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We present the photometric calibration of the twelve optical passbands observed by the Javalambre Photometric Local Universe Survey (J-PLUS). The proposed calibration method has four steps: (i) definition of a high-quality set of calibration stars using Gaia information and available 3D dust maps; (ii) anchoring of the J-PLUS gri passbands to the Pan-STARRS photometric solution, accounting for the variation of the calibration with the position of the sources on the CCD; (iii) homogenization of the photometry in the other nine J-PLUS filters using the dust de-reddened instrumental stellar locus in (X - r) versus (g - i) colours, where X is the filter to calibrate. The zero point variation along the CCD in these filters was estimated with the distance to the stellar locus. Finally, (iv) the absolute colour calibration was obtained with the white dwarf locus. We performed a joint Bayesian modelling of eleven J-PLUS colour-colour diagrams using the theoretical white dwarf locus as reference. This provides the needed offsets to transform instrumental magnitudes to calibrated magnitudes outside the atmosphere. The uncertainty of the J-PLUS photometric calibration, estimated from duplicated objects observed in adjacent pointings and accounting for the absolute colour and flux calibration errors, are ~19 mmag in u, J0378 and J0395, ~11 mmag in J0410 and J0430, and ~8 mmag in g, J0515, r, J0660, i, J0861, and z. We present an optimized calibration method for the large area multi-filter J-PLUS project, reaching 1-2% accuracy within an area of 1 022 square degrees without the need for long observing calibration campaigns or constant atmospheric monitoring. The proposed method will be adapted for the photometric calibration of J-PAS, that will observe several thousand square degrees with 56 narrow optical filters.

Hepatitis B virus causes acute and chronic infections in millions of people worldwide and, since 1982, a vaccine with 95% effectiveness has been available for immunization. The main component of the recombinant hepatitis B vaccine is the surface antigen protein (HBsAg). In this work, the effect of pH, ionic strength and temperature on the native state of the HBsAg antigen were studied by a combination of biophysical methods that included small angle X-ray scattering, synchrotron radiation circular dichroism, fluorescence and surface plasmon resonance spectroscopies, as well as in vivo and in vitro potency assays. The native conformation, morphology, radius of gyration, and antigenic properties of the HBsAg antigen demonstrate high stability to pH treatment, especially in the pH range employed in all stages of HBsAg vaccine production and storage. The HBsAg protein presents thermal melting point close to 56 °C, reaching a more unfolded state after crossing this point, but it only experiences loss of vaccine potency and antigenic properties at 100 °C. Interestingly, a 6-month storage period does not affect vaccine stability, and the results are similar when the protein is kept under refrigerated conditions or at room temperature (20 °C). At frozen temperatures, large aggregates (>200 nm) are formed and possibly cause loss of HBsAg content, but that does not affect the in vivo assay. Furthermore, HBsAg has a well-ordered secondary structure content that is not affected when the protein is formulated with silica SBA-15, targeting the oral delivery of the vaccine. The combined results from all the characterization techniques employed in this study showed the high stability of the antigen at different storage temperature and extreme values of pH. These findings are important for considering the delivery of HBsAg to the immune system via an oral vaccine.

We present the photometric calibration of the 12 optical passbands observed by the Javalambre Photometric Local Universe Survey (J-PLUS). Methods. The proposed calibration method has four steps: (i) definition of a high-quality set of calibration stars using Gaia information and available 3D dust maps; (ii) anchoring of the J-PLUS gri passbands to the Pan-STARRS photometric solution, accounting for the variation in the calibration with the position of the sources on the CCD; (iii) homogenization of the photometry in the other nine J-PLUS filters using the dust de-reddened instrumental stellar locus in (chi - r) versus (g-i) colours, where chi is the filter to calibrate. The zero point variation along the CCD in these filters was estimated with the distance to the stellar locus. Finally, (iv) the absolute colour calibration was obtained with the white dwarf locus. We performed a joint Bayesian modelling of 11 J-PLUS colour-colour diagrams using the theoretical white dwarf locus as reference. This provides the needed o ffsets to transform instrumental magnitudes to calibrated magnitudes outside the atmosphere. Results. The uncertainty of the J-PLUS photometric calibration, estimated from duplicated objects observed in adjacent pointings and accounting for the absolute colour and flux calibration errors, are similar to 19 mmag in u, J0378, and J0395; similar to 11 mmag in J0410 and J0430; and similar to 8 mmag in g, J0515, r, J0660, i, J0861, and z. Conclusions. We present an optimized calibration method for the large-area multi-filter J-PLUS project, reaching 1-2% accuracy within an area of 1022 square degrees without the need for long observing calibration campaigns or constant atmospheric monitoring. The proposed method will be adapted for the photometric calibration of J-PAS, that will observe several thousand square degrees with 56 narrow optical filters.© ESO 2019

Human transforming growth factor beta induced protein (TGFBIp) is composed of 683 residues, including an N-terminal cysteine-rich (EMI) domain, four homologous fasciclin domains, and an Arg-Gly-Asp (RGD) motif near the C-terminus. The protein is of interest because mutations in the TGFBI gene encoding TGFBIp lead to corneal dystrophy (CD), a condition where protein aggregates within the cornea compromise transparency. The complete three-dimensional structure of TGFBIp is not yet available, with the exception of a partial X-ray structure of the archetype FAS1 domain derived from Drosophila fasciclin-1. In this study, small-angle X-ray scattering (SAXS) models of intact wild-type (WT) human TGFBIp and a mutant (R124H) are presented. The mutation R124H leads to a variant of granular CD. The deduced structure of the TGFBIp monomer consists of four FAS1 domains in a simple "beads-on-a-string" arrangement, constructed by the superimposition of four consecutive Drosophila fasciclin domains. The SAXS-based model of the TGFBIp R124H mutant displayed no structural differences from WT. Both WT TGFBIp and the R124H mutant formed trimers at higher protein concentrations. The similar association properties and three-dimensional shape of the two proteins suggest that the mutation does not induce any major structural rearrangements, but points towards the role of other corneal-specific factors in the formation of corneal R124H deposits.