Cardioviruses have a unique 2A protein (143 aa). During genome translation, the encephalomyocarditis virus (EMCV) 2A is released through a ribosome skipping event mitigated through C-terminal 2A sequences and by subsequent N-terminal reaction with viral 3Cpro. Although viral replication is cytoplasmic, mature 2A accumulates in nucleoli shortly after infection. Some protein also transiently associates with cytoplasmic 40S ribosomal subunits, an activity contributing to inhibition of cellular cap-dependent translation. Cardiovirus sequences predict an eIF4E binding site (aa 126–134) and a nuclear localization signal (NLS, aa 91–102), within 2A, both of which are functional during EMCV infection. Point mutations preventing eIF4E:2A interactions gave small-plaque phenotype viruses, but still inhibited cellular cap-dependent translation. Deletions within the NLS motif relocalized 2A to the cytoplasm and abrogated the inhibition of cap-dependent translation. A fusion protein linking the 2A NLS to eGFP was sufficient to redirect the reporter to the nucleus but not into nucleoli.
A key genomic characteristic that helps define Hantavirus as a genus of the family Bunyaviridae is the presence of distinctive terminal complementary nucleotides that promote the folding of the viral genomic segments into "panhandle" hairpin structures. The hantavirus nucleocapsid protein (N protein), which is encoded by the smallest of the three negative-sense genomic RNA segments, undergoes in vivo and in vitro trimerization. Trimeric hantavirus N protein specifically recognizes the panhandle structure formed by complementary base sequence of 5 and 3 ends of viral genomic RNA. N protein trimers from the Andes, Puumala, Prospect Hill, Seoul, and Sin Nombre viruses recognize their individual homologous panhandles as well as other hantavirus panhandles with high affinity. In contrast, these hantavirus N proteins bind with markedly reduced affinity to the panhandles from the genera Bunyavirus, Tospovirus, and Phlebovirus or Nairovirus. Interactions between most hantavirus N and heterologous hantavirus viral RNA panhandles are mediated by the nine terminal conserved nucleotides of the panhandle, whereas Sin Nombre virus N requires the first 23 nucleotides for high-affinity binding. Trimeric hantavirus N complexes undergo a prominent conformational change while interacting with panhandles from members of the genus Hantavirus but not while interacting with panhandles from viruses of other genera of the family Bunyaviridae. These data indicate that high-affinity interactions between trimeric N and hantavirus panhandles are conserved within the genus Hantavirus.Hantaviruses are classified as emerging viruses which cause two often fatal diseases that arise by infection of endothelial cells: hemorrhagic fever with renal syndrome and hantavirus cardiopulmonary syndrome (30-33). Each hantavirus is carried by one or a limited number of wild rodent species and transmitted to humans through the aerosol route. The two diseases associated with hantaviruses both cause striking increases in vascular permeability and are elicited by viruses such as Hantaan virus and Sin Nombre virus (SNV), respectively. Hemorrhagic fever with renal syndrome and hantavirus cardiopulmonary syndrome are generally restricted to the Old World and New World, respectively (34). Hantaviruses comprise a genus in the family Bunyaviridae. Members of this virus family have genomes composed of three minus-strand viral RNA (vRNA) segments whose mRNAs encode an RNA-dependent RNA polymerase (RdRp) (L segment), the nucleocapsid protein (N protein; S segment) and G1 and G2 glycoproteins (M segment). The G1 and G2 proteins are posttranslationally processed through the endoplasmic reticulum and Golgi apparatus and ultimately presented on the viral surface. These proteins enable viruses to enter new host cells via their attachment to integrin receptors (7,8). In the virion the three genomic RNA molecules form a complex with N protein and presumably with RdRp.During replication, assembly is initiated with the binding of nucleocapsid protein at a unique encapsidation si...
We have compared the analytical performance and biological variability of three commercially available bone resorption assays: Pyrilinks®-D, Osteomark®, and CrossLaps™, for the measurement of urinary free deoxypyridinoline (Dpd), cross-linked N-telopeptides of type I collagen (NTx), and linear C-telopeptides of type I collagen (CTx), respectively. The intraassay and interassay CVs for precision of the Dpd and NTx assays were <10% for analyte concentrations greater than the second calibrator (i.e., 3 nmol/L Dpd or 30 nmol bone collagen equivalents/L NTx). The CTx assay demonstrated poor precision for analyte concentration lower than the third calibrator (i.e., 200 μg/L). The NTx assay exhibited nonlinear recovery for sample dilutions prepared in buffer; however, this nonlinear recovery could be corrected for sample dilutions made in urine at a low analyte concentration. Supplement recoveries of each of the three assays were within 100% ± 10% on average. All three analytes showed stability through five freeze–thaw cycles. The mean day-to-day variations were 16% for Dpd, and 23% for both NTx and CTx. Similar diurnal rhythm was observed for all three assays on average, with the peak in the early morning and the nadir in the afternoon. Mean amplitude of the diurnal variation was 37% for Dpd and NTx, and 57% for CTx. Variations within the reference intervals for a healthy premenopausal population were 28% for Dpd, 57% for NTx, and 56% for CTx. Pyrilinks-D has demonstrated analytical precision and accuracy equal or superior to Osteomark and CrossLaps in all areas. Dpd exhibits the least biological variability day-to-day, within individuals across the diurnal cycle, and within a healthy premenopausal population.
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