메뉴 건너뛰기




Volumn 14, Issue 11, 2015, Pages 1064-1072

Analysis of the Aspergillus fumigatus biofilm extracellular matrix by solid-state nuclear magnetic resonance spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; SCLEROPROTEIN;

EID: 84942878263     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00050-15     Document Type: Article
Times cited : (70)

References (41)
  • 1
    • 0035423126 scopus 로고    scopus 로고
    • The pathobiology of Aspergillus fumigatus
    • Latge JP. 2001. The pathobiology of Aspergillus fumigatus. Trends Microbiol 9:382-389. http://dx.doi.org/10.1016/S0966-842X(01)02104-7.
    • (2001) Trends Microbiol , vol.9 , pp. 382-389
    • Latge, J.P.1
  • 2
    • 67651083816 scopus 로고    scopus 로고
    • Nosocomial aspergillosis and building construction
    • Haiduven D. 2009. Nosocomial aspergillosis and building construction. Med Mycol 47:S210-216. http://dx.doi.org/10.1080/13693780802247694.
    • (2009) Med Mycol , vol.47 , pp. S210-S216
    • Haiduven, D.1
  • 3
    • 0030942448 scopus 로고    scopus 로고
    • Aspergillus flavus cultured from a salinefilled implant
    • Rosenblatt WB, Pollock A. 1997. Aspergillus flavus cultured from a salinefilled implant. Plast Reconstr Surg 99:1470-1472.
    • (1997) Plast Reconstr Surg , vol.99 , pp. 1470-1472
    • Rosenblatt, W.B.1    Pollock, A.2
  • 4
    • 79952658324 scopus 로고    scopus 로고
    • Aspergillus fumigatus in the clinical setting
    • Muller F-MC, Seidler M, Beauvais A. 2011. Aspergillus fumigatus in the clinical setting. Med Mycol 49:S96-S100. http://dx.doi.org/10.3109/13693786.2010.502190.
    • (2011) Med Mycol , vol.49 , pp. S96-S100
    • Muller, F.-M.1    Seidler, M.2    Beauvais, A.3
  • 6
    • 64549134317 scopus 로고    scopus 로고
    • Characterization of a biofilm-like extracellular matrix in FLO1-expressing Saccharomyces cerevisiae cells
    • Beauvais A, Loussert C, Prevost MC, Verstrepen K, Latge JP. 2009. Characterization of a biofilm-like extracellular matrix in FLO1-expressing Saccharomyces cerevisiae cells. FEMS Yeast Res 9:411-419. http://dx.doi.org/10.1111/j.1567-1364.2009.00482.x.
    • (2009) FEMS Yeast Res , vol.9 , pp. 411-419
    • Beauvais, A.1    Loussert, C.2    Prevost, M.C.3    Verstrepen, K.4    Latge, J.P.5
  • 8
    • 84942087410 scopus 로고    scopus 로고
    • Biofilm formation by Aspergillus fumigatus
    • Kaur S, Singh S. 2014. Biofilm formation by Aspergillus fumigatus. Med Mycol 52:2-9. http://dx.doi.org/10.3109/13693786.2013.819592.
    • (2014) Med Mycol , vol.52 , pp. 2-9
    • Kaur, S.1    Singh, S.2
  • 9
    • 34748871970 scopus 로고    scopus 로고
    • Development of a simple model for studying the effects of antifungal agents on multicellular communities of Aspergillus fumigatus
    • Mowat E, Butcher J, Lang S, Williams C, Ramage G. 2007. Development of a simple model for studying the effects of antifungal agents on multicellular communities of Aspergillus fumigatus. J Med Microbiol 56:1205-1212. http://dx.doi.org/10.1099/jmm.0.47247-0.
    • (2007) J Med Microbiol , vol.56 , pp. 1205-1212
    • Mowat, E.1    Butcher, J.2    Lang, S.3    Williams, C.4    Ramage, G.5
  • 10
    • 84897971296 scopus 로고    scopus 로고
    • Development and antimicrobial susceptibility studies of in vitro monomicrobial and polymicrobial biofilm models with Aspergillus fumigatus and Psuedomonas aeruginosa
    • Manavathu EK, Vager DL, Vazquez JA. 2014. Development and antimicrobial susceptibility studies of in vitro monomicrobial and polymicrobial biofilm models with Aspergillus fumigatus and Psuedomonas aeruginosa. BMC Microbiol 14:53. http://dx.doi.org/10.1186/1471-2180-14-53.
