Heparan sulfate proteoglycan is an important attachment factor for cell entry of Akabane and Schmallenberg viruses

Akabane (AKAV) and Schmallenberg (SBV) viruses are Orthobunyavirus transmitted by arthropod vectors with a broad cellular tropism in vitro as well as in vivo Both AKAV and SBV cause arthrogryposis-hydranencephaly syndrome in ruminants. The main cellular receptor and attachment factor for entry of these orthobunyaviruses are unknown. Here, we found that AKAV and SBV infections were inhibited by the addition of heparin or enzymatic removal of cell surface heparan sulfates. To confirm this finding, we prepared heparan sulfate proteoglycan (HSPG)-knockout (KO) cells by using a CRISPR/Cas9 system and measured the binding quantities of these viruses to cell surfaces. We observed a substantial reduction in AKAV and SBV binding to cells, limiting the infections by these viruses. These data demonstrate that HSPGs are important cellular attachment factors for AKAV and SBV, at least in vitro, to promote virus replication in susceptive cells. Importance: AKAV and SBV are the etiological agents of arthrogryposis-hydranencephaly syndrome in ruminants, which causes considerable economic losses in the livestock industry. Here, we identified heparan sulfate proteoglycan as a major cellular attachment factor for the entry of AKAV and SBV. Moreover, we found that heparin is a strong inhibitor of AKAV and SBV infections. Revealing the molecular mechanisms of virus-host interactions is critical in order to understand virus biology and develop novel live attenuated vaccines

Large Magnetic-Field-Induced Strains in Sintered Chromium Tellurides

Sintered samples of Cr3Te4 and Cr2Te3 are found to show large strains accompanied by large volume changes under a magnetic field. In Cr3Te4, volume increases of deltaV/V = 500-1170 ppm by applying a magnetic field of 9 T are observed over the entire temperature range below 350 K. At room temperature, the deltaV/V value exceeds 1000 ppm, which is considerably larger than the maximum values reported for Cr-based magnets thus far and is comparable to the room-temperature value of forced-volume magnetostriction in invar alloys. Cr2Te3 show a large deltaV/V of 680 ppm when applying a magnetic field of 9 T at 200 K. Both samples display particularly large volume increases around the Curie temperature, where they also show negative thermal expansion due to microstructural effects, suggesting that the cooperation between anisotropic lattice deformation associated with the magnetic ordering and microstructural effects is essential for the manifestation of the large magnetic-field-induced volume changes.Comment: 6 pages, 6 figure

マイクロ波CTマンモグラフィの開発

24個の固定ダイポールアンテナを用いて三次元マイクロ波CT実験を行い，スーパーコンピュータを用いてForward-Backward Time Stepping（FBTS）法によるCT計算を行った．その結果得られた知見は，FBTS法が雑音に強いこと，及び計算の初期設定やキャリブレーション設定が精度向上に重要なことである．また計算モデル化が容易な広帯域平面アンテナの開発も行った．これらの知見を生かし，FBTS法マイクロ波CTマンモグラフィ装置の概念設計を行った

EDITORIAL

Ligand-mediated drug delivery systems have enormous potential for improving the efficacy of cancer treatment. In particular, Arg-Gly-Asp peptides are promising ligand molecules for targeting α_vβ₃/α_vβ₅ integrins, which are overexpressed in angiogenic sites and tumors, such as intractable human glioblastoma (U87MG). We here achieved highly efficient drug delivery to U87MG tumors by using a platinum anticancer drug-incorporating polymeric micelle (PM) with cyclic Arg-Gly-Asp (cRGD) ligand molecules. Intravital confocal laser scanning microscopy revealed that the cRGD-linked polymeric micelles (cRGD/m) accumulated rapidly and had high permeability from vessels into the tumor parenchyma compared with the PM having nontargeted ligand, “cyclic-Arg-Ala-Asp” (cRAD). As both cRGD/m- and cRAD-linked polymeric micelles have similar characteristics, including their size, surface charge, and the amount of incorporated drugs, it is likely that the selective and accelerated accumulation of cRGD/m into tumors occurred <i>via</i> an active internalization pathway, possibly transcytosis, thereby producing significant antitumor effects in an orthotopic mouse model of U87MG human glioblastoma