The measurement of the noise-equivalent spectral radiance of SIMBIO-SYS/VIHI spectrometer

We report about the measurement of the Noise- Equivalent Spectral Radiance (NESR) of the VIHI imaging spectromter aboard ESA's Bepi Colombo mission to Mercury. The knowledge of the NESR allows to determine the capability of an optical detector to measure faint signals. A description of the setup used to determine the NESR during the prelaunch calibration campaign is given. The processing of the data col- lected at various operative temperatures and integration times is described. The sensitivity study of the NESR has been performed at the expected detector's temperatures and integration times with the goal to determine the minimum spectral radiance at which VIHI is sensitive during the different observation phases of the mission. A simulation of the expected Signal-to-Noise Ratio (SNR) of VIHI during the different orbital phases is provided

Righe della stratosfera (40-85 cm-1

SIGLEITItal

Adeno-Associated Virus Serotype 4 (AAV4) and AAV5 Both Require Sialic Acid Binding for Hemagglutination and Efficient Transduction but Differ in Sialic Acid Linkage Specificity

Adeno-associated virus serotype 4 (AAV4) and AAV5 have different tropisms compared to AAV2 and to each other. We recently reported that α2-3 sialic acid is required for AAV5 binding and transduction. In this study, we characterized AAV4 binding and transduction and found it also binds sialic acid, but the specificity is significantly different from AAV5. AAV4 can hemagglutinate red blood cells from several species, whereas AAV5 hemagglutinates only rhesus monkey red blood cells. Treatment of red blood cells with trypsin inhibited hemagglutination for both AAV4 and AAV5, suggesting that the agglutinin is a protein. Treatment of Cos and red blood cells with neuraminidases also indicated that AAV4 bound α2-3 sialic acid. However, resialylation experiments with neuraminidase-treated red blood cells demonstrated that AAV4 binding required α2–3 O-linked sialic acid, whereas AAV5 required N-linked sialic acid. Similarly, resialylation of sialic acid-deficient CHO cells supported this same conclusion. The difference in linkage specificity for AAV4 and AAV5 was confirmed by binding and transduction experiments with cells incubated with either N-linked or O-linked inhibitors of glycosylation. Furthermore, AAV4 transduction was only blocked with soluble α2-3 sialic acid, whereas AAV5 could be blocked with either α2–3 or α2-6 sialic acid. These results suggest that AAV4 and AAV5 require different sialic acid-containing glycoproteins for binding and transduction of target cells and they further explain the different tropism of AAV4 and AAV5