    • (2014) BMC Microbiol , vol.14 , pp. 53
    • Manavathu, E.K.1    Vager, D.L.2    Vazquez, J.A.3
  • 11
    • 0035152224 scopus 로고    scopus 로고
    • Biofilm exopolysaccharides: A strong and sticky framework
    • Sutherland IW. 2001. Biofilm exopolysaccharides: a strong and sticky framework. Microbiology 147:3-9. http://dx.doi.org/10.1099/00221287-147-1-3.
    • (2001) Microbiology , vol.147 , pp. 3-9
    • Sutherland, I.W.1
  • 12
    • 78149426499 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy on complex biomolecules
    • Renault M, Cukkemane A, Baldus M. 2010. Solid-state NMR spectroscopy on complex biomolecules. Angew Chem Int Ed Engl 49:8347-8357.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 8347-8357
    • Renault, M.1    Cukkemane, A.2    Baldus, M.3
  • 13
    • 0037195278 scopus 로고    scopus 로고
    • Rotational-echo double resonance characterization of vancomycin mode of action in S. Aureus
    • Cegelski L, Hing AW, Kim SJ, Studelska DR, O’Connor RD, Mehta AK, Schaefer J. 2002. Rotational-echo double resonance characterization of vancomycin mode of action in S. aureus. Biochemistry 41:13053-13058. http://dx.doi.org/10.1021/bi0202326.
    • (2002) Biochemistry , vol.41 , pp. 13053-13058
    • Cegelski, L.1    Hing, A.W.2    Kim, S.J.3    Studelska, D.R.4    O’connor, R.D.5    Mehta, A.K.6    Schaefer, J.7
  • 14
    • 52449084468 scopus 로고    scopus 로고
    • Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopy
    • Curtis-Fisk J, Spencer RM, Weliky DP. 2008. Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopy. J Am Chem Soc 130: 12568-12569. http://dx.doi.org/10.1021/ja8039426.
    • (2008) J am Chem Soc , vol.130 , pp. 12568-12569
    • Curtis-Fisk, J.1    Spencer, R.M.2    Weliky, D.P.3
  • 15
    • 84885597871 scopus 로고    scopus 로고
    • REDOR applications in biology: An overview
    • In McDermott AE, Polenova T, John Wiley & Sons Ltd., Chichester, United Kingdom
    • Toke O, Cegelski L. 2010. REDOR applications in biology: an overview, p 743-490. In McDermott AE, Polenova T (ed), Solid-state NMR studies of biopolymers. John Wiley & Sons Ltd., Chichester, United Kingdom.
    • (2010) Solid-State NMR Studies of Biopolymers , pp. 490-743
    • Toke, O.1    Cegelski, L.2
  • 16
    • 85028780557 scopus 로고    scopus 로고
    • Peptidoglycan architecture of Grampositive bacteria by solid-state NMR
    • Kim SJ, Chang J, Singh M. 2015. Peptidoglycan architecture of Grampositive bacteria by solid-state NMR. Biochim Biophys Acta Biomembr 1848:350-362. http://dx.doi.org/10.1016/j.bbamem.2014.05.031.
    • (2015) Biochim Biophys Acta Biomembr , vol.1848 , pp. 350-362
    • Kim, S.J.1    Chang, J.2    Singh, M.3
  • 17
    • 84979852596 scopus 로고    scopus 로고
    • Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization
    • Yamamoto K, Caporini MA, Im SC, Waskell L, Ramamoorthy A. 2015. Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization. Biochim Biophys Acta Biomembr 1848:342-349. http://dx.doi.org/10.1016/j.bbamem.2014.07.008.
    • (2015) Biochim Biophys Acta Biomembr , vol.1848 , pp. 342-349
    • Yamamoto, K.1    Caporini, M.A.2    Im, S.C.3    Waskell, L.4    Ramamoorthy, A.5
  • 18
    • 67349241519 scopus 로고    scopus 로고
    • Beyond NMR spectra of antimicrobial peptides: Dynamical images at atomic resolution and functional insights
    • Ramamoorthy A. 2009. Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights. Solid State Nucl Magn Reson 35:201-207. http://dx.doi.org/10.1016/j.ssnmr.2009.03.003.
