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Articles

Heating-induced transition of Potyvirus Potato Virus A coat protein into β-structure

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Pages 250-258 | Received 06 Nov 2014, Accepted 10 Feb 2015, Published online: 08 Apr 2015

References

  • Baratova, L. A., Efimov, A. V., Dobrov, E. N., Fedorova, N. V., Hunt, R., Badun, G. A., … Jarvekulg, L. (2001). In situ spatial organization of potato virus A coat protein subunits as assessed by tritium bombardment. Journal of Virology, 75, 9696–9702.10.1128/JVI.75.20.9696-9702.2001
  • Bhak, G., Choe, Y. J., & Paik, S. R. (2009). Mechanism of amyloidogenesis: Nucleation-dependent fibrillation versus double-concerted fibrillation. Biochemistry and Molecular Biology Reports, 30, 541–551.
  • Chiti, F., & Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annual Review of Biochemistry, 75, 333–366.10.1146/annurev.biochem.75.101304.123901
  • Chiti, F., & Dobson, C. M. (2009). Amyloid formation by globular proteins under native conditions. Nature Chemical Biology, 5, 15–22.10.1038/nchembio.131
  • Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003). Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature, 424, 805–808.10.1038/nature01891
  • Conchillo-Solé, O., de Groot, N. S., Avilés, F.X., Vendrell, J., Daura, X., & Ventura, S. (2007). AGGRESCAN: A server for the prediction and evaluation of “hot spots” of aggregation in polypeptides. BMC Bioinformatics, 8, 65–81.10.1186/1471-2105-8-65
  • Cui, X., Wei, T., Chowda-Reddy, R., Sun, G., & Wang, A. (2010). The tobacco etch virus P3 protein forms mobile inclusions via the early secretary pathway and traffics along actin microfilaments. Virology, 397, 56–63.10.1016/j.virol.2009.11.015
  • Dobrov, E., Nikitin, N., Trifonova, E., Parshina, E., Makarov, V., Maksimov, G., … Atabekov, J. (2014). β-structure of the coat protein subunits in spherical particles generated by tobacco mosaic virus thermal denaturation. Journal of Biomolecular Structure and Dynamics, 32, 701–708.
  • Dunker, A. K., Williams, R. W., & Peticolas, W. L. (1979). Ultraviolet and laser Raman investigation of the buried tyrosines in fd phage. Journal of Biological Chemistry, 254, 6444–6448.
  • Eisenberg, D., & Jucker, M. (2012). The amyloid state of proteins in human diseases. Cell, 148, 1188–1203.10.1016/j.cell.2012.02.022
  • El Moustaine, D., Perrier, V., Smeller, L., Lange, R., & Torrent, J. (2009). Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways. FEBS Journal, 275, 2021–2031.
  • Fernandez-Escamilla, A. M., Rousseau, F., Schymkowitz, J., & Serrano, L. (2004). Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nature Biotechnology, 22, 1302–1306.10.1038/nbt1012
  • Fowler, D. M., Koulov, A. V., Balch, W. E., & Kelly, J. W. (2007). Functional amyloid – From bacteria to humans. Trends in Biochemical Sciences, 32, 217–224.10.1016/j.tibs.2007.03.003
  • Goodman, R. M., Horne, R. W., & Hobart, J. M. (1975). Reconstruction of potato virus X in vitro: II Characterization of the reconstituted product. Virology, 68, 299–308.
  • Harrison, R. S., Sharpe, D. C., Singh, Y., & Fairlie, D. P. (2007). Amyloid peptides and proteins in review. Reviews of Physiology Biochemistry and Pharmacology, 159, 1–77.
  • Iconomidou, V. A., & Hamodrakas, S. J. (2008). Natural protective amyloids. Current Protein and Peptide Science, 9, 291–309.10.2174/138920308784534041
  • Kelley, L. A., & Sternberg, M. J. (2009). Protein structure prediction on the web: A case study using the phyre server. Nature Protocols, 4, 363–371.10.1038/nprot.2009.2
  • Kendall, A., McDonald, M., Bian, W., Bowles, T., Baumgarten, S. C., Shi, J., … Stubbs, G. (2008). Structure of flexible filamentous plant viruses. Journal of Virology, 82, 9546–9554.10.1128/JVI.00895-08
  • Ksenofontov, A. L., Kozlovskii, V. S., Kordyukova, L. V., Radyukhin, V. A., Timofeeva, A. V., & Dobrov, E. N. (2006). Determination of concentration and aggregate size in influenza virus preparations from true UV absorption spectra. Molecular Biology, 40, 152–158.10.1134/S0026893306010201
