메뉴 건너뛰기




Volumn 123, Issue 4, 2007, Pages 305-319

Analytical applications of Fourier transform-infrared (FT-IR) spectroscopy in microbiology and prion research

Author keywords

Fourier transform infrared (FT IR) spectroscopy; Microorganisms; Prion; Prion diseases; Prion protein; Transmissible spongiform encephalopathies

Indexed keywords

PRION PROTEIN;

EID: 34547121477     PISSN: 03781135     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vetmic.2007.04.010     Document Type: Article
Times cited : (237)

References (60)
  • 2
    • 0031881510 scopus 로고    scopus 로고
    • Cerebral targeting indicates vagal spread of infection in hamsters fed with scrapie
    • Beekes M., McBride P.A., and Baldauf E. Cerebral targeting indicates vagal spread of infection in hamsters fed with scrapie. J. Gen. Virol. 79 (1998) 601-607
    • (1998) J. Gen. Virol. , vol.79 , pp. 601-607
    • Beekes, M.1    McBride, P.A.2    Baldauf, E.3
  • 3
    • 23844471279 scopus 로고    scopus 로고
    • Blood infectivity, processing and screening tests in transmissible spongiform encephalopathy
    • Brown P. Blood infectivity, processing and screening tests in transmissible spongiform encephalopathy. Vox Sang. 89 (2005) 63-70
    • (2005) Vox Sang. , vol.89 , pp. 63-70
    • Brown, P.1
  • 4
    • 28044460065 scopus 로고    scopus 로고
    • In vivo detection of scrapie cases from blood by infrared spectroscopy
    • Carmona P., Monzon M., Monleon E., Badiola J.J., and Monreal J. In vivo detection of scrapie cases from blood by infrared spectroscopy. J. Gen. Virol. 86 (2005) 3425-3431
    • (2005) J. Gen. Virol. , vol.86 , pp. 3425-3431
    • Carmona, P.1    Monzon, M.2    Monleon, E.3    Badiola, J.J.4    Monreal, J.5
  • 5
    • 24744446203 scopus 로고    scopus 로고
    • Detection of prions in blood
    • Castilla J., Saa P., and Soto C. Detection of prions in blood. Nat. Med. 11 (2005) 982-985
    • (2005) Nat. Med. , vol.11 , pp. 982-985
    • Castilla, J.1    Saa, P.2    Soto, C.3
  • 6
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey B.W., Dong A., Bhat K.S., Ernst D., Hayes S.F., and Caughey W.S. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30 (1991) 7672-7680
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 7
    • 0033610870 scopus 로고    scopus 로고
    • Strain-dependent differences in beta-sheet conformations of abnormal prion protein
    • Caughey B., Raymond G.J., and Bessen R.A. Strain-dependent differences in beta-sheet conformations of abnormal prion protein. J. Biol. Chem. 273 (1998) 32230-32235
    • (1998) J. Biol. Chem. , vol.273 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 8
    • 0029839357 scopus 로고    scopus 로고
    • In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy
    • Choo L.P., Wetzel D.L., Halliday W.C., Jackson M., Levine S.M., and Mantsch H.H. In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy. Biophys. J. 71 (1996) 1672-1679
    • (1996) Biophys. J. , vol.71 , pp. 1672-1679
    • Choo, L.P.1    Wetzel, D.L.2    Halliday, W.C.3    Jackson, M.4    Levine, S.M.5    Mantsch, H.H.6
  • 9
    • 0003007623 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Chalmers J.M., and Griffiths P.R. (Eds), John Wiley & Sons, Chichester, UK
    • Fabian H., and Mäntele W. Infrared spectroscopy of proteins. In: Chalmers J.M., and Griffiths P.R. (Eds). Handbook of Vibrational Spectroscopy (2002), John Wiley & Sons, Chichester, UK 3399-3425
    • (2002) Handbook of Vibrational Spectroscopy , pp. 3399-3425
    • Fabian, H.1    Mäntele, W.2
  • 10
    • 29044440038 scopus 로고    scopus 로고
    • FT-IR spectroscopy as a tool for rapid identification and intra-species characterization of airborne filamentous fungi
    • Fischer G., Braun S., Thissen R., and Dott W. FT-IR spectroscopy as a tool for rapid identification and intra-species characterization of airborne filamentous fungi. J. Microbiol. Meth. 64 (2006) 63-77
    • (2006) J. Microbiol. Meth. , vol.64 , pp. 63-77
    • Fischer, G.1    Braun, S.2    Thissen, R.3    Dott, W.4
  • 11
    • 0027388993 scopus 로고
    • Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity
    • Gasset M., Baldwin M.A., Fletterick R.J., and Prusiner S.B. Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 1-5
