Grauls CM, Nordmann P. 2012. A case of New Delhi metallo--lactamase 1 (NDM-1)-producing Klebsiella pneumoniae with putative secondary transmission from the Balkan Region in the Netherlands. Antimicrob Agents Chemother 56:2790–2791. https://doi.org/10.1128/AAC.00111-12.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 2790-2791
    • Halaby, T.1    Reuland, A.E.2    Naiemi, N.3    Potron, A.4    Savelkoul, P.H.5    Vanenbrouke-Grauls, C.M.6    Nordmann, P.7
  • 19
    • 84929431381 scopus 로고    scopus 로고
    • KPC and NDM-1 genes in related Enterobacteriaceae strains and plasmids from Pakistan and the United States
    • Pesesky MW, Hussain T, Wallace M, Wang B, Andleeb S, Burnham CD, Dantas G. 2015. KPC and NDM-1 genes in related Enterobacteriaceae strains and plasmids from Pakistan and the United States. J Emerg Infect Dis 21:1034–1037. https://doi.org/10.3201/eid2106.141504.
    • (2015) J Emerg Infect Dis , vol.21 , pp. 1034-1037
    • Pesesky, M.W.1    Hussain, T.2    Wallace, M.3    Wang, B.4    Andleeb, S.5    Burnham, C.D.6    Dantas, G.7
  • 22
    • 84961212560 scopus 로고    scopus 로고
    • New Delhi metallo--lactamase-1-producing Klebsiella pneumoniae, Florida, USA
    • Li JJ, Munoz-Price LS, Spychala CN, DePascale D, Doi Y. 2016. New Delhi metallo--lactamase-1-producing Klebsiella pneumoniae, Florida, USA. Emerg Infect Dis 22:744–746. https://doi.org/10.3201/eid2204.151176.
    • (2016) Emerg Infect Dis , vol.22 , pp. 744-746
    • Li, J.J.1    Munoz-Price, L.S.2    Spychala, C.N.3    DePascale, D.4    Doi, Y.5
  • 23
    • 84980019673 scopus 로고    scopus 로고
    • Global dissemination of carbapenemase-producing Klebsiella pneumoniae: Epidemiology, genetic context, treatment options, and detection methods
    • Lee C-R, Lee JH, Park KS, Kim YB, Jeong BC, Lee SH. 2016. Global dissemination of carbapenemase-producing Klebsiella pneumoniae: epidemiology, genetic context, treatment options, and detection methods. Front Microbiol 7:895. https://doi.org/10.3389/fmicb.2016.00895.
    • (2016) Front Microbiol , vol.7 , pp. 895
    • Lee, C.-R.1    Lee, J.H.2    Park, K.S.3    Kim, Y.B.4    Jeong, B.C.5    Lee, S.H.6
  • 24
    • 84942240891 scopus 로고    scopus 로고
    • Carbapenemase-producing Klebsiella pneumoniae, a key pathogen set for global nosocomial dominance
    • Pitout JD, Nordmann P, Poirel L. 2015. Carbapenemase-producing Klebsiella pneumoniae, a key pathogen set for global nosocomial dominance. Antimicrob Agents Chemother 59:5873–5884. https://doi.org/10.1128/AAC.01019-15.
    • (2015) Antimicrob Agents Chemother , vol.59 , pp. 5873-5884
    • Pitout, J.D.1    Nordmann, P.2    Poirel, L.3
  • 25
    • 84902590942 scopus 로고    scopus 로고
    • Resistance determinants and mobile genetic elements of an NDM-1-encoding Klebsiella pneumoniae strain
    • Hudson CM, Bent ZW, Meagher RJ, Williams KP. 2014. Resistance determinants and mobile genetic elements of an NDM-1-encoding Klebsiella pneumoniae strain. PLoS One 9:e99209. https://doi.org/10.1371/journal.pone.0099209.