    • (2009) Solid State Nucl Magn Reson , vol.35 , pp. 201-207
    • Ramamoorthy, A.1
  • 19
    • 84861124184 scopus 로고    scopus 로고
    • Dimethyl sulfoxide and ethanol elicit increased amyloid biogenesis and amyloid-integrated biofilm formation in E. Coli
    • Lim JY, May JM, Cegelski L. 2012. Dimethyl sulfoxide and ethanol elicit increased amyloid biogenesis and amyloid-integrated biofilm formation in E. coli. Appl Environ Microbiol 78:3369-3378. http://dx.doi.org/10.1128/AEM.07743-11.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 3369-3378
    • Lim, J.Y.1    May, J.M.2    Cegelski, L.3
  • 20
    • 84886720456 scopus 로고    scopus 로고
    • Sum of the parts: Composition and architecture of the bacterial extracellular matrix
    • McCrate OA, Zhou X, Reichhardt C, Cegelski L. 2013. Sum of the parts: composition and architecture of the bacterial extracellular matrix. J Mol Biol 425:4286-4294. http://dx.doi.org/10.1016/j.jmb.2013.06.022.
    • (2013) J Mol Biol , vol.425 , pp. 4286-4294
    • McCrate, O.A.1    Zhou, X.2    Reichhardt, C.3    Cegelski, L.4
  • 21
    • 84924325992 scopus 로고    scopus 로고
    • Characterization of the Vibrio cholerae extracellular matrix: A top-down solid-state NMR approach
    • Reichhardt C, Fong JC, Yildiz F, Cegelski L. 2015. Characterization of the Vibrio cholerae extracellular matrix: a top-down solid-state NMR approach. Biochim Biophys Acta 1848:378-383. http://dx.doi.org/10.1016/j.bbamem.2014.05.030.
    • (2015) Biochim Biophys Acta , vol.1848 , pp. 378-383
    • Reichhardt, C.1    Fong, J.C.2    Yildiz, F.3    Cegelski, L.4
  • 22
    • 84896317885 scopus 로고    scopus 로고
    • Solid-state NMR for bacterial biofilms
    • Reichhardt C, Cegelski L. 2014. Solid-state NMR for bacterial biofilms. Mol Phys 112:887-894. http://dx.doi.org/10.1080/00268976.2013.837983.
    • (2014) Mol Phys , vol.112 , pp. 887-894
    • Reichhardt, C.1    Cegelski, L.2
  • 23
    • 1842612577 scopus 로고    scopus 로고
    • Bacterial biofilms: From the natural environment to infectious diseases
    • Hall-Stoodley L, Costerton JW, Stoodley P. 2004. Bacterial biofilms: from the natural environment to infectious diseases. Nat Rev Microbiol 2:95-108. http://dx.doi.org/10.1038/nrmicro821.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 95-108
    • Hall-Stoodley, L.1    Costerton, J.W.2    Stoodley, P.3
  • 25
    • 33646570211 scopus 로고    scopus 로고
    • Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions
    • Oda K, Kakizono D, Yamada O, Iefuji H, Akita O, Iwashita K. 2006. Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions. Appl Environ Microbiol 72:3448-3457. http://dx.doi.org/10.1128/AEM.72.5.3448-3457.2006.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 3448-3457
    • Oda, K.1    Kakizono, D.2    Yamada, O.3    Iefuji, H.4    Akita, O.5    Iwashita, K.6
  • 26
    • 0032425403 scopus 로고    scopus 로고
    • Immunological characterization of Asp f 2, a major allergen from Aspergillus fumigatus associated with allergic bronchopulmonary aspergillosis
    • Banerjee B, Greenberger PA, Fink JN, Kurup VP. 1998. Immunological characterization of Asp f 2, a major allergen from Aspergillus fumigatus associated with allergic bronchopulmonary aspergillosis. Infect Immun 66:5175-5182.
    • (1998) Infect Immun , vol.66 , pp. 5175-5182
    • Banerjee, B.1    Greenberger, P.A.2    Fink, J.N.3    Kurup, V.P.4
  • 27
    • 0001250543 scopus 로고
    • Carbon-13 nuclear magnetic resonance of polymers spinning at the magic angle
    • Schaefer J, Stejskal EO. 1976. Carbon-13 nuclear magnetic resonance of polymers spinning at the magic angle. J Am Chem Soc 98:1031-1032. http://dx.doi.org/10.1021/ja00420a036.
    • (1976) J am Chem Soc , vol.98 , pp. 1031-1032
    • Schaefer, J.1    Stejskal, E.O.2
  • 28
    • 0001026653 scopus 로고
    • High-resolution carbon-13 nuclear magnetic resonance study of some solid, glassy polymers
    • Schaefer J, Stejskal EO, Buchdahl R. 1975. High-resolution carbon-13 nuclear magnetic resonance study of some solid, glassy polymers. Macromolecules 8:291-296. http://dx.doi.org/10.1021/ma60045a010.
