The cultivation of Castanea sativa (Mill.) in Europe, from its origin to its diffusion on a continental scale

The history of Castanea sativa (sweet chestnut) cultivation since medieval times has been well described on the basis of the very rich documentation available. Far fewer attempts have been made to give a historical synthesis of the events that led to the cultivation of sweet chestnut in much earlier times. In this article we attempt to reconstruct this part of the European history of chestnut cultivation and its early diffusion by use of different sources of information, such as pollen studies, archaeology, history and literature. Using this multidisciplinary approach, we have tried to identify the roles of the Greek and Roman civilizations in the dissemination of chestnut cultivation on a European scale. In particular, we show that use of the chestnut for food was not the primary driving force behind the introduction of the tree into Europe by the Romans. Apart from the Insubrian Region in the north of the Italian peninsula, no other centre of chestnut cultivation existed in Europe during the Roman period. The Romans may have introduced the idea of systematically cultivating and using chestnut. In certain cases they introduced the species itself; however no evidence of systematic planting of chestnut exists. The greatest interest in the management of chestnut for fruit production most probably developed after the Roman period and can be associated with the socio-economic structures of medieval times. It was then that self-sufficient cultures based on the cultivation of chestnut as a source of subsistence were forme

Interactions between Saccharomyces and Oenococcus oeni strains from Amarone wine affect malolactic fermentation and wine composition

Research Note

Mapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras.

The troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. On the other hand the TnI inhibitory and C-terminal domains were completely digested by trypsin in the absence of calcium while the addition of calcium results in the protection of only residues 114137

