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1.
Phys Rev Lett ; 128(15): 155301, 2022 Apr 15.
Article de Anglais | MEDLINE | ID: mdl-35499894

RÉSUMÉ

Using femtosecond time-resolved x-ray diffraction, we investigated optically excited coherent acoustic phonons in the Weyl semimetal TaAs. The low symmetry of the (112) surface probed in our experiment enables the simultaneous excitation of longitudinal and shear acoustic modes, whose dispersion closely matches our simulations. We observed an asymmetry in the spectral line shape of the longitudinal mode that is notably absent from the shear mode, suggesting a time-dependent frequency chirp that is likely driven by photoinduced carrier diffusion. We argue on the basis of symmetry that these acoustic deformations can transiently alter the electronic structure near the Weyl points and support this with model calculations. Our study underscores the benefit of using off-axis crystal orientations when optically exciting acoustic deformations in topological semimetals, allowing one to transiently change their crystal and electronic structures.

2.
Int J Food Microbiol ; 363: 109510, 2022 Feb 16.
Article de Anglais | MEDLINE | ID: mdl-34974282

RÉSUMÉ

This study evaluated the antifungal effect of ZnO nanoparticles (ZnO-NPs) on Fusarium proliferatum growth and fumonisin accumulation both on a maize-based medium (in vitro) and on irradiated maize grains (in situ). The ZnO-NPs were obtained by drop-by-drop synthesis without further thermal treatment and characterized by scanning electronic microscopy/ energy dispersive X-ray spectroscopy (SEM/EDS) and X-ray diffraction (XRD). SEM analysis showed them as thin flakes of 200 × 200 nm, ~30 nm thickness and its purity were confirmed by XRD. During the in vitro assay ZnO-NPs (0, 0.8; 4, 8 g L-1) were evaluated at 25 °C during 21 days under darkness or photoperiod incubation (12/12 h light (cold white and black fluorescent lamps)/darkness) to determine its possible photocatalytic influence. Fumonisins were detected by high performance liquid chromatography coupled to mass spectrometry (HPLC- MS/MS). All ZnO-NPs concentrations significantly affected growth rates and FB1 accumulation by F. proliferatum RCFP 5033 (p < 0.05). Similar reduction of growth and FB1 (%) was observed at 0.8 and 8 g L-1 ZnO-NPs under photoperiod or darkness incubation. FB1 reduction was observed after 14 and 21 days, although the highest reduction occurred after 14 days under photoperiod incubation (84-98%). No clear light enhancing effect on the antifungal and anti-mycotoxin capability of the ZnO-NPs was observed. Morphological alterations in mycelia and conidia were observed by SEM. Under the in situ assay, the effect of the ZnO-NPs (0, 0.4, 0.8, 2 g kg-1) on growth rates and fumonisin B1, B2 and B3 accumulation by two F. proliferatum strains was evaluated on irradiated maize grains adjusted to 0.995, 0.98 and 0.97 aW in darkness at 25 °C during 21 days. Also, zinc acetate at 0.8 g kg-1 was included to compare their antifungal effect against the same ZnO-NPs concentration. Growth rates decreased significantly as ZnO-NPs concentrations increased. Higher than 60% of growth reduction was observed for both F. proliferatum strains. Zinc acetate significantly reduced growth, although it was less efficient that the same ZnO-NPs concentration. ZnO-NPs reduced total fumonisins accumulation by 71-99% at 0.8-2 g kg-1 ZnO-NPs and 0.98-0.995 aW. Moreover, 0.4 g kg-1 ZnO-NPs also produced significant reduction of the 3 fumonisins. This study showed the application of ZnO-NPs in maize grains could be a low cost and environmental impact strategy to control phytopathogen and toxigenic fungi such as F. proliferatum and to reduce fumonisins accumulation, both during crop development at preharvest stage and during maize storage.