    • (1975) Macromolecules , vol.8 , pp. 291-296
    • Schaefer, J.1    Stejskal, E.O.2    Buchdahl, R.3
  • 29
    • 0023050064 scopus 로고
    • Analysis of chitin structure by nuclear magnetic resonance spectroscopy and chitinolytic enzyme digestion
    • Fukamizo T, Kramer KJ, Mueller DD, Schaefer J, Garbow J, Jacob GS. 1986. Analysis of chitin structure by nuclear magnetic resonance spectroscopy and chitinolytic enzyme digestion. Arch Biochem Biophys 249:15-26. http://dx.doi.org/10.1016/0003-9861(86)90555-2.
    • (1986) Arch Biochem Biophys , vol.249 , pp. 15-26
    • Fukamizo, T.1    Kramer, K.J.2    Mueller, D.D.3    Schaefer, J.4    Garbow, J.5    Jacob, G.S.6
  • 30
    • 0035663318 scopus 로고    scopus 로고
    • Aspergillus fumigatus cell wall: Composition and biosynthesis
    • Bernard M, Latge JP. 2001. Aspergillus fumigatus cell wall: composition and biosynthesis. Med Mycol 39:S9-S17.
    • (2001) Med Mycol , vol.39 , pp. S9-S17
    • Bernard, M.1    Latge, J.P.2
  • 31
    • 45149145322 scopus 로고
    • Rotational-echo double-resonance NMR
    • Gullion T, Schaefer J. 1989. Rotational-echo double-resonance NMR. J Magn Reson 81:196-200.
    • (1989) J Magn Reson , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 36
    • 0031029702 scopus 로고    scopus 로고
    • Role of oxidants in microbial pathophysiology
    • Miller RA, Britigan BE. 1997. Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 10:1-18.
    • (1997) Clin Microbiol Rev , vol.10 , pp. 1-18
    • Miller, R.A.1    Britigan, B.E.2
  • 38
    • 18744386931 scopus 로고    scopus 로고
    • PKSP-dependent reduction of phagolysosome fusion and intracellular kill of Aspergillus fumigatus conidia by human monocyte-derived macrophages
    • Jahn B, Langfelder K, Schneider U, Schindel C, Brakhage AA. 2002. PKSP-dependent reduction of phagolysosome fusion and intracellular kill of Aspergillus fumigatus conidia by human monocyte-derived macrophages. Cell Microbiol 4:793-803. http://dx.doi.org/10.1046/j.1462-5822.2002.00228.x.
    • (2002) Cell Microbiol , vol.4 , pp. 793-803
    • Jahn, B.1    Langfelder, K.2    Schneider, U.3    Schindel, C.4    Brakhage, A.A.5
  • 39
    • 42349092473 scopus 로고    scopus 로고
    • Following fungal melanin biosynthesis with solid-state NMR: Biopolymer molecular structures and possible connections to cell-wall polysaccharides
    • Zhong J, Frases S, Wang H, Casadevall A, Stark RE. 2008. Following fungal melanin biosynthesis with solid-state NMR: biopolymer molecular structures and possible connections to cell-wall polysaccharides. Biochemistry 47:4701-4710. http://dx.doi.org/10.1021/bi702093r.
    • (2008) Biochemistry , vol.47 , pp. 4701-4710
    • Zhong, J.1    Frases, S.2    Wang, H.3    Casadevall, A.4    Stark, R.E.5
  • 40
    • 84897512217 scopus 로고    scopus 로고
    • Melanin from the nitrogen-fixing bacterium Azotobacter chroococcum: A spectroscopic characterization
    • Banerjee A, Supakar S, Banerjee R. 2014. Melanin from the nitrogen-fixing bacterium Azotobacter chroococcum: a spectroscopic characterization. PLoS One 9:e84574. http://dx.doi.org/10.1371/journal.pone.0084574.
    • (2014) Plos One , vol.9
    • Banerjee, A.1    Supakar, S.2    Banerjee, R.3
  • 41
    • 84874519965 scopus 로고    scopus 로고
    • Extracellular DNA release acts as an antifungal resistance mechanism in mature Aspergillus fumigatus biofilms
    • Rajendran R, Williams C, Lappin DF, Millington O, Martins M, Ramage G. 2013. Extracellular DNA release acts as an antifungal resistance mechanism in mature Aspergillus fumigatus biofilms. Eukaryot Cell 12: 420-429. http://dx.doi.org/10.1128/EC.00287-12.
    • (2013) Eukaryot Cell , vol.12 , pp. 420-429
    • Rajendran, R.1    Williams, C.2    Lappin, D.F.3    Millington, O.4    Martins, M.5    Ramage, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.