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Prion diseases are neurodegenerative disorders caused by misfolding of the normal prion protein (PrP) into a pathogenic "scrapie" conformation. To better understand the cellular and molecular mechanisms that govern the conformational changes (conversion) of PrP, we compared the dynamics of PrP from mammals susceptible (hamster and mouse) and resistant (rabbit) to prion diseases in transgenic flies. We recently showed that hamster PrP induces spongiform degeneration and accumulates into highly aggregated, scrapie-like conformers in transgenic flies. We show now that rabbit PrP does not induce spongiform degeneration and does not convert into scrapie-like conformers. Surprisingly, mouse PrP induces weak neurodegeneration and accumulates small amounts of scrapie-like conformers. Thus, the expression of three highly conserved mammalian prion proteins in transgenic flies uncovered prominent differences in their conformational dynamics. How these properties are encoded in the amino acid sequence remains to be elucidated.Genetic and biochemical evidence indicates that the prion protein (PrP) 3 is the causative agent in the pathogenesis of prion diseases (1). The pioneers of prion biology successfully transmitted prions to many laboratory animals, including mice, rats, hamsters, and guinea pigs (2, 3). However, rabbits proved resistant to different prion strains from humans and sheep and from mice-adapted scrapie sheep prions. One interpretation of these results is that the cellular environment of the rabbit may lack a conversion factor or express conversion inhibitors that prevent the acquisition of neurotoxic conformers. However, expression of recombinant PrP from sheep and rodents (mouse and bank vole) in rabbit RK13 epithelial cells followed by challenge with autologous prions led to persistent proteinase K-resistant PrP (PrP res or PrP Sc ) replication, indicating that rabbit cells provide a molecular environment consistent with PrP Sc conversion (4, 5). Alternatively, key amino acid substitutions in the sequence of rabbit PrP may impose structural constraints that prevent its conversion. To answer these questions Priola and co-workers (6) expressed rabbit PrP (RaPrP) in prion-infected mouse neuroblastoma cells and showed that RaPrP could not be converted into PrP Sc , indicating that the amino acid sequence of RaPrP prevents its conformational conversion. Thus, understanding the conformational properties of RaPrP can contribute to unraveling the rules governing prion transmission and neuropathology.PrP is a membrane-anchored glycoprotein highly enriched in the brain with the ability to undergo conformational changes. PrP Sc has been postulated as the causative agent in prion diseases, and it is composed of specific folding species of PrP that are replicated by autocatalytic mechanisms (7). However, the structure of PrP Sc has not yet been resolved. Structural studies performed with either purified or recombinant PrP C have confirmed the intrinsic ability of PrP to misfold into conformations that are transmissib...

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BackgroundIn the past few decades, microalgae biofuel has become one of the most interesting sources of renewable energy. However, the higher cost of microalgae biofuel compared to that of petroleum prevented microalgae biofuel production. Therefore, the research on increasing lipid productivity from microalgae becomes more important. The lipid production source, triacylglycerol biosynthesis in microalgae requires short chain fatty acids as substrates, which are synthesized in chloroplasts. However, the transport mechanism of fatty acids from microalgae chloroplasts to cytosol remains unknown.ResultscDNAs from two homologs of the Arabidopsis fatty acid exporter 1 (FAX1) were cloned from Chlamydomonas reinhardtii and were named crfax1 and crfax2. Both CrFAXs were involved in fatty acid transport, and their substrates were mainly C16 and C18 fatty acids. Overexpression of both CrFAXs increased the accumulation of the total lipid content in algae cells, and the fatty acid compositions were changed under normal TAP or nitrogen deprivation conditions. Overexpression of both CrFAXs also increased the chlorophyll content. The MGDG content was decreased but the TAG, DAG, DGDG and other lipid contents were increased in CrFAXs overexpression strains.ConclusionThese results reveal that CrFAX1 and CrFAX2 were involved in mediating fatty acid export for lipids biosynthesis in C. reinhardtii. In addition, overexpression of both CrFAXs obviously increased the intracellular lipid content, especially the triacylglycerol content in microalgae, which provides a potential technology for the production of more biofuels using microalgae.Electronic supplementary materialThe online version of this article (10.1186/s13068-018-1332-4) contains supplementary material, which is available to authorized users.

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International audienceHeat treatment is one of the essential operations widely used in most dairy processes, and heat stability is one of the essential properties of milk. Casein micelles are the major component in milk responsible for the heat stability of milk during processing. This study assessed the effects of heat treatment temperature and duration on the average size, turbidity, polydispersity index and heat stability of casein micelles in yak skim milk and distilled water. The results showed that whey protein had an important role in influencing the heat stability of casein micelles. The average size, polydispersity index and turbidity of micelles in skim milk were higher than those of micelles in distilled water in all cases while the heat stability of casein micelles in skim milk was lower than those in distilled water. As a result of the heat treatment, the size of micelles in skim milk increased due to complex of casein/whey protein formed via covalent bonds, whereas it decreased in distilled water attributed to the change of hydrophobicity in micelles. The size distribution of particles broadened with increasing heating temperature, resulting in the increase in turbidity and polydispersity index of casein micelles both in skim milk and distilled water. The micelles in skim milk combined with whey protein during heating. These findings will help processors design appropriate heating conditions for yak milk and yak casein products and help identify new opportunities for product development

BackgroundPolyunsaturated fatty acids (PUFAs), which contain two or more double bonds in their backbone, are the focus of intensive global research, because of their nutritional value, medicinal applications, and potential use as biofuel. However, the ability to produce these economically important compounds is limited, because it is both expensive and technically challenging to separate omega-3 polyunsaturated fatty acids (ω-3 PUFAs) from natural oils. Although the biosynthetic pathways of some plant and microalgal ω-3 PUFAs have been deciphered, current understanding of the correlation between fatty acid desaturase content and fatty acid synthesis in Synechocystis sp. PCC6803 is incomplete.ResultsWe constructed a series of homologous vectors for the endogenous and exogenous expression of Δ6 and Δ15 fatty acid desaturases under the control of the photosynthesis psbA2 promoter in transgenic Synechocystis sp. PCC6803. We generated six homologous recombinants, harboring various fatty acid desaturase genes from Synechocystis sp. PCC6803, Gibberella fujikuroi and Mortierella alpina. These lines produced up to 8.9 mg/l of α-linolenic acid (ALA) and 4.1 mg/l of stearidonic acid (SDA), which are more than six times the corresponding wild-type levels, at 20°C and 30°C. Thus, transgenic expression of Δ6 and Δ15 fatty acid desaturases enhances the accumulation of specific ω-3 PUFAs in Synechocystis sp. PCC6803.ConclusionsIn the blue-green alga Synechocystis sp. PCC6803, overexpression of endogenous and exogenous genes encoding PUFA desaturases markedly increased accumulation of ALA and SDA and decreased accumulation of linoleic acid and γ-linolenic acid. This study lays the foundation for increasing the fatty acid content of cyanobacteria and, ultimately, for producing nutritional and medicinal products with high levels of essential ω-3 PUFAs.