    • (2014) PLoS One , vol.9 , pp. e99209
    • Hudson, C.M.1    Bent, Z.W.2    Meagher, R.J.3    Williams, K.P.4
  • 26
    • 84907049122 scopus 로고    scopus 로고
    • Carbapenemase-producing Klebsiella pneumoniae
    • Robilotti E, Deresinski S. 2014. Carbapenemase-producing Klebsiella pneumoniae. F1000Prime Rep 6:80. https://doi.org/10.12703/P6-80.
    • (2014) F1000Prime Rep , vol.6 , pp. 80
    • Robilotti, E.1    Deresinski, S.2
  • 28
    • 84940905795 scopus 로고    scopus 로고
    • Impact of the New Delhi metallo-beta-lactamase on beta-lactam antibiotics
    • Zmarlicka MT, Nailor MD, Nicolau DP. 2015. Impact of the New Delhi metallo-beta-lactamase on beta-lactam antibiotics. Infect Drug Resist 8:297–309. https://doi.org/10.2147/IDR.S39186.
    • (2015) Infect Drug Resist , vol.8 , pp. 297-309
    • Zmarlicka, M.T.1    Nailor, M.D.2    Nicolau, D.P.3
  • 30
    • 33748302776 scopus 로고    scopus 로고
    • Acute respiratory distress syndrome and pneumonia: A comprehensive review of clinical data
    • Bauer TT, Ewig S, Rodloff AC, Muller E. 2006. Acute respiratory distress syndrome and pneumonia: a comprehensive review of clinical data. Clin Infect Dis 43:748–756. https://doi.org/10.1086/506430.
    • (2006) Clin Infect Dis , vol.43 , pp. 748-756
    • Bauer, T.T.1    Ewig, S.2    Rodloff, A.C.3    Muller, E.4
  • 31
    • 10044272802 scopus 로고    scopus 로고
    • Molecular mechanism for activation and regulation of matrix metalloproteinases during bacterial infections and respiratory inflammation
    • Okamoto T, Akuta T, Tamura F, van Der Vliet A, Akaike T. 2004. Molecular mechanism for activation and regulation of matrix metalloproteinases during bacterial infections and respiratory inflammation. Biol Chem 385:997–1006. https://doi.org/10.1515/BC.2004.130.
    • (2004) Biol Chem , vol.385 , pp. 997-1006
    • Okamoto, T.1    Akuta, T.2    Tamura, F.3    van Der Vliet, A.4    Akaike, T.5
  • 33
    • 84857051083 scopus 로고    scopus 로고
    • Efficacies of colistin and tigecycline in mice with experimental pneumonia due to NDM-1-producing strains of Klebsiella pneumoniae and Escherichia coli
    • Docobo-érez F, Nordmann P, Domínguez-Herrera J, López-Rojas R, Smani Y, Poirel L, Pachón J. 2012. Efficacies of colistin and tigecycline in mice with experimental pneumonia due to NDM-1-producing strains of Klebsiella pneumoniae and Escherichia coli. Int J Antimicrob Agents 39: 251–254. https://doi.org/10.1016/j.ijantimicag.2011.10.012.
    • (2012) Int J Antimicrob Agents , vol.39 , pp. 251-254
    • Docobo-érez, F.1    Nordmann, P.2    Domínguez-Herrera, J.3    López-Rojas, R.4    Smani, Y.5    Poirel, L.6    Pachón, J.7
  • 34
    • 84907180244 scopus 로고    scopus 로고
    • Pegylation improves the pharmacokinetics and bioavailability of small-molecule drugs hydrolyzable by esterases: A study of phospho-ibuprofen
    • Mattheolabakis G, Wong CC, Sun Y, Amella CA, Richards R, Constan-tinides PP, Rigas B. 2014. Pegylation improves the pharmacokinetics and bioavailability of small-molecule drugs hydrolyzable by esterases: a study of phospho-ibuprofen. J Pharmacol Exp Ther 351:61–66. https://doi.org/10.1124/jpet.114.217208.
