Translation Revision: Correlating Revision Procedure and Error Detection

This article reports on an empirical study on translation revision. With the aim of investigating the possible link between revision procedure and quality, the research correlates an indicator of quality, error detection, with revision procedure. Error detection and revision procedure were studied drawing on a convergent parallel mixed-methods research design involving three different sources of data. Nine subjects performed a revision task and thus produced text data; their activities on the computer screen were captured and saved as video fi les; and retrospective interviews were conducted with the revisers upon completion of the task. Results show that the highest error detection scores were linked with a variety of revision procedures, but with one common denominator: the target text was consistently the point of departure. Revisers with high error detection scores thus engaged in various different revision procedures, but their focus of attention in the initial operations was the translation rather than the source text in all cases. Conversely, the revisers whose initial attention was directed towards the source text received the lowest error detection scores in the revision task

A fungal lytic polysaccharide monooxygenase is required for cell wall integrity, thermotolerance, and virulence of the fungal human pathogen Cryptococcus neoformans

Fungi often adapt to environmental stress by altering their size, shape, or rate of cell division. These morphological changes require reorganization of the cell wall, a structural feature external to the cell membrane composed of highly interconnected polysaccharides and glycoproteins. Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that are typically secreted into the extracellular space to catalyze initial oxidative steps in the degradation of complex biopolymers such as chitin and cellulose. However, their roles in modifying endogenous microbial carbohydrates are poorly characterized. The CEL1 gene in the human fungal pathogen Cryptococcus neoformans (Cn) is predicted by sequence homology to encode an LPMO of the AA9 enzyme family. The CEL1 gene is induced by host physiological pH and temperature, and it is primarily localized to the fungal cell wall. Targeted mutation of the CEL1 gene revealed that it is required for the expression of stress response phenotypes, including thermotolerance, cell wall integrity, and efficient cell cycle progression. Accordingly, a cel1Δ deletion mutant was avirulent in two models of C. neoformans infection. Therefore, in contrast to LPMO activity in other microorganisms that primarily targets exogenous polysaccharides, these data suggest that CnCel1 promotes intrinsic fungal cell wall remodeling events required for efficient adaptation to the host environment

Sensory and rheological screening of exopolysaccharide producing strains of bacterial yoghurt cultures

Yoghurts were produced with 24 different cultures differing in their ability to produce exopolysaccharides (EPS). Rheological and sensory analyses showed large differences in texture properties in the yoghurt samples. EPS production was found to have a major effect oil the texture properties, but varying textures within the EPS +/- groups were also found. Yoghurts fermented with EPS-producing cultures showed increased mouth thickness and ropiness and tended to be creamier than yoghurts without these cultures; in contrast, these yoghurts had the lowest syneresis and highest gel firmness (initial gel strength before the yoghurt was subjected to shear). Correlations between rheological parameters and sensory texture attributes included G* correlating with gel firmness, while viscosity measured at 241 s(-1) correlated with mouth thickness. An interesting viscometry relationship was found between ropiness and hysteresis loop area

A fungal lytic polysaccharide monooxygenase is required for cell wall integrity, thermotolerance, and virulence of the fungal human pathogen Cryptococcus neoformans

International audienceFungi often adapt to environmental stress by altering their size, shape, or rate of cell division. These morphological changes require reorganization of the cell wall, a structural feature external to the cell membrane composed of highly interconnected polysaccharides and glycoproteins. Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that are typically secreted into the extracellular space to catalyze initial oxidative steps in the degradation of complex biopolymers such as chitin and cellulose. However, their roles in modifying endogenous microbial carbohydrates are poorly characterized. The CEL1 gene in the human fungal pathogen Cryptococcus neoformans (Cn) is predicted by sequence homology to encode an LPMO of the AA9 enzyme family. The CEL1 gene is induced by host physiological pH and temperature, and it is primarily localized to the fungal cell wall. Targeted mutation of the CEL1 gene revealed that it is required for the expression of stress response phenotypes, including thermotolerance, cell wall integrity, and efficient cell cycle progression. Accordingly, a cel1Δ deletion mutant was avirulent in two models of C. neoformans infection. Therefore, in contrast to LPMO activity in other microorganisms that primarily targets exogenous polysaccharides, these data suggest that CnCel1 promotes intrinsic fungal cell wall remodeling events required for efficient adaptation to the host environment