Sujet(s)
Fumonisines , Fusarium , Oxyde de zinc , Spectrométrie de masse en tandem , Zea mays , Oxyde de zinc/pharmacologie
3.
Int J Food Microbiol ; 318: 108468, 2020 Apr 02.
Article de Anglais | MEDLINE | ID: mdl-31816528

RÉSUMÉ

This study examined the effect of interacting conditions of water activity (aW, 0.995, 0.98 and 0.95) and temperature (15, 25 and 30 °C) on growth rate of two Fusarium thapsinum and one F. andiyazi strains isolated from sorghum in Argentina. In addition, the effect of interacting conditions (aW × temperature × incubation time (7, 14, 21 and 28 days)) on mycotoxin production (moniliformin (MON), fusaric acid (FA) and fusarin C (FUS C)) on a sorghum grain substrate was evaluated. Statistical analysis showed that aW and temperature significantly affected growth of both species, mainly the aW. Incubation time significantly influenced mycotoxin production by both species as well, mostly for FA. Maximum growth rates of the F. thapsinum strains were obtained at the highest aW (0.995) and 25 °C and growth rate decreased as aW and temperature were reduced. The same growth profile was observed for F. andiyazi RCFA09 (maximum growth rates at 0.995-25 °C). Mycotoxin production by both species was detected at the highest aW levels whereas at 0.95 aW only low amounts of MON were produced by F. thapsinum. Maximum MON and FUS C production by both F. thapsinum strains was observed at 0.995 aW and 25-30 °C after 28 days of incubation. Also, F. thapsinum strains showed maximum FA production at the highest aW and temperature but after 14 days; after this incubation time toxin levels significantly decreased. The responses to aW and temperature of F. andiyazi were similar to that of F. thapsinum strains in relation to FA and FUS C production. Maximum levels of FA were detected at the highest aW after 14 days of incubation at 25-30 °C. Fusarin C was produced at all assayed temperatures but maximum levels were detected at 30 °C and 0.995 aW after 28 days of incubation. Two-dimensional profiles on the interactions of aW by temperature were developed from these data to identify conditions that indicate a significant risk from MON, FA and FUS C accumulation on sorghum grains. The results of this study suggest that sorghum grains could be colonized by these species and toxin production can occur, especially during development stages under field conditions at high water activity of grains or during grain storage if the drying process is slow or deficient. To our knowledge, this study described for the first time FUS C production by F. thapsinum and F. andiyazi under interacting conditions of aW, temperature and incubation time on sorghum grains.


Sujet(s)
Grains comestibles/microbiologie , Fusarium/croissance et développement , Fusarium/métabolisme , Mycotoxines/biosynthèse , Sorghum/microbiologie , Argentine , Grains comestibles/composition chimique , Manipulation des aliments , Fusarium/isolement et purification , Mycotoxines/analyse , Sorghum/composition chimique , Température , Facteurs temps , Eau/analyse
4.
Phys Rev Lett ; 118(2): 027002, 2017 Jan 13.
Article de Anglais | MEDLINE | ID: mdl-28128591

RÉSUMÉ

X-ray diffraction was employed to study the evolution of the charge density wave (CDW) in Cu_{x}TiSe_{2} as a function of copper intercalation in order to clarify the relationship between the CDW and superconductivity. The results show a CDW incommensuration arising at an intercalation value coincident with the onset of superconductivity at around x=0.055(5). Additionally, it was found that the charge density wave persists to higher intercalant concentrations than previously assumed, demonstrating that the CDW does not terminate inside the superconducting dome. A charge density wave peak was observed in samples up to x=0.091(6), the highest copper concentration examined in this study. The phase diagram established in this work suggests that charge density wave incommensuration may play a role in the formation of the superconducting state.

5.
Mycotoxin Res ; 31(3): 145-50, 2015 Aug.
Article de Anglais | MEDLINE | ID: mdl-25982450

RÉSUMÉ

In this study, gliotoxin production by Aspergillus fumigatus strains from animal environment is studied. Moreover, a rapid, easy and environment-friendly micro-analytical sample treatment procedure coupled with LC-MS/MS was applied for the determination of gliotoxin from A. fumigatus cultures. The ability of gliotoxin production by 143 strains was assayed in yeast extract sucrose agar, and 1 ml of chloroform was used for toxin extraction without further clean-up. Mean recoveries at two spiking levels (2500 and 7000 ng/g; n = 6) were 100.3 ± 6.6 % relative SD (RSD) and 92.4 ± 3.8 % RSD. Repeatability and within-laboratory reproducibility for different concentration levels of gliotoxin (25 to 1000 ng/ml; n = 12) ranged from 0.3 to 5.4 % RSD and from 3.9 to 12.7 % RSD, respectively. The detection limit of the analytical method was 3.5 ng/g. The ability for gliotoxin production by A. fumigatus revealed that 61.5 % of the strains were able to produce the toxin at levels ranging from LOQ to 3430.5 ng/g. However, all the tested samples had similar percentages of producing strains (81.8 to 86.6 %). The micro-analytical sample treatment coupled with LC-MS/MS detection is a precise and useful methodology for determining gliotoxin from fungal extracts of A. fumigatus and allows working both fast and safely and also reducing the effect on the environment. This toxin plays a critical role in the pathobiology of A. fumigatus, and its presence in animal environments could affect animal health and productivity; in addition, there are risks of contamination for rural workers during handling and storage of animal feedstuffs.