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 1-5
    • Gasset, M.1    Baldwin, M.A.2    Fletterick, R.J.3    Prusiner, S.B.4
  • 12
    • 0026042799 scopus 로고
    • Elaboration of a procedure for identification of bacteria using Fourier-transform infrared spectral libraries: a stepwise correlation approach
    • Helm D., Labischinski H., and Naumann D. Elaboration of a procedure for identification of bacteria using Fourier-transform infrared spectral libraries: a stepwise correlation approach. J. Microbiol. Meth. 14 (1991) 127-147
    • (1991) J. Microbiol. Meth. , vol.14 , pp. 127-147
    • Helm, D.1    Labischinski, H.2    Naumann, D.3
  • 13
    • 0026028597 scopus 로고
    • Classification and identification of bacteria by Fourier-transform infrared spectroscopy
    • Helm D., Labischinski H., Schallehn G., and Naumann D. Classification and identification of bacteria by Fourier-transform infrared spectroscopy. J. Gen. Microbiol. 137 (1991) 69-79
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 69-79
    • Helm, D.1    Labischinski, H.2    Schallehn, G.3    Naumann, D.4
  • 15
    • 0034711569 scopus 로고    scopus 로고
    • Increased ferric iron content and iron-induced oxidative stress in the brains of scrapie-infected mice
    • Kim N.H., Park S.J., Jin J.K., Kwon M.S., Choi E.K., Carp R.I., and Kim Y.S. Increased ferric iron content and iron-induced oxidative stress in the brains of scrapie-infected mice. Brain Res. 884 (2000) 98-103
    • (2000) Brain Res. , vol.884 , pp. 98-103
    • Kim, N.H.1    Park, S.J.2    Jin, J.K.3    Kwon, M.S.4    Choi, E.K.5    Carp, R.I.6    Kim, Y.S.7
  • 17
    • 0034660034 scopus 로고    scopus 로고
    • Detection of pathological molecular alterations in scrapie-infected hamster brain by Fourier transform infrared (FT-IR) spectroscopy
    • Kneipp J., Lasch P., Baldauf E., Beekes M., and Naumann D. Detection of pathological molecular alterations in scrapie-infected hamster brain by Fourier transform infrared (FT-IR) spectroscopy. Biochim. Biophys. Acta 1501 (2000) 189-199
    • (2000) Biochim. Biophys. Acta , vol.1501 , pp. 189-199
    • Kneipp, J.1    Lasch, P.2    Baldauf, E.3    Beekes, M.4    Naumann, D.5
  • 18
    • 0037092437 scopus 로고    scopus 로고
    • Molecular changes of preclinical scrapie can be detected by infrared spectroscopy
    • Kneipp J., Beekes M., Lasch P., and Naumann D. Molecular changes of preclinical scrapie can be detected by infrared spectroscopy. J. Neurosci. 22 (2002) 2989-2997
    • (2002) J. Neurosci. , vol.22 , pp. 2989-2997
    • Kneipp, J.1    Beekes, M.2    Lasch, P.3    Naumann, D.4
  • 21
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S., and Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38 (1986) 181-364
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 23
    • 0342864805 scopus 로고    scopus 로고
    • Rapid and reliable identification of food-borne yeasts by Fourier-transform infrared spectroscopy
    • Kümmerle M., Scherer S., and Seiler S. Rapid and reliable identification of food-borne yeasts by Fourier-transform infrared spectroscopy. Appl. Environ. Microbiol. 64 (1998) 2207-2214
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2207-2214
    • Kümmerle, M.1    Scherer, S.2    Seiler, S.3
  • 24
    • 0345600215 scopus 로고    scopus 로고
    • Identification of bovine spongiform encephalopathy (BSE) in bovine serum using infrared spectroscopy and multivariate classification analysis
    • Lasch P., Schmitt J., Beekes M., Eiden M., Moecks J., Petrich W., Fabian H., and Naumann D. Identification of bovine spongiform encephalopathy (BSE) in bovine serum using infrared spectroscopy and multivariate classification analysis. Anal. Chem. 75 (2003) 6673-6678
    • (2003) Anal. Chem. , vol.75 , pp. 6673-6678
    • Lasch, P.1    Schmitt, J.2    Beekes, M.3    Eiden, M.4    Moecks, J.5    Petrich, W.6    Fabian, H.7    Naumann, D.8
  • 25
    • 34547108788 scopus 로고    scopus 로고
    • Lasch, P., Beekes, M., Schmitt, J., Naumann, D., 2006. Detection of preclinical scrapie from serum by infrared spectroscopy and chemometrics. Anal. Bioanal. Chem. (Epub ahead of print).
