43 research outputs found

    The Influence of Thermal Crosslinking on Solubility of Films Prepared from Collagen Hydrolysate

    Get PDF
    The presented work describes a method of utilizing collagen hydrolysate obtained through enzymatic hydrolysis of chrome-tanned shavings for preparing biodegradable films. Films were prepared by casting from a solution of collagen hydrolysate with added plasticizer (glycerol) and cross-linking agent (starch dialdehyde). Films thus prepared were subjected to thermal annealing at 60, 70, 80 and 90 oC for 24 hours. Thermal annealing is a mode of physical cross-linking of biodegradable films. The work studied effect of thermal crosslinking on film solubility. Solubility curves are important for applying biodegradable films in industrial practice. Thermal annealing was found to affect the cross-linking degree of prepared film in significant manner, hence, also, its solubility. Results indicate that collagen hydrolysate, following certain modification by plasticizer and cross-linking agent is capable of producing films whose properties may be additionally modified.RESUMEN: El trabajo presentado describe un método para utilizar una solución de un hidrolizado colagénico por hidrólisis enzimática de rebajaduras de cuero al cromo en la preparación de películas biodegradables. Películas fueron preparadas por vaciado desde una solución del hidrolizado colagénico con un plastificante añadido (glicerina) y un agente reticulante (almidón dialdehídico). Las películas así preparadas fueron sometidas a un fraguado térmico de 60, 70, y 90ºC durante 24 horas. Fraguado térmico es un método de reticulación de películas biodegradables. El trabajo estudió el efecto del fraguado térmico sobre la propiedad de solubilidad de la película. Curvas de solubilidad son importantes en las prácticas de aplicación industrial de películas biodegradables. El fraguado térmico, se encontró que afecta en forma significante el grado de reticulación de las películas así preparadas, luego entonces, su solubilidad. Resultados indican que el hidrolizado de colágeno, con consiguientes modificaciones por plastificante y agente reticulante, es capaz de producir películas cuyas propiedades pueden ser adicionalmente modificadas

    ‘No memory, no desire’: psychoanalysis in Brazil during repressive times

    Get PDF
    Until recently, the growth and significance of Brazilian psychoanalysis has been neglected in histories of psychoanalysis. Not only is this history long and rich in its professional and cultural dimensions, but there was an especially important ‘event’ – the so-called ‘Cabernite-Lobo affair’ – that took place during the period of the military dictatorship, which can be seen as dramatising some of the issues concerning the erasure of memory in psychoanalysis, especially in connection with political difficulties. In this paper, we provide an outline of the origins and dissemination of psychoanalysis in Brazil before looking again at the Cabernite-Lobo affair in order to examine in a situated way how psychoanalysis engages with political extremism, and particularly to explore the consequences of an unthinking generalisation of the idea of ‘neutrality’ from the consulting room to the institutional setting. We draw especially on Brazilian papers in Portuguese, which have not been accessible in the English-language psychoanalytic literature

    An Internal Ribosome Entry Site Directs Translation of the 39-Gene from Pelargonium Flower Break Virus Genomic RNA: Implications for Infectivity