Sujet(s)
Aspergillus fumigatus/métabolisme , Contamination des aliments/analyse , Gliotoxine/analyse , Ensilage/microbiologie , Animaux , Chromatographie en phase liquide à haute performance , Gliotoxine/métabolisme , Reproductibilité des résultats , Spectrométrie de masse en tandem
6.
Clin Microbiol Infect ; 21(8): 799.e1-3, 2015 Aug.
Article de Anglais | MEDLINE | ID: mdl-25889358

RÉSUMÉ

Stool samples were obtained from healthy children and children with diarrhoea in Rio de Janeiro, Brazil, and analysed for aichivirus A and salivirus by reverse transcription PCR. Aichivirus A was detected in 5 (0.8%) and salivirus in 10 (1.7%) of the samples obtained from children with diarrhoea. None of the healthy children tested positive for these viruses. The results demonstrate that these viruses continuously circulate in the country, although at a low frequency.


Sujet(s)
Diarrhée/virologie , Gastroentérite/virologie , Infections à Picornaviridae/virologie , Picornaviridae/classification , Picornaviridae/isolement et purification , Brésil/épidémiologie , Enfant , Enfant d'âge préscolaire , Diarrhée/épidémiologie , Fèces/virologie , Femelle , Gastroentérite/épidémiologie , Humains , Nourrisson , Mâle , Infections à Picornaviridae/épidémiologie , Prévalence , Études rétrospectives , RT-PCR
7.
Lett Appl Microbiol ; 57(6): 484-91, 2013 Dec.
Article de Anglais | MEDLINE | ID: mdl-23889550

RÉSUMÉ

UNLABELLED: Aspergillus fumigatus, a well-known human and animal pathogen causing aspergillosis, has been historically identified by morphological and microscopic features. However, recent studies have shown that species identification on the basis of morphology alone is problematic. The aim of this work was to confirm the taxonomic state at specie level of a set of clinical (human and animal) and animal environment A. fumigatus strains identified by morphological criteria applying a PCR-RFLP assay by an in silico and in situ analysis with three restriction enzymes. The A. fumigatus gliotoxin-producing ability was also determined. Previous to the in situ PCR-RFLP analysis, an in silico assay with BccI, MspI and Sau3AI restriction enzymes was carried out. After that, these enzymes were used for in situ assay. All A. fumigatus strains isolated from corn silage, human aspergillosis and bovine mastitis and high per cent of the strains isolated from cereals, animal feedstuff and sorghum silage were able to produce high gliotoxin levels. Also, all these strains identified by morphological criteria as A. fumigatus, regardless of its isolation source, had band patterns according to A. fumigatus sensu stricto by PCR-RFLP markers. SIGNIFICANCE AND IMPACT OF THE STUDY: Aspergillus fumigatus is a well-known human and animal pathogen causing aspergillosis. In this study, clinical (human and animal) and animal environment strains were able to produce high gliotoxin levels and had band profiles according to A. fumigatus sensu stricto by PCR-RFLP markers. The results obtained here suggest that strains involved in human and animal aspergillosis could come from the animal environment in which A. fumigatus is frequently found. Its presence in animal environments could affect animal health and productivity; in addition, there are risks of contamination for rural workers during handling and storage of animal feedstuffs.