Small Angle X-ray Scattering From Lipid-bound Myelin Basic Protein In Solution

The structure of myelin basic protein (MBP), purified from the myelin sheath in both lipid-free (LF-MBP) and lipid-bound (LB-MBP) forms, was investigated in solution by small angle x-ray scattering. The water-soluble LF-MBP, extracted at pH 7.0. Under all conditions, the scattering from the two protein forms was different, indicating different molecular shapes. For the LB-MBP, well-defined scattering curves were obtained, suggesting that the protein had a unique, compact (but not globular) structure. Furthermore, these data were compatible with earlier results from molecular modeling calculations on the MBP structure which have been refined by us. In contrast, the LF-MBP data were in accordance with the expected open-coil conformation. The results represent the first direct structural information from x-ray scattering measurements on MBP in its native lipidic environment in solution.861 I455460Altschul, S.F., Madden, T.L., Schäffer, A.A.Z.J., Zhang, Z., Miller, W., Gapped, L.D.J., BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Res., 25, pp. 3389-3402Alvord, E.C., Kies, M.W., Suckling, A.L., (1984) Experimental Allergic Encephalomyelitis: A Useful Model for Multiple Sclerosis, , Alan R. Liss Inc., New YorkBates, I.R., Harauz, G., Molecular dynamics exposes α-helices in myelin basic protein (2003) J. Mol. Mod., , published online 24 July 2003Beniac, D.R., Luckevich, M.D., Czamota, G.J., Tompkins, T.A., Ridsdale, R.A., Ottensmeyer, F.P., Moscarello, M.A., Harauz, G., Three-dimensional structure of myelin basic protein. I. Reconstruction via angular reconstitution of randomly oriented single particles (1997) J. Biol. Chem., 272, pp. 4261-4268Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N., Bourne, P.E., The Protein Data Bank (2000) Nucleic Acids Res., 28, pp. 235-242Bobba, A., Munno, I., Greco, B., Pellegrino, N.M., Riccio, P., Jirillo, E., Quagliariello, E., On the spontaneous adherence of myelin basic protein to T-lymphocytes (1991) Biochem. Biophys. Res. Commun., 180, pp. 1125-1129Boggs, J.M., Moscarello, M.A., Papahadiopolos, D., Structural organization of myelin-role of lipid-protein interactions determined in model systems (1982) Lipid-Protein Interactions, 2, pp. 1-51. , P. C. Jost and O. H. Griffith, editors. Wiley & Sons, New YorkDeibler, G., Martenson, R.E., Kies, M.W., Large-scale preparation of myelin basic protein from central nervous tissue of several mammalian species (1972) Prep. Biochem., 2, pp. 139-165Deibler, G.E., Boyd, L.F., Kies, M.W., Proteolytic activity associated with purified myelin basic protein (1984) Experimental Allergic Encephalomyelitis: A Useful Model for Multiple Sclerosis, pp. 249-256. , E. C. Alvord Jr., M. W. Kies, and A. J. Suckling, editors. Liss, New YorkEpand, R.M., Moscarello, M.A., Zierenberg, B., Vail, W.J., The folded conformation of the encephalogenic protein of the human brain (1974) Biochemistry, 13, pp. 1264-1267Garavito, R.M., Ferguson-Miller, S., Detergents as tools in membrane biochemistry (2001) J. Biol. Chem., 276, pp. 32403-32406Glatter, O., Convolution square root of band-limited symmetrical functions and its applications to small-angle scattering data (1981) J. Appl. Crystallogr., 14, pp. 101-108Gow, A., Smith, R., The thermodynamically stable state of myelin basic protein in solution is a flexible coil (1989) Biochem. J., 257, pp. 535-540Guinier, A., Fournet, G., (1955) Small-Angle Scattering of X-Rays, , Wiley & Sons, New YorkHaas, H., Torrielli, M., Steitz, R., Cavatorta, P., Sorbi, R., Riccio, P., Gliozzi, A., Myelin model membranes on solid substrate (1998) Thin Sol. Films, 327-329, pp. 627-631Kellermann, G., Vicentin, E., Tamura, E., Rocha, M., Tolentino, H., Barbosa, A., Craievich, A., Torriani, I., The small-angle x-ray scattering beamline of the Brazilian Synchrotron Light Laboratory (1997) J. Appl. Crystallogr., 30, pp. 880-883Kirschner, D.A., Blaurock, A.E., Organization, phylogenetic variations and dynamic transitions of myelin (1992) Myelin: Biology and Chemistry, pp. 3-78. , R. E. Martenson, editor. CRC Press, Boca Raton, FLKrigbaum, W.R., Hsu, T.S., Molecular conformation of bovine A1 basic protein, a coiling macromolecule in aqueous solution (1975) Biochemistry, 14, pp. 2542-2546Liebes, L.F., Zand, R., Phillips, W.D., Solution behavior, circular dichroism and 22 MHz PMR studies of the bovine myelin basic protein (1975) Biochim. Biophys. Acta, 405, pp. 27-39Liuzzi, G.M., Tamborra, R., Ventola, A., Bisaccia, F., Quagliariello, E., Riccio, P., Different recognition by clostripain of myelin basic protein in the lipid-bound and lipid-free forms (1996) Biochem. Biophys. Res. Commun., 226, pp. 566-571Lolli, F., Liuzzi, G.M., Vergelli, M., Massacesi, L., Ballerini, C., Amaducci, L., Riccio, P., Antibodies specific for the lipid-bound form of myelin basic protein during experimental autoimmune encephalomyelitis (1993) J. Neuroimmunol., 44, pp. 69-76Massacesi, L., Vergelli, M., Zehetbauer, B., Liuzzi, G.M., Olivotto, J., Ballerini, C., Uccelli, A., Amaducci, L., Induction of the autoimmune encephalomyelitis in rats and immune response to myelin basic protein in lipid bound form (1993) J. Neurol. Sci., 119, pp. 91-98Mazzanti, B., Vergelli, M., Riccio, P., Martin, R., McFarland, H.F., Liuzzi, M.G., Amaducci, L., Massacesi, L., T-cell response to myelin basic protein and lipid-bound myelin basic protein in patients with Multiple Sclerosis and health donors (1998) J. Neuroimmunol., 82, pp. 96-100Moscarello, M.A., Evolving biological concepts and therapeutic approaches (1996) Cell Biology and Pathology of Myelin, , R. M. Devon, R. Doucette, B. H. J. Juurlink, A. J. Nazarali, D. J. Schreyer, and V. M. K. Verge, editors. Plenum Publishing, New YorkOliveira, C.L.P., Dos Santos, D.R., Kellermann, G., Plivelic, T., Torriani, I.L., Data treatment program for the SAXS beamline (1997) LNLS Technical Note, , unpublished, available for beam line usersPerkins, J.P., X-ray and neutron solution scattering (1988) Modern Physical Methods in Biochemistry, Part B, pp. 134-265. , A. Neuberger and L. L. M. van Deenen, editors. Elsevier, Amsterdam, The NetherlandsPolverini, E., Fasano, A., Zito, F., Riccio, P., Cavatorta, P., Conformation of bovine myelin basic protein purified with bound lipids (1999) Eur. Biophys. J., 28, pp. 351-355Readhead, C., Popko, B., Takahashi, N., Shine, H.D., Saavedra, R.A., Sidman, R.L., Hood, L., Expression of a myelin basic protein gene in transgenic mice: Correlation of the dismyelinating phenotype (1987) Cell, 48, pp. 703-712Riccio, P., Rosenbusch, J.P., Quagliarello, E., A new procedure to isolate brain myelin basic protein in a lipid-bound form (1984) FEBS Lett., 177, pp. 236-240Riccio, P., Masotti, L., Cavatorta, P., De Santis, A., Juretic, D., Bobba, A., Pasquali-Ronchetti, I., Quagliariello, E., Myelin basic protein ability to organize lipid bilayers: Structural transitions in bilayers of lysophosphatidylcholine micelles (1986) Biochem. Biophys. Res. Commun., 134, pp. 313-319Riccio, P., Quagliariello, E., Lipid-bound, native-like, myelin basic protein: A well-known protein in a new guise, or an unlikely story? (1993) J. Neurochem., 61, pp. 787-788Riccio, P., Bobba, A., Romito, E., Minetola, M., Quagliariello, E., A new detergent to purify CNS myelin basic protein isoforms in lipid-bound form (1994) Neuroreport, 24, pp. 689-692Riccio, P., Fasano, A., Borenshtein, N., Bleve-Zacheo, T., Kirschner, D.A., Multilamellar packing of myelin modeled by lipid-bound MBP (2000) J. Neurosci. Res., 59, pp. 513-521Ridsdale, R.A., Beniac, D.R., Tompkins, T.A., Moscarello, M.A., Harauz, G., Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis (1997) J. Biol. Chem., 272, pp. 4269-4275Rosenbusch, J.P., Stability of membrane proteins: Relevance for the selection of appropriate methods for high-resolution structure determinations (2001) J. Struct. Biol., 136, pp. 144-157Semenyuk, V., Svergun, D.I., GNOM - A program package for small angle scattering data processing (1991) J. Appl. Crystallogr., 24, pp. 537-540Smith, R., Self-association of myelin basic protein: Enhancement by detergents and lipids (1982) Biochemistry, 12, pp. 2697-2701Smith, R., The basic protein of CNS myelin: Its structure and ligand binding (1992) J. Neurochem., 59, pp. 1589-1608Staugaitis, S.M., Colman, D.R., Pedraza, L., Membrane adhesion and other functions for the myelin basic proteins (1996) Bioessays, 18, pp. 13-18Stoffel, W., The myelin membrane of the central nervous system-essential macromolecular structure and function (1990) Angew. Chem. Int. Ed. Engl., 29, pp. 958-976Svergun, D.I., Petoukhov, M.V., Koch, M.H.J., Determination of domain structure of proteins from x-ray solution scattering (2001) Biophys. J., 80, pp. 2946-2953Vergelli, M., Pinet, V., Vogt, A.B., Kalbus, M., Malnati, M., Riccio, P., Long, E.O., Martin, R., HLA-DR-restricted presentation of purified myelin basic protein is independent of intracellular processing (1997) Eur. J. Immunol., 27, pp. 941-951Vriend, G., WHAT IF: A molecular modeling and drug design program (1990) J. Mol. Graph., 8, pp. 52-5