    Get PDF
    [EN] Pelargonium flower break virus (PFBV, genus Carmovirus) has a single-stranded positive-sense genomic RNA (gRNA) which contains five ORFs. The two 59-proximal ORFs encode the replicases, two internal ORFs encode movement proteins, and the 39-proximal ORF encodes a polypeptide (p37) which plays a dual role as capsid protein and as suppressor of RNA silencing. Like other members of family Tombusviridae, carmoviruses express ORFs that are not 59-proximal from subgenomic RNAs. However, in one case, corresponding to Hisbiscus chlorotic ringspot virus, it has been reported that the 39-proximal gene can be translated from the gRNA through an internal ribosome entry site (IRES). Here we show that PFBV also holds an IRES that mediates production of p37 from the gRNA, raising the question of whether this translation strategy may be conserved in the genus. The PFBV IRES was functional both in vitro and in vivo and either in the viral context or when inserted into synthetic bicistronic constructs. Through deletion and mutagenesis studies we have found that the IRES is contained within a 80 nt segment and have identified some structural traits that influence IRES function. Interestingly, mutations that diminish IRES activity strongly reduced the infectivity of the virus while the progress of the infection was favoured by mutations potentiating such activity. These results support the biological significance of the IRES-driven p37 translation and suggest that production of the silencing suppressor from the gRNA might allow the virus to early counteract the defence response of the host, thus facilitating pathogen multiplication and spread.This research was supported by grants BFU2006-11230 and BFU2009-11699 from the Spanish Ministerio de Ciencia e Innovacion (MICINN) and by grants ACOM/2006/210 and ACOMP/2009/040 (to CH) and GVPRE/2008/121 (to OF-M) from the Generalitat Valenciana. The latter was the recipient of an I3P postdoctoral contract from the Spanish Consejo Superior de Investigaciones Cientificas and an additional contract from MICINN. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Fernandez Miragall, O.; Hernandez Fort, C. (2011). An Internal Ribosome Entry Site Directs Translation of the 39-Gene from Pelargonium Flower Break Virus Genomic RNA: Implications for Infectivity. PLoS ONE. 6(7):22617-22617. https://doi.org/10.1371/journal.pone.0022617S226172261767Gallie, D. R. (1996). Translational control of cellular and viral mRNAs. Plant Molecular Biology, 32(1-2), 145-158. doi:10.1007/bf00039381Kozak, M. (2002). Pushing the limits of the scanning mechanism for initiation of translation. Gene, 299(1-2), 1-34. doi:10.1016/s0378-1119(02)01056-9Sachs, A. B., Sarnow, P., & Hentze, M. W. (1997). Starting at the Beginning, Middle, and End: Translation Initiation in Eukaryotes. Cell, 89(6), 831-838. doi:10.1016/s0092-8674(00)80268-8Kozak, M. (1992). Regulation of Translation in Eukaryotic Systems. Annual Review of Cell Biology, 8(1), 197-225. doi:10.1146/annurev.cb.08.110192.001213Sonenberg, N., & Hinnebusch, A. G. (2009). Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets. Cell, 136(4), 731-745. doi:10.1016/j.cell.2009.01.042F�tterer, J., & Hohn, T. (1996). Translation in plants-rules and exceptions. Plant Molecular Biology, 32(1-2), 159-189. doi:10.1007/bf00039382Gale, M., Tan, S.-L., & Katze, M. G. (2000). Translational Control of Viral Gene Expression in Eukaryotes. Microbiology and Molecular Biology Reviews, 64(2), 239-280. doi:10.1128/mmbr.64.2.239-280.2000Kozak, M. (2001). Constraints on reinitiation of translation in mammals. Nucleic Acids Research, 29(24), 5226-5232. doi:10.1093/nar/29.24.5226Pelletier, J., & Sonenberg, N. (1988). Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature, 334(6180), 320-325. doi:10.1038/334320a0Mokrejš, M., Mašek, T., Vopálenský, V., Hlubuček, P., Delbos, P., & Pospíšek, M. (2009). IRESite—a tool for the examination of viral and cellular internal ribosome entry sites. Nucleic Acids Research, 38(suppl_1), D131-D136. doi:10.1093/nar/gkp981Basso, J., Dallaire, P., Charest, P. J., Devantier, Y., & Laliberte, J.-F. (1994). Evidence for an Internal Ribosome Entry Site Within the 5’ Non-translated Region of Turnip Mosaic Potyvirus RNA. Journal of General Virology, 75(11), 3157-3165. doi:10.1099/0022-1317-75-11-3157Levis, C., & Astier-Manifacier, S. (1993). The 5′ untranslated region of PVY RNA, even located in an internal position, enables initiation of translation. Virus Genes, 7(4), 367-379. doi:10.1007/bf01703392Karetnikov, A., & Lehto, K. (2007). The RNA2 5’ leader of Blackcurrant reversion virus mediates efficient in vivo translation through an internal ribosomal entry site mechanism. Journal of General Virology, 88(1), 286-297. doi:10.1099/vir.0.82307-0Ivanov, P. A., Karpova, O. V., Skulachev, M. V., Tomashevskaya, O. L., Rodionova, N. P., Dorokhov, Y. L., & Atabekov, J. G. (1997). A Tobamovirus Genome That Contains an Internal Ribosome Entry Site Functionalin Vitro. Virology, 232(1), 32-43. doi:10.1006/viro.1997.8525Skulachev, M. V., Ivanov, P. A., Karpova, O. V., Korpela, T., Rodionova, N. P., Dorokhov, Y. L., & Atabekov, J. G. (1999). Internal Initiation of Translation Directed by the 5′-Untranslated Region of the Tobamovirus Subgenomic RNA I2. Virology, 263(1), 139-154. doi:10.1006/viro.1999.9928Jaag, H. M., Kawchuk, L., Rohde, W., Fischer, R., Emans, N., & Prufer, D. (2003). An unusual internal ribosomal entry site of inverted symmetry directs expression of a potato leafroll polerovirus replication-associated protein. Proceedings of the National Academy of Sciences, 100(15), 8939-8944. doi:10.1073/pnas.1332697100Balvay, L., Rifo, R. S., Ricci, E. P., Decimo, D., & Ohlmann, T. (2009). Structural and functional diversity of viral IRESes. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 1789(9-10), 542-557. doi:10.1016/j.bbagrm.2009.07.005Kneller, E. L. P., Rakotondrafara, A. M., & Miller, W. A. (2006). Cap-independent translation of plant viral RNAs. Virus Research, 119(1), 63-75. doi:10.1016/j.virusres.2005.10.010Rico, P., & Hern�ndez, C. (2004). Complete nucleotide sequence and genome organization of Pelargonium flower break virus. Archives of Virology, 149(3), 641-651. doi:10.1007/s00705-003-0231-5Martinez-Turino, S., & Hernandez, C. (2010). Identification and characterization of RNA-binding activity in the ORF1-encoded replicase protein of Pelargonium flower break virus. Journal of General Virology, 91(12), 3075-3084. doi:10.1099/vir.0.023093-0Martínez-Turiño, S., & Hernández, C. (2011). A membrane-associated movement protein of Pelargonium flower break virus shows RNA-binding activity and contains a biologically relevant leucine zipper-like motif. Virology, 413(2), 310-319. doi:10.1016/j.virol.2011.03.001Martinez-Turino, S., & Hernandez, C. (2009). Inhibition of RNA silencing by the coat protein of Pelargonium flower break virus: distinctions from closely related suppressors. Journal of General Virology, 90(2), 519-525. doi:10.1099/vir.0.006098-0Rico, P., & Hernández, C. (2009). Characterization of the subgenomic RNAs produced by Pelargonium flower break virus: Identification of two novel RNAs species. Virus Research, 142(1-2), 100-107. doi:10.1016/j.virusres.2009.01.018Koh, D. C.-Y., Wong, S.-M., & Liu, D. X. (2003). Synergism of the 3′-Untranslated Region and an Internal Ribosome Entry Site Differentially Enhances the Translation of a Plant Virus Coat Protein. Journal of Biological Chemistry, 278(23), 20565-20573. doi:10.1074/jbc.m210212200Hellen, C. U. T. (2001). Internal ribosome entry sites in eukaryotic mRNA molecules. Genes & Development, 15(13), 1593-1612. doi:10.1101/gad.891101Martínez-Salas, E. (1999). Internal ribosome entry site biology and its use in expression vectors. Current Opinion in Biotechnology, 10(5), 458-464. doi:10.1016/s0958-1669(99)00010-5Dobrikova, E., Florez, P., Bradrick, S., & Gromeier, M. (2003). Activity of a type 1 picornavirus internal ribosomal entry site is determined by sequences within the 3’ nontranslated region. Proceedings of the National Academy of Sciences, 100(25), 15125-15130. doi:10.1073/pnas.2436464100Belsham, G. J. (2009). Divergent picornavirus IRES elements. Virus Research, 139(2), 183-192. doi:10.1016/j.virusres.2008.07.001Fernández-Miragall, O., Quinto, S. L. de, & Martínez-Salas, E. (2009). Relevance of RNA structure for the activity of picornavirus IRES elements. Virus Research, 139(2), 172-182. doi:10.1016/j.virusres.2008.07.009Pestova, T. V., Kolupaeva, V. G., Lomakin, I. B., Pilipenko, E. V., Shatsky, I. N., Agol, V. I., & Hellen, C. U. T. (2001). Molecular mechanisms of translation initiation in eukaryotes. Proceedings of the National Academy of Sciences, 98(13), 7029-7036. doi:10.1073/pnas.111145798FERNANDEZ-MIRAGALL, O. (2003). Structural organization of a viral IRES depends on the integrity of the GNRA motif. RNA, 9(11), 1333-1344. doi:10.1261/rna.5950603ROBERTSON, M. E. M., SEAMONS, R. A., & BELSHAM, G. J. (1999). A selection system for functional internal ribosome entry site (IRES) elements: Analysis of the requirement for a conserved GNRA tetraloop in the encephalomyocarditis virus IRES. RNA, 5(9), 1167-1179. doi:10.1017/s1355838299990301Dorokhov, Y. L., Skulachev, M. V., Ivanov, P. A., Zvereva, S. D., Tjulkina, L. G., Merits, A., … Atabekov, J. G. (2002). Polypurine (A)-rich sequences promote cross-kingdom conservation of internal ribosome entry. Proceedings of the National Academy of Sciences, 99(8), 5301-5306. doi:10.1073/pnas.082107599Xia, X., & Holcik, M. (2009). Strong Eukaryotic IRESs Have Weak Secondary Structure. PLoS ONE, 4(1), e4136. doi:10.1371/journal.pone.0004136Lu, J., Zhang, J., Wang, X., Jiang, H., Liu, C., & Hu, Y. (2006). In vitro and in vivo identification of structural and sequence elements in the 5’ untranslated region of Ectropis obliqua picorna-like virus required for internal initiation. Journal of General Virology, 87(12), 3667-3677. doi:10.1099/vir.0.82090-0Yang, L. J., Hidaka, M., Sonoda, J., Masaki, H., & Uozumi, T. (1997). Mutational Analysis of the Potato Virus Y 5′ Untranslated Region for Alteration in Translational Enhancement in Tobacco Protoplasts. Bioscience, Biotechnology, and Biochemistry, 61(12), 2131-2133. doi:10.1271/bbb.61.2131BERGAMINI, G., PREISS, T., & HENTZE, M. W. (2000). Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system. RNA, 6(12), 1781-1790. doi:10.1017/s1355838200001679Bradrick, S. S. (2006). The hepatitis C virus 3’-untranslated region or a poly(A) tract promote efficient translation subsequent to the initiation phase. Nucleic Acids Research, 34(4), 1293-1303. doi:10.1093/nar/gkl019Lopez de Quinto, S. (2002). IRES-driven translation is stimulated separately by the FMDV 3’-NCR and poly(A) sequences. Nucleic Acids Research, 30(20), 4398-4405. doi:10.1093/nar/gkf569Song, Y., Friebe, P., Tzima, E., Junemann, C., Bartenschlager, R., & Niepmann, M. (2006). The Hepatitis C Virus RNA 3’-Untranslated Region Strongly Enhances Translation Directed by the Internal Ribosome Entry Site. Journal of Virology, 80(23), 11579-11588. doi:10.1128/jvi.00675-06Koh, D. C.-Y., Liu, D. X., & Wong, S.-M. (2002). A Six-Nucleotide Segment within the 3’ Untranslated Region of Hibiscus Chlorotic Ringspot Virus Plays an Essential Role in Translational Enhancement. Journal of Virology, 76(3), 1144-1153. doi:10.1128/jvi.76.3.1144-1153.2002Stupina, V. A., Meskauskas, A., McCormack, J. C., Yingling, Y. G., Shapiro, B. A., Dinman, J. D., & Simon, A. E. (2008). The 3’ proximal translational enhancer of Turnip crinkle virus binds to 60S ribosomal subunits. RNA, 14(11), 2379-2393. doi:10.1261/rna.1227808Truniger, V., Nieto, C., González-Ibeas, D., & Aranda, M. (2008). Mechanism of plant eIF4E-mediated resistance against a Carmovirus (Tombusviridae): cap-independent translation of a viral RNA controlledin cisby an (a)virulence determinant. The Plant Journal, 56(5), 716-727. doi:10.1111/j.1365-313x.2008.03630.xMiller, W. A., Wang, Z., & Treder, K. (2007). The amazing diversity of cap-independent translation elements in the 3′-untranslated regions of plant viral RNAs. Biochemical Society Transactions, 35(6), 1629-1633. doi:10.1042/bst0351629Miller, W. A., & White, K. A. (2006). Long-Distance RNA-RNA Interactions in Plant Virus Gene Expression and Replication. Annual Review of Phytopathology, 44(1), 447-467. doi:10.1146/annurev.phyto.44.070505.143353Koh, D. C.-Y., Wang, X., Wong, S.-M., & Liu, D. X. (2006). Translation initiation at an upstream CUG codon regulates the expression of Hibiscus chlorotic ringspot virus coat protein. Virus Research, 122(1-2), 35-44. doi:10.1016/j.virusres.2006.06.008Castaño, A., Ruiz, L., & Hernández, C. (2009). Insights into the translational regulation of biologically active open reading frames of Pelargonium line pattern virus. Virology, 386(2), 417-426. doi:10.1016/j.virol.2009.01.017Fraser, C. S., & Doudna, J. A. (2006). Structural and mechanistic insights into hepatitis C viral translation initiation. Nature Reviews Microbiology, 5(1), 29-38. doi:10.1038/nrmicro1558LÓPEZ-LASTRA, M., RIVAS, A., & BARRÍA, M. I. (2005). Protein synthesis in eukaryotes: The growing biological relevance of cap-independent translation initiation. Biological Research, 38(2-3). doi:10.4067/s0716-97602005000200003Pacheco, A., & Martinez-Salas, E. (2010). Insights into the Biology of IRES Elements through Riboproteomic Approaches. Journal of Biomedicine and Biotechnology, 2010, 1-12. doi:10.1155/2010/458927Bernstein, J., Sella, O., Le, S.-Y., & Elroy-Stein, O. (1997). PDGF2/c-sismRNA Leader Contains a Differentiation-linked Internal Ribosomal Entry Site (D-IRES). Journal of Biological Chemistry, 272(14), 9356-9362. doi:10.1074/jbc.272.14.9356Scheper, G. C., Voorma, H. O., & Thomas, A. A. M. (1994). Basepairing with 18S ribosomal RNA in internal initiation of translation. FEBS Letters, 352(3), 271-275. doi:10.1016/0014-5793(94)00975-9Dresios, J., Chappell, S. A., Zhou, W., & Mauro, V. P. (2005). An mRNA-rRNA base-pairing mechanism for translation initiation in eukaryotes. Nature Structural & Molecular Biology, 13(1), 30-34. doi:10.1038/nsmb1031Reigadas, S., Pacheco, A., Ramajo, J., de Quinto, S. L., & Martinez-Salas, E. (2005). Specific interference between two unrelated internal ribosome entry site elements impairs translation efficiency. FEBS Letters, 579(30), 6803-6808. doi:10.1016/j.febslet.2005.11.015Ishitani, M., Xiong, L., Stevenson, B., & Zhu, J. K. (1997). Genetic analysis of osmotic and cold stress signal transduction in Arabidopsis: interactions and convergence of abscisic acid-dependent and abscisic acid-independent pathways. The Plant Cell, 9(11), 1935-1949. doi:10.1105/tpc.9.11.1935Knoester, M., van Loon, L. C., van den Heuvel, J., Hennig, J., Bol, J. F., & Linthorst, H. J. M. (1998). Ethylene-insensitive tobacco lacks nonhost resistance against soil-borne fungi. Proceedings of the National Academy of Sciences, 95(4), 1933-1937. doi:10.1073/pnas.95.4.1933Mathews, D. H., Sabina, J., Zuker, M., & Turner, D. H. (1999). Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. Journal of Molecular Biology, 288(5), 911-940. doi:10.1006/jmbi.1999.2700Zuker, M. (2003). Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Research, 31(13), 3406-3415. doi:10.1093/nar/gkg59