  • 27
    • 18144377567 scopus 로고    scopus 로고
    • Historical survey of infrared and Raman spectroscopy of biological materials
    • Gremlich H. (Ed), Marcel Dekker, New York, USA
    • Mantsch H. Historical survey of infrared and Raman spectroscopy of biological materials. In: Gremlich H. (Ed). Infrared and Raman Spectroscopy of Biological Materials (2001), Marcel Dekker, New York, USA 1-14
    • (2001) Infrared and Raman Spectroscopy of Biological Materials , pp. 1-14
    • Mantsch, H.1
  • 30
    • 0034856845 scopus 로고    scopus 로고
    • Early spread of scrapie from the gastrointestinal tract to the central nervous system involves autonomic fibers of the splanchnic and vagus nerves
    • McBride P.A., Schulz-Schaeffer W.J., Donaldson M., Bruce M., Diringer H., Kretzschmar H.A., and Beekes M. Early spread of scrapie from the gastrointestinal tract to the central nervous system involves autonomic fibers of the splanchnic and vagus nerves. J. Virol. 75 (2001) 9320-9327
    • (2001) J. Virol. , vol.75 , pp. 9320-9327
    • McBride, P.A.1    Schulz-Schaeffer, W.J.2    Donaldson, M.3    Bruce, M.4    Diringer, H.5    Kretzschmar, H.A.6    Beekes, M.7
  • 31
    • 0030569412 scopus 로고    scopus 로고
    • Metal-dependent alpha-helix formation promoted by the glycine-rich octapeptide region of prion protein
    • Miura T., Hori-i A., and Takeuchi H. Metal-dependent alpha-helix formation promoted by the glycine-rich octapeptide region of prion protein. FEBS Lett. 396 (1996) 248-252
    • (1996) FEBS Lett. , vol.396 , pp. 248-252
    • Miura, T.1    Hori-i, A.2    Takeuchi, H.3
  • 32
    • 0005166726 scopus 로고    scopus 로고
    • Infrared spectroscopy in microbiology
    • Meyers R.A. (Ed), John Wiley & Sons, Chichester, UK
    • Naumann D. Infrared spectroscopy in microbiology. In: Meyers R.A. (Ed). Encyclopedia of Analytical Chemistry (2000), John Wiley & Sons, Chichester, UK 102-131
    • (2000) Encyclopedia of Analytical Chemistry , pp. 102-131
    • Naumann, D.1
  • 33
    • 0000764248 scopus 로고    scopus 로고
    • FT-Infrared and FT-Raman spectroscopy in biomedical research
    • Gremlich H.U. (Ed), Marcel Dekker, New York, USA
    • Naumann D. FT-Infrared and FT-Raman spectroscopy in biomedical research. In: Gremlich H.U. (Ed). Infrared and Raman Spectroscopy of Biological Materials (2001), Marcel Dekker, New York, USA 323-377
    • (2001) Infrared and Raman Spectroscopy of Biological Materials , pp. 323-377
    • Naumann, D.1
  • 34
    • 0026413442 scopus 로고
    • Microbiological characterizations by FT-IR spectroscopy
    • Naumann D., Helm D., and Labischinski H. Microbiological characterizations by FT-IR spectroscopy. Nature 351 (1991) 81
    • (1991) Nature , vol.351 , pp. 81
    • Naumann, D.1    Helm, D.2    Labischinski, H.3
  • 35
    • 0842306198 scopus 로고    scopus 로고
    • Characterization and identification of microorganisms by FT-IR microspectrometry
    • Ngo Thi N.A., Kirschner C., and Naumann D. Characterization and identification of microorganisms by FT-IR microspectrometry. J. Mol. Struct. 661-662 (2003) 371-380
    • (2003) J. Mol. Struct. , vol.661-662 , pp. 371-380
    • Ngo Thi, N.A.1    Kirschner, C.2    Naumann, D.3
  • 36
    • 0036158218 scopus 로고    scopus 로고
    • Identification of coryneform bacteria and related taxa by Fourier-transform infrared (FT-IR) spectroscopy
    • Oberreuter H., Seiler H., and Scherer S. Identification of coryneform bacteria and related taxa by Fourier-transform infrared (FT-IR) spectroscopy. Int. J. Syst. Evol. Microbiol. 52 (2002) 91-100
    • (2002) Int. J. Syst. Evol. Microbiol. , vol.52 , pp. 91-100