Sujet(s)
Aspergillose/microbiologie , Aspergillose/médecine vétérinaire , Aspergillus fumigatus/classification , Grains comestibles/microbiologie , Gliotoxine/métabolisme , Mammite bovine/microbiologie , Ensilage/microbiologie , Animaux , Aspergillus fumigatus/génétique , Aspergillus fumigatus/isolement et purification , Aspergillus fumigatus/métabolisme , Techniques de typage bactérien , Séquence nucléotidique , Brésil , Bovins , Femelle , Humains , Données de séquences moléculaires , Réaction de polymérisation en chaîne , Polymorphisme de restriction
8.
Lett Appl Microbiol ; 50(1): 77-81, 2010 Jan.
Article de Anglais | MEDLINE | ID: mdl-19889107

RÉSUMÉ

AIMS: To evaluate gliotoxin production by Aspergillus fumigatus strains isolated from feedstuff intended for domestic animals and pets, and to determine the amount of gliotoxin in these substrates. METHODS AND RESULTS: A total of 150 feedstuff samples were collected. They were composed of 30 samples each of five different feed types (pigs, poultry, cattle, horse and pets). Aspergillus fumigatus gliotoxin production ability and gliotoxin presence in feedstuff was determined by HPLC. Aspergillus fumigatus strains were isolated from all of the tested samples. Strains from cattle, horses and pet food were able to produce gliotoxin. Corn silage samples intended for cattle did not show gliotoxin contamination. All the other tested samples had gliotoxin levels ranging from 29 to 209 microg g(-1). Horse and poultry feed samples had the greatest contamination frequency. CONCLUSIONS: Feed samples contaminated with gliotoxin are potentially toxic to animals. SIGNIFICANCE AND IMPACT OF THE STUDY: The presence of gliotoxin could affect animal productivity and health. Moreover, there are risks of contamination to farm workers handling improperly stored animal feed. Aspergillus fumigatus strains isolated from different sources should be investigated to determine prevention and control strategies.


Sujet(s)
Aliment pour animaux , Animaux domestiques , Aspergillus fumigatus/isolement et purification , Contamination des aliments , Gliotoxine/analyse , Aliment pour animaux/analyse , Aliment pour animaux/microbiologie , Animaux , Argentine , Aspergillus fumigatus/métabolisme , Bovins , Chromatographie en phase liquide à haute performance , Numération de colonies microbiennes , Microbiologie alimentaire , Gliotoxine/biosynthèse , Equus caballus , Volaille , Ensilage/analyse , Suidae , Zea mays
9.
Allerg Immunol (Leipz) ; 37(1): 37-45, 1991.
Article de Allemand | MEDLINE | ID: mdl-2063729

RÉSUMÉ

In 353 sera (from healthy donors as well as patients suffering from rheumatoid arthritis, systemic lupus erythematosus, hepatitis, malignant melanoma) circulating immune complexes were determined by C1q-binding test and a C1q solid-phase ELISA. Using peroxidase-labelled antibodies (from rabbit) against human mu-, gamma-, and alpha-heavy chains, the immunoglobulin classes in the complexes were determined. In rheumatoid arthritis, immune complexes contain IgM more frequently (41.5%) than in systemic lupus erythematosus (10%). Immune complexes containing only IgA as immunoglobulin were found in 24 cases. Our results including binding experiments with chemically aggregated IgA suggest, that the binding of C1q to IgA is not necessarily followed by classical complement activation.


Sujet(s)
Complexe antigène-anticorps/analyse , Immunoglobuline A/analyse , Immunoglobuline G/analyse , Immunoglobuline M/analyse , Complexe antigène-anticorps/métabolisme , Polyarthrite rhumatoïde/immunologie , Activation du complément , Complément C1q/analyse , Complément C1q/métabolisme , Test ELISA/méthodes , Hépatite/immunologie , Humains , Lupus érythémateux disséminé/immunologie , Mélanome/immunologie
10.
Adv Exp Med Biol ; 120B: 275-86, 1979.
Article de Anglais | MEDLINE | ID: mdl-229704

RÉSUMÉ

Endothelial cells are a major source of kininase enzymes including kininase II. Kininase II is situated along the plasma membrane, not as an ecto-enzyme but as an enzyme synthesized by the endothelial cells themselves. However, it is likely that endothelial cells do more than degrade kinins. These cells are contractile and may possess kinin receptors; a possibility supported by the fact that kinins stimulate endothelial cells to form and release prostaglandin-related substances. In addition, we have found that endothelial cells in culture are reactive with antibodies to alpha 2-macroglobulin. Endothelial cells can hydrolyze [3H]Pro-Phe-Arg-anilide, a kallikrein substrate, but the reaction is not inhibited by soya bean trypsin inhibitor (SBTI) or Trasylol. Possibly kallikrein or a related trypsin-like enzyme is bound to alpha 2-macroglobulin and is not free to react with the inhibitors. Thus, endothelial cells can bind and inhibit kallikrein-like enzymes, degrade kinins and respond to kinin stimulation.


