PubMed · 7702273
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P Mathelier-Fusade, F Leynadier. 1994. [Cold urticaria].. https://pubmed.ncbi.nlm.nih.gov/7702273/
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We have developed high-density DNA microarrays of yeast ORFs. These microarrays can monitor hybridization to ORFs for applications such as quantitative differential gene expression analysis and screening for sequence polymorphisms. Automated scripts retrieved sequence information from public databases to locate predicted ORFs and select appropriate primers for amplification. The primers were used to amplify yeast ORFs in 96-well plates, and the resulting products were arrayed using an automated micro arraying device. Arrays containing up to 2,479 yeast ORFs were printed on a single slide. The hybridization of fluorescently labeled samples to the array were detected and quantitated with a laser confocal scanning microscope. Applications of the microarrays are shown for genetic and gene expression analysis at the whole genome level.
Low pH-induced fusion mediated by the hemagglutinin (HA) of influenza virus involves a conformational change in the protein that leads to the insertion of a "fusion peptide" of the protein into the target membrane. It has been suggested that this insertion, aided by the formation of a complex of multiple HA trimers, would lead to perturbation of the bilayer structure of the membrane, initiating fusion. Here we present data showing that the interaction of the bromelain released ectodomain of the protein (BHA) with liposomal membranes at low pH leads to pore formation, at least at low temperatures. Strongly temperature-dependent low pH-induced inactivation of BHA resulted in a complete lack of activity of BHA above 10 degrees C. Even at 0 degrees C, only about 5% of the BHA participated in pore formation. Viral HA was less rapidly inactivated and still induced pores at 37 degrees C. BHA-induced pore formation showed a sigmoidal time course. Once BHA had formed a pore in one liposome, it did not form a pore in a further liposome. Quantitative analysis of pore formation indicated that one single BHA trimer sufficed to produce a pore. These data indicate that fusion peptide insertion perturbs the membrane and that the formation of a complex of trimers is not a prerequisite for the perturbation.
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