Early changes in inflammatory and pro-thrombotic biomarkers in patients initiating antiretroviral therapy with abacavir or tenofovir

<p>Abstract</p> <p>Background</p> <p>Abacavir has been associated with an increased risk of acute myocardial infarction, but the pathogenic mechanisms remain unknown. We evaluated longitudinal changes in pro-atherosclerotic biomarkers in patients initiating abacavir or tenofovir.</p> <p>Methods</p> <p>Consecutive patients initiating antiretroviral therapy (ART) with abacavir/lamivudine or tenofovir/emtricitabine were included. Plasma levels of high sensitivity C reactive protein (hsCRP), interleukin-6 (IL-6), intercellular adhesion molecule-1, vascular cell adhesion molecule-1 (sVCAM-1) and plasminogen activator inhibitor-1 (PAI-1) were measured at baseline and at different time points throughout 48 weeks. Comparisons were adjusted for age, sex, ART status at inclusion, viral load, lipodystrophy, Framingham score and hepatitis C virus co-infection status.</p> <p>Results</p> <p>50 patients were analyzed, 28 initiating abacavir and 22 tenofovir. The endothelial biomarker sVCAM-1 declined significantly in both treatment groups. hsCRP tended to increase soon after starting therapy with abacavir, a trend that was not seen in those initiating tenofovir. IL-6 significantly increased only at week 24 from baseline in patients on abacavir (+225%, p < 0.01) although the differences were not significant between groups. The procoagulant biomarker PAI-1 plasma levels increased from baseline at week 12 (+57%; p = 0.017), week 24 (+72%; p = 0.008), and week 48 (+149%; p < 0.001) in patients on tenofovir, but differences between groups were not statistically significant.</p> <p>Conclusion</p> <p>Changes in biomarkers of inflammation, coagulation, and endothelial function are not different in viremic patients starting ART with abacavir/lamivudine or tenofovir/emtricitabine. These changes occur in the early phases of treatment and include anti- and pro-atherosclerotic effects with both drugs.</p

Finished genome of the fungal wheat pathogen Mycosphaerella graminicola Reveals dispensome structure, chromosome plasticity, and stealth pathogenesis.