Sujet(s)
Endothélium/enzymologie , Kallicréines/métabolisme , Kinines/métabolisme , Peptidyl-Dipeptidase A/métabolisme , Animaux , Acides arachidoniques/métabolisme , Bradykinine/pharmacologie , Bovins , Cellules cultivées , Endothélium/effets des médicaments et des substances chimiques , Cochons d'Inde , Kallicréines/antagonistes et inhibiteurs , Muscles lisses vasculaires/enzymologie , Peptidyl-Dipeptidase A/biosynthèse , Prostaglandines/biosynthèse , Artère pulmonaire/enzymologie
11.
Adv Exp Med Biol ; 120B: 599-606, 1979.
Article de Anglais | MEDLINE | ID: mdl-229713

RÉSUMÉ

Urines and sera (human, guinea pig and rat) contain low molecular weight inhibitors of angiotensin converting enzyme (ACE). The urines contain ACE, but the enzyme is scarcely measurable without prior ultrafiltration or dialysis. The activity increases strikingly through three ultrafiltration steps using a membrane with a 10,000 MW retention limit. As implied, the ultrafiltrates contain inhibitory activity and can prevent the hydrolysis of [3H]benzoyl-Gly-His-Leu by ACE from any source, including lung and serum. Human urinary ultrafiltrate contains at least three inhibitors separable on Bio-Gel P-2. The inhibitors are acidic and can be partially purified on Bio-Rex 70 developed with an acetic acid gradient. The smallest of the inhibitors can be purified to apparent homogeneity by partition chromatography (sephadex G-25; butanol, acetic acid, H2O; 4:1:5). The excretion of inhibitory activity varies in response to dietary salt: Activity is low when rats are maintained on a high NaCl diet and is high (3 x's control) on a low NaCl diet. Thus, the activity of ACE may be modulated in vivo by naturally-occurring enzyme inhibitors. Whether some hypertensive patients are deficient in ACE inhibitory activity remains to be determined.


Sujet(s)
Inhibiteurs de l'enzyme de conversion de l'angiotensine , Inhibiteurs de protéases/sang , Animaux , Cochons d'Inde , Humains , Cinétique , Masse moléculaire , Peptidyl-Dipeptidase A/urine , Inhibiteurs de protéases/urine , Rats
13.
Adv Exp Med Biol ; 120A: 313-23, 1979.
Article de Anglais | MEDLINE | ID: mdl-227242

RÉSUMÉ

The excretion of kallikrein in urine varies, but the pathophysiologic implications are not clear. To help clarify the role of the urinary kallikrein-kinin system, we have begun to define components of the system as they occur in urine. To minimize artifacts which may arise through extensive purification procedures, we studied urinary protein concentrates prepared by ultrafiltration. The concentrates were separated by chromatography on Sephacryl. Urine contains abundant kininase activity, but in strongly inhibited forms. Kininase II is separable into at least two forms. Another major kininase can hydrolyze benzoyl-Pro-Phe-Arg and is inhibited by arginine but not by BPP9a or SQ 14,225. Its molecular weight is approximately 63,000. A third kininase, not inhibited by BPP9a, is excluded from Sephacryl. Human urine appears to contain only one kallikrein-like enzyme (MW 45,000). In addition, urine contains a protein (MW approximately 80,000) which reacts with trypsin to release bradykinin and which inhibits the hydrolysis of Pro-Phe-Arg-[3H]anilide by urinary kallikrein. Thus, in addition to kallikrein and kinins, urine contains kininogen and at least three kininase enzymes. Urinary ultrafiltrate contains an inhibitory substance (approximately MW 400).


Sujet(s)
Kallicréines/urine , Kinines/urine , Animaux , Aprotinine/urine , Cochons d'Inde , Humains , Kininogènes/urine , Lysine carboxypeptidase/urine , Mâle , Masse moléculaire , Peptidyl-Dipeptidase A/urine , Spécificité d'espèce
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