    • (2014) J Pharmacol Exp Ther , vol.351 , pp. 61-66
    • Mattheolabakis, G.1    Wong, C.C.2    Sun, Y.3    Amella, C.A.4    Richards, R.5    Constan-Tinides, P.P.6    Rigas, B.7
  • 35
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • Harris JM, Chess RB. 2003. Effect of pegylation on pharmaceuticals. Nat Rev Drug Discov 2:214–221. https://doi.org/10.1038/nrd1033.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 36
    • 84979197352 scopus 로고    scopus 로고
    • Colistin for lung infection: An update
    • Gurjar M. 2015. Colistin for lung infection: an update. J Intensive Care 3:3. https://doi.org/10.1186/s40560-015-0072-9.
    • (2015) J Intensive Care , vol.3 , pp. 3
    • Gurjar, M.1
  • 37
    • 17644389620 scopus 로고    scopus 로고
    • Colistin: The revival of polymyxins for the management of multidrug-resistant gram-negative bacterial infections
    • Falagas ME, Kasiakou SK. 2005. Colistin: the revival of polymyxins for the management of multidrug-resistant gram-negative bacterial infections. Clin Infect Dis 40:1333–1341. https://doi.org/10.1086/429323.
    • (2005) Clin Infect Dis , vol.40 , pp. 1333-1341
    • Falagas, M.E.1    Kasiakou, S.K.2
  • 38
    • 0030051258 scopus 로고    scopus 로고
    • Characterization of cystatin C from bovine parotid glands: Cysteine proteinase inhibition and antiviral properties
    • Cimerman N, Kosorok MD, Korant BD, Turk B, Turk V. 1996. Characterization of cystatin C from bovine parotid glands: cysteine proteinase inhibition and antiviral properties. Biol Chem Hoppe Seyler 377:19–23. https://doi.org/10.1515/bchm3.1996.377.1.19.
    • (1996) Biol Chem Hoppe Seyler , vol.377 , pp. 19-23
    • Cimerman, N.1    Kosorok, M.D.2    Korant, B.D.3    Turk, B.4    Turk, V.5
  • 39
    • 0025177313 scopus 로고
    • Cystatin C, a human proteinase inhibitor, blocks replication of herpes simplex virus
    • Björck L, Grubb A, Kjellén L. 1990. Cystatin C, a human proteinase inhibitor, blocks replication of herpes simplex virus. J Virol 64:941–943.
    • (1990) J Virol , vol.64 , pp. 941-943
    • Björck, L.1    Grubb, A.2    Kjellén, L.3
  • 40
    • 78650365533 scopus 로고    scopus 로고
    • Cystatin cures visceral leishmaniasis by NF-B-mediated proinflammatory response through co-ordination of TLR/MyD88 signaling with p105-Tpl2-ERK pathway
    • Kar S, Ukil A, Das PK. 2011. Cystatin cures visceral leishmaniasis by NF-B-mediated proinflammatory response through co-ordination of TLR/MyD88 signaling with p105-Tpl2-ERK pathway. Eur J Immunol 41: 116–127. https://doi.org/10.1002/eji.201040533.
    • (2011) Eur J Immunol , vol.41 , pp. 116-127
    • Kar, S.1    Ukil, A.2    Das, P.K.3
  • 41
    • 77950220938 scopus 로고    scopus 로고
    • Toll-like receptor 3 agonist protection against experimental Francisella tularensis respiratory tract infection
    • Pyles RB, Jezek GE, Eaves-Pyles TD. 2010. Toll-like receptor 3 agonist protection against experimental Francisella tularensis respiratory tract infection. Infect Immun 78:1700 –1710. https://doi.org/10.1128/IAI.00736-09.
    • (2010) Infect Immun , vol.78 , pp. 1700-1710
    • Pyles, R.B.1    Jezek, G.E.2    Eaves-Pyles, T.D.3
  • 42
    • 84862749864 scopus 로고    scopus 로고
    • Rapid determination of methicillin resistance among Staphylococcus aureus clinical isolates by colorimetric methods
    • Coban AY. 2012. Rapid determination of methicillin resistance among Staphylococcus aureus clinical isolates by colorimetric methods. J Clin Microbiol 50:2191–2193. https://doi.org/10.1128/JCM.00471-12.
    • (2012) J Clin Microbiol , vol.50 , pp. 2191-2193
    • Coban, A.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.