    Heat-treated biodegradable films and foils of collagen hydrolysate crosslinked with dialdehyde starch

    No full text

    Bioconversion of waste sheep wool to microbial peptone by Bacillus licheniformis

    No full text
    Peptones are among the most expensive culture components used in the cultivation of microorganisms. This study was performed to prepare a protein hydrolysate from sheep wool using a locally isolated keratinolytic bacterium Bacillus licheniformis EY2 (GenBank: MN809476), and to investigate the usability of the prepared hydrolysate as a peptone in a microbial medium. The optimum pH, temperature, and incubation time for wool hydrolysis and keratinolytic activity were determined as 7.0, 55 degrees C, and 6 days, respectively. Optimum concentrations of KH(2)PO4, MgSO4, and NaCl were determined as 1.5, 0.5, and 2 g/L, respectively. After the prepared hydrolysate was partially purified, it was converted to wool peptone (WP). The total protein, ash, carbohydrate, and lipid content of WP was found to be 82.7, 7.2, 0.1, and 0.2 g/100 g, respectively. Fourier transform infrared (FTIR) analysis of WP confirmed the formation of sulfoxide bonds (S=O), which indicated the breaking of disulfide bonds. When compared with commercial tryptone peptone (TP), WP was found to be superior for the cell growth performances of Esherichia coli, Bacillus subtilis, Staphylococcus aureus, Lactobacillus plantarum, Pediococcus pentosaceus, Candia albicans and Aspergillus niger. A protein hydrolysate (including wool protein hydrolysate) prepared via microbial hydrolysis was tested for the first time as a peptone source. The cost of WP is much lower than commercial peptones. At the same time, the method developed offers an environmentally friendly approach for the reduction of the amount of unutilized or waste sheep wool. (c) 2021 Society of Industrial Chemistry and John Wiley & Sons Ltd
    corecore