Adherence of the opportunistic fungus Aspergillus fumigatus to the extracellular matrix components is considered a crucial step in the establishment of the infection. Given the high carbohydrate content of these glycoproteins and the role of carbohydrate-protein interactions in numerous adherence processes, the presence of a lectin in A. fumigatus was investigated. Different fungal extracts obtained by sonication or grinding in liquid nitrogen from resting or swollen conidia, as well as from germ tubes and mycelium, were tested by hemagglutination assays using rabbit erythrocytes. A lectin activity was recovered in all the extracts tested. However, sonication of resting conidia resulted in the highest specific activity. Purification of the lectin was achieved by gel filtration followed by ion-exchange and hydrophobic-interaction chromatographies. Analysis of the purified lectin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed an apparent molecular mass of 32 kDa, which is similar to that of the alkaline protease already identified from different strains of A. fumigatus. However, as evidenced by the use of an alkaline protease-deficient mutant, the two activities were supported by distinct proteins. In addition, hemagglutination inhibition experiments using different saccharides and glycoproteins demonstrated the specificity of the lectin for sialic acid residues. Together these results suggest that this lectin may contribute to the attachment of conidia to the extracellular matrix components through the recognition of the numerous terminal sialic acid residues of their carbohydrate chains.

Chemically -driven isothermal close space vapour transport was used to prepare pure MoO2 films which were eventually converted to MoO3 by annealing in air. According to temperaturedependent Raman measurements, the MoO2/MoO3 phase transformation was found to occur in the 225 -350 o C range; no other phases were detected during the transition. A clear change in composition and Raman spectra, as well as noticeable modifications of the band gap and the absorption coefficient confirmed the conversion from MoO2 to MoO3. An extensive characterization of films of both pure phases was carried out. In particular, a procedure was developed to determine the dispersion relation of the refractive index of MoO2 from the shift of the interference fringes the used SiO2/Si substrate. The obtained refractive index was corrected taking into account the porosity calculated from elastic backscattering spectrometry. The Debye temperature and the residual resistivity were extracted from the electrical resistivity temperature dependence using the Bloch -Grüneisen equation. MoO3 converted samples presented very high resistivity and a typical semiconducting behaviour. They also showed intense and broad luminescence spectra, which were deconvoluted considering several contributions; and its behaviour with temperature was examined. Furthermore, surface photovoltage spectra were taken and the relation of these spectra with the photoluminescence is discussed.

In an attempt to define the molecular basis of the adherence of Aspergillus fumigatus conidia to the host tissues, a step which might be mediated by the recognition of basement membrane laminin or fibrinogen, we analyzed the binding of these glycoproteins by flow cytometry and a microtiter plate adherence assay. Flow cytometry revealed that the binding of fluorescein isothiocyanate-labeled laminin to conidia was saturable and specific. Moreover, the ability of conidia to bind laminin increased with their maturation. Competition experiments showed a cross-reactivity between laminin and fibrinogen binding and a lack of interactions with glycosaminoglycans. In addition, the binding of laminin was not inhibited by the different adhesive synthetic peptides tested. Furthermore, the microtiter plate assay of adherence to chymotrypsin degradation products of laminin or fibrinogen purified by gel filtration suggested a unique binding site common to sequential degradation fragments or the presence of multiple binding sites on the two ligands. Therefore, the role of carbohydrates in the recognition process was investigated. Among the carbohydrates tested, constitutive of the conidial wall or of the oligosaccharide side chains of laminin and fibrinogen, only N-acetylneuraminic acid and sialyllactose inhibited the binding of these glycoproteins to conidia. In conclusion, these results strengthen the idea that the laminin and fibrinogen receptors in A. fumigatus are identical and suggest an interaction mediated by a sialic acid-specific lectin of the conidial wall.

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The needs of the population included in this survey, showed the importance to consider cognitive (necessity of obtaining clear and extensive information), social (maintaining everyday relationships), emotional (illness and its diagnostic and therapeutic procedures often generate mood disorders), and practical (environmental and architectural aspects can lead to either an improvement or a worsening of the hospitalisation perception) factors. All of these factors have shown a beneficial contribution, leading to an earlier recovery of health.

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