X-ray luminescence computed tomography (XLCT) is a new molecular imaging modality. In this Letter, we first in vivo tomographically image the near-IR-emitting nanophosphor (Gd₂O₃:Eu³⁺) in nude mice (N=2). In practically, incorporating the compressive sensing technique, the XLCT reconstruction is performed only using single-view data. The experimental results indicate that the single-view reconstruction is feasible to image XLCT in vivo. The location error is less than 1.5 mm. Further, the imaging time can be greatly reduced compared with previous XLCT systems. Therefore, it is suited for imaging fast distribution of x-ray-excitable nanophosphors within a biological object.

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The data indicate a probable high rate of Brucella bacteremia, suggesting a potential risk of transfusion-transmitted brucellosis. Blood donation screening for Brucella infection may be considered in the high Brucella-endemic areas of China.

Hepatitis B virus surface antigen (HBsAg), a specific antigen on the membrane of hepatitis B virus (HBV)-infected cells, provides a perfect target for therapeutic drugs. In order to mediate successful targeted delivery of these therapies, it is essential to have antibodies that recognize HBsAg with high specificity and affinity. In this report, we constructed a natural immune antigen binding fragments (Fab) antibody phage display library against HBsAg and after three rounds of panning, five Fab fragments with significant HBsAg binding ability were selected and analysed. DNA sequencing revealed that all the light chains had the same sequence, while all the Fd genes exhibited different sequences. For further application, all of the Fab antibodies were reconstructed into single chain antibodies (scFvs) and expressed in Escherichia coli BL21 cells. Indirect enzyme-linked immunosorbent assay analysis demonstrated that all five scFvs maintained a high affinity for HBsAg and could bind HBsAg on the membrane of HBV-infected cells. Indirect fluorescent staining analysis revealed that one of the scFvs (scFv15) could be internalized into HBsAg-positive HepG2.2.15 cells through clathrin-mediated endocytosis pathway. The internalizing scFv15 antibody would have great potential for the targeted delivery of therapeutics to HBV-infected cells.