    • Oberreuter, H.1    Seiler, H.2    Scherer, S.3
  • 38
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • Peden A.H., Head M.W., Ritchie D.L., Bell J.E., and Ironside J.W. Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 364 (2004) 527-529
    • (2004) Lancet , vol.364 , pp. 527-529
    • Peden, A.H.1    Head, M.W.2    Ritchie, D.L.3    Bell, J.E.4    Ironside, J.W.5
  • 39
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 41
    • 0029923896 scopus 로고    scopus 로고
    • The UK epidemic of BSE: slow virus or chronic pesticide-initiated modification of the prion protein? Part 1. Mechanisms for a chemically induced pathogenesis/transmissibility
    • Purdey M. The UK epidemic of BSE: slow virus or chronic pesticide-initiated modification of the prion protein? Part 1. Mechanisms for a chemically induced pathogenesis/transmissibility. Med. Hypotheses 46 (1996) 429-443
    • (1996) Med. Hypotheses , vol.46 , pp. 429-443
    • Purdey, M.1
  • 42
    • 0029968884 scopus 로고    scopus 로고
    • The UK epidemic of BSE: slow virus or chronic pesticide-initiated modification of the prion protein? Part 2. An epidemiological perspective
    • Purdey M. The UK epidemic of BSE: slow virus or chronic pesticide-initiated modification of the prion protein? Part 2. An epidemiological perspective. Med. Hypotheses 46 (1996) 445-454
    • (1996) Med. Hypotheses , vol.46 , pp. 445-454
    • Purdey, M.1
  • 43
    • 0034018313 scopus 로고    scopus 로고
    • Ecosystems supporting clusters of sporadic TSEs demonstrate excesses of the radical-generating divalent cation manganese and deficiencies of antioxidant co factors Cu, Se, Fe, Zn. Does a foreign cation substitution at prion protein's Cu domain initiate TSE?
    • Purdey M. Ecosystems supporting clusters of sporadic TSEs demonstrate excesses of the radical-generating divalent cation manganese and deficiencies of antioxidant co factors Cu, Se, Fe, Zn. Does a foreign cation substitution at prion protein's Cu domain initiate TSE?. Med. Hypotheses 54 (2000) 278-306
    • (2000) Med. Hypotheses , vol.54 , pp. 278-306
    • Purdey, M.1
  • 44
    • 33144464483 scopus 로고    scopus 로고
    • Reliable and rapid identification of Listeria monocytogenes and Listeria species by artificial neural network-based Fourier transform infrared spectroscopy
    • Rebuffo C.A., Schmitt J., Wenning M., von Stetten F., and Scherer S. Reliable and rapid identification of Listeria monocytogenes and Listeria species by artificial neural network-based Fourier transform infrared spectroscopy. Appl. Environ. Microbiol. 72 (2006) 994-1000
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 994-1000
    • Rebuffo, C.A.1    Schmitt, J.2    Wenning, M.3    von Stetten, F.4    Scherer, S.5
  • 45
    • 33745879463 scopus 로고    scopus 로고
    • Presymptomatic detection of prions in blood
    • Saa P., Castilla J., and Soto C. Presymptomatic detection of prions in blood. Science 313 (2006) 92-94
    • (2006) Science , vol.313 , pp. 92-94
    • Saa, P.1    Castilla, J.2    Soto, C.3
  • 49
    • 0036683501 scopus 로고    scopus 로고
    • Identification of scrapie infection from blood serum by Fourier transform infrared spectroscopy
    • Schmitt J., Beekes M., Brauer A., Udelhoven T., Lasch P., and Naumann D. Identification of scrapie infection from blood serum by Fourier transform infrared spectroscopy. Anal. Chem. 74 (2002) 3865-3868
    • (2002) Anal. Chem. , vol.74 , pp. 3865-3868
    • Schmitt, J.1    Beekes, M.2    Brauer, A.3    Udelhoven, T.4    Lasch, P.5    Naumann, D.6
  • 50
    • 33745058355 scopus 로고    scopus 로고