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Divergence Involving Global Regulatory Gene Mutations in an Escherichia coli Population Evolving under Phosphate Limitation

Many of the important changes in evolution are regulatory in nature. Sequenced bacterial genomes point to flexibility in regulatory circuits but we do not know how regulation is remodeled in evolving bacteria. Here, we study the regulatory changes that emerge in populations evolving under controlled conditions during experimental evolution of Escherichia coli in a phosphate-limited chemostat culture. Genomes were sequenced from five clones with different combinations of phenotypic properties that coexisted in a population after 37 days. Each of the distinct isolates contained a different mutation in 1 of 3 highly pleiotropic regulatory genes (hfq, spoT, or rpoS). The mutations resulted in dissimilar proteomic changes, consistent with the documented effects of hfq, spoT, and rpoS mutations. The different mutations do share a common benefit, however, in that the mutations each redirect cellular resources away from stress responses that are redundant in a constant selection environment. The hfq mutation lowers several individual stress responses as well the small RNA–dependent activation of rpoS translation and hence general stress resistance. The spoT mutation reduces ppGpp levels, decreasing the stringent response as well as rpoS expression. The mutations in and upstream of rpoS resulted in partial or complete loss of general stress resistance. Our observations suggest that the degeneracy at the core of bacterial stress regulation provides alternative solutions to a common evolutionary challenge. These results can explain phenotypic divergence in a constant environment and also how evolutionary jumps and adaptive radiations involve altered gene regulation

Influence of IL28B Polymorphisms on Response to a Lower-Than-Standard Dose peg-IFN-α 2a for Genotype 3 Chronic Hepatitis C in HIV-Coinfected Patients

Background: Data on which to base definitive recommendations on the doses and duration of therapy for genotype 3 HCV/HIV-coinfected patients are scarce. We evaluated the efficacy of a lower peginterferon-α 2a dose and a shorter duration of therapy than the current standard of care in genotype 3 HCV/HIV-coinfected patients. Methods and Findings: Pilot, open-label, single arm clinical trial which involved 58 Caucasian HCV/HIV-coinfected patients who received weekly 135 μg peginterferon-α 2a plus ribavirin 400 mg twice daily during 20 weeks after attaining undetectable viremia. The relationships between baseline patient-related variables, including IL28B genotype, plasma HCV-RNA, ribavirin dose/kg, peginterferon-α 2a and ribavirin levels with virological responses were analyzed. Only 4 patients showed lack of response and 5 patients dropped out due to adverse events related to the study medication. Overall, sustained virologic response (SVR) rates were 58.3% by intention-to-treat and 71.4% by per protocol analysis, respectively. Among patients with rapid virologic response (RVR), SVR and relapses rates were 92.6% and 7.4%, respectively. No relationships were observed between viral responses and ribavirin dose/kg, peginterferon-α 2a concentrations, ribavirin levels or rs129679860 genotype. Conclusions: Weekly 135 μg pegIFN-α 2a could be as effective as the standard 180 μg dose, with a very low incidence of severe adverse events. A 24-week treatment duration appears to be appropriate in patients achieving RVR, but extending treatment up to just 20 weeks beyond negativization of viremia is associated with a high relapse rate in those patients not achieving RVR. There was no influence of IL28B genotype on the virological responses. © 2012 López-Cortés et al.Funding provided by Fundación Pública Andaluza para la gestión de la Investigación en Salud de Sevilla. Hospitales Universitarios Virgen del Rocío. Seville, Spain. The enzyme-linked immunosorbent assay Hu-INF-α kits for determination of pegIFN-α-2a were financed by Roche Pharma, S.A. (Spain).Peer Reviewe

Intraspecies Genomic Groups in Enterococcus faecium and Their Correlation with Origin and Pathogenicity

http://aem.asm.org/Seventy-eight Enterococcus faecium strains from various sources were characterized by random amplified polymorphic DNA (RAPD)-PCR, amplified fragment length polymorphism (AFLP), and pulsed-field gel electrophoresis (PFGE) analysis of SmaI restriction patterns. Two main genomic groups (I and II) were obtained in both RAPD-PCR and AFLP analyses. DNA-DNA hybridization values between representative strains of both groups demonstrated a mean DNA-DNA reassociation level of 71%. PFGE analysis revealed high genetic strain diversity within the two genomic groups. Only group I contained strains originating from human clinical samples or strains that were vancomycin-resistant or beta-hemolytic. No differentiating phenotypic features between groups I and II were found using the rapid ID 32 STREP system. The two groups could be further subdivided into, respectively, four and three subclusters in both RAPD-PCR and AFLP analyses, and a high correlation was seen between the subclusters generated by these two methods. Subclusters of group I were to some extent correlated with origin, pathogenicity, and bacteriocinogeny of the strains. Host specificity of E. faecium strains was not confirmed