  • Ksenofontov, A. L., Paalme, V., Arutyunyan, A. M., Semenyuk, P. I., Fedorova, N. V., Rumvolt, R., … Dobrov, E. N. (2013). Partially disordered structure in intravirus coat protein of potyvirus potato virus A. PLoS ONE, 8, e67830.10.1371/journal.pone.0067830
  • Laemmli, U. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685.10.1038/227680a0
  • LeVine III, H. (1999). Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods in Enzymology, 309, 274–284.10.1016/S0076-6879(99)09020-5
  • Louis-Jeune, C., Andrade-Navarro, M. A., & Perez-Iratxeta, C. (2012). Prediction of protein secondary structure from circular dichroism using theoretically derived spectra. Proteins: Structure, Function, and Bioinformatics, 80, 374–381.10.1002/prot.v80.2
  • Lukashina, E., Badun, G., Fedorova, N., Ksenofontov, A., Nemykh, M., Serebryakova, M., … Dobrov, E. (2009). Tritium planigraphy study of structural alterations in the coat protein of potato virus X induced by binding of its triple gene block 1 protein to virions. FEBS Journal, 276, 7006–7015.10.1111/j.1742-4658.2009.07408.x
  • Maiti, N. C., Apetri, M. M., Zagorski, M. G., Carey, P. R., & Anderson, V. E. (2004). Raman spectroscopic characterization of secondary structure in natively unfolded proteins: α-synuclein. Journal of the American Chemical Society, 126, 2399–2408.10.1021/ja0356176
  • Makarov, V. V., Skurat, E. V., Semenyuk, P. I., Abashkin, D. A., Kalinina, N. O., Arutyunyan, A. M., … Dobrov, E. N. (2013). Structural lability of barley stripe mosaic virus virions. PLoS ONE, 8, e60942.10.1371/journal.pone.0060942
  • Nilsson, M. R. (2004). Techniques to study amyloid fibril formation in vitro. Methods, 34, 151–160.10.1016/j.ymeth.2004.03.012
  • Schmitz, S. K. (1990). An introduction to dynamic light scattering by macromolecules, ( 449 pp.). New York, NY: Academic Press.
  • Semenova, A. A., Goodilin, E. A., Brazhe, N. A., Ivanov, V. K., Baranchikov, A. E., Lebedev, V. A., & Goldt, A. E. (2012). Planar SERS nanostructures with stochastic silver ring morphology for biosensor chips. Journal of Materials Chemistry, 22, 24530–24544.10.1039/c2jm34686a
  • Seo, J.-K., Vo Phan, M. S. V., Kang, S.-H., Choi, H.-S., & Kim, K.-H. (2013). The charged residues in the surface-exposed C-terminus of the soybean mosaic virus coat protein are critical for cell-to-cell movement. Virology, 446, 95–101.10.1016/j.virol.2013.07.033
  • Sipe, J. D., Benson, M. D., Buxbaum, J. N., Ikeda, S. I., Merlini, G., Saraiva, M. J. M., & Westermark, P. (2010). Amyloid fibril protein nomenclature: 2010 Recommendations from the nomenclature committee of the international society of amyloidosis. Amyloid, 17, 101–104.10.3109/13506129.2010.526812
  • Tatineni, S., Kovacs, F., & French, R. (2014). Wheat streak mosaic virus infects systemically despite extensive coat protein deletions: Identification of virion assembly and cell-to-cell movement determinants. Journal of Virology, 88, 1366–1380.10.1128/JVI.02737-13
  • Thomas, G., & Day, L. A. (1981). Conformational transitions in Pf3 and their implications for the structure and assembly of filamentous bacterial viruses. Proceedings of the National Academy of Sciences, 78, 2962–2966.10.1073/pnas.78.5.2962
  • Tsolis, A. C., Papandreou, N. C., Iconomidou, V. A., & Hamodrakas, S. J. (2013). A consensus method for the prediction of ‘aggregation-prone’ peptides in globular proteins. PLoS ONE, 8, e54175.10.1371/journal.pone.0054175
  • Uversky, V. N. (2010). Mysterious oligomerization of the amyloidogenic proteins. FEBS Journal, 277, 2940–2953.10.1111/j.1742-4658.2010.07721.x
  • van der Wel, P. C. A., Lewandowski, J. R., & Griffin, R. G. (2010). Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR. Biochemistry, 49, 9457–9469.10.1021/bi100077x
  • Yang, S., Wang, T., Bohon, J., Gagné, M.-E. L., Bolduc, M., Leclerc, D., & Li, H. (2012). Crystal structure of the coat protein of the flexible filamentous papaya mosaic virus. Journal of Molecular Biology, 422, 263–273.10.1016/j.jmb.2012.05.032
  • Zheng, R., Zheng, X., Dong, J., & Carey, P. R. (2004). Proteins can convert to β-sheet in single crystals. Protein Science, 13, 1288–1294.10.1110/ps.03550404

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