    • Structural differences between TSEs strains investigated by FT-IR spectroscopy
    • Spassov S., Beekes M., and Naumann D. Structural differences between TSEs strains investigated by FT-IR spectroscopy. Biochim. Biophys. Acta 1760 (2006) 1138-1149
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1138-1149
    • Spassov, S.1    Beekes, M.2    Naumann, D.3
  • 52
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • Surewicz W.K., and Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta 952 (1988) 115-130
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 53
    • 4043137988 scopus 로고    scopus 로고
    • Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein
    • Thomzig A., Spassov S., Friedrich M., Naumann D., and Beekes M. Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein. J. Biol. Chem. 279 (2004) 33847-33854
    • (2004) J. Biol. Chem. , vol.279 , pp. 33847-33854
    • Thomzig, A.1    Spassov, S.2    Friedrich, M.3    Naumann, D.4    Beekes, M.5
  • 55
    • 0034294095 scopus 로고    scopus 로고
    • Development of a hierarchical classification system with artificial neural networks and FT-IR spectra for the identification of bacteria
    • Udelhoven T., Naumann D., and Schmitt J. Development of a hierarchical classification system with artificial neural networks and FT-IR spectra for the identification of bacteria. Appl. Spectrosc. 54 (2000) 1471-1479
    • (2000) Appl. Spectrosc. , vol.54 , pp. 1471-1479
    • Udelhoven, T.1    Naumann, D.2    Schmitt, J.3
  • 56
    • 34547103199 scopus 로고    scopus 로고
    • UK Health Protection Agency, 2006. New case of variant CJD associated with blood transfusion. Press Statement 9 February 2006.
  • 57
    • 22144457133 scopus 로고    scopus 로고
    • In situ characterization of prion protein structure and metal accumulation in scrapie-infected cells by synchrotron infrared and X-ray imaging
    • Wang Q., Kretlow A., Beekes M., Naumann D., and Miller L. In situ characterization of prion protein structure and metal accumulation in scrapie-infected cells by synchrotron infrared and X-ray imaging. Vib. Spectrosc. 38 (2005) 61-69
    • (2005) Vib. Spectrosc. , vol.38 , pp. 61-69
    • Wang, Q.1    Kretlow, A.2    Beekes, M.3    Naumann, D.4    Miller, L.5
  • 58
    • 0036795042 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopy, a novel and rapid tool for identification of yeasts
    • Wenning M., Seiler H., and Scherer S. Fourier-transform infrared spectroscopy, a novel and rapid tool for identification of yeasts. Appl. Environ. Microbiol. 68 (2002) 4717-4720
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4717-4720
    • Wenning, M.1    Seiler, H.2    Scherer, S.3
  • 59
    • 16444364685 scopus 로고    scopus 로고
    • Biological applications of infrared microspectroscopy
    • Gremlich H.U. (Ed), Marcel Dekker, New York, USA
    • Wetzel D.L., and Levine S.M. Biological applications of infrared microspectroscopy. In: Gremlich H.U. (Ed). Infrared and Raman Spectroscopy of Biological Materials (2001), Marcel Dekker, New York, USA 101-142
    • (2001) Infrared and Raman Spectroscopy of Biological Materials , pp. 101-142
    • Wetzel, D.L.1    Levine, S.M.2
  • 60
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native-sheet proteins and amyloid fibrils
    • Zandomeneghi G., Krebs M.R.H., McCammon M.G., and Fandrich M. FTIR reveals structural differences between native-sheet proteins and amyloid fibrils. Protein Sci. 13 (2004) 3314-3321
    • (2004) Protein Sci. , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.H.2    McCammon, M.G.3    Fandrich, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.