![]() ![]() Even during typical epidemic years, despite the availability of influenza vaccines, approximately 250,000 to 500,000 people die worldwide due to severe complications associated with influenza virus infections (World Health Organization ). This has been highlighted by the regular occurrence of human cases of infection with highly pathogenic H5N1 avian influenza viruses since 2003 ( 46) and by the emergence of a new H1N1 influenza virus of swine origin in 2009 ( 33). Influenza virus continues to pose a serious threat to worldwide public health due to its rapid and unpredictable evolution. Furthermore, the existence of cell lines stably expressing the complementing GFP fragment will facilitate applications to many other viral and nonviral systems. This new virus, or adaptations of it, will be of use in elucidating many aspects of influenza virus host cell interactions as well as in screening for new antiviral compounds. Our data establish the potential of split-GFP-based recombinant viruses for the tracking of viral proteins during a quasi-wild-type infection. Following nuclear export, vRNPs showed a transient pericentriolar accumulation and intermittent rapid (∼1 μm/s), directional movements in the cytoplasm, dependent on both microtubules and actin filaments. ![]() This system was used to characterize the intranuclear dynamics of PB2 by fluorescence correlation spectroscopy and to visualize the trafficking of viral ribonucleoproteins (vRNPs) by dynamic light microscopy in live infected cells. The viral PB2 proteins were fused to the 16 C-terminal amino acids of the GFP, whereas the large transcomplementing GFP fragment was supplied by transient or stable expression in cultured cells that were permissive to infection. 23:102–107, 2005) to produce a quasi-wild-type recombinant A/WSN/33/influenza virus which allows expression of individually fluorescent PB2 polymerase subunits in infected cells. To circumvent this limitation, we used the split-green fluorescent protein (split-GFP) system (S. ![]() This is largely due to the difficulty of encoding fluorescent fusion proteins within the viral genome. One of my peace lilies had been in the same pot for more than 10 years so it was well overdue to be divided.Īs you can see in the photo below it was getting too big for the pot and it hadn’t bloomed for a couple of years so it was really time for division.Studies on the intracellular trafficking of influenza virus ribonucleoproteins are currently limited by the lack of a method enabling their visualization during infection in single cells. Some people are concerned about damaging their plant by dividing it and prefer to repot it in a larger container and that’s ok, but bear in mind that peace lilies can get quite big after five to 10 years of growth. If your peace lily has outgrown its pot but it only has one stalk or crown you won’t be able to divide it, so in this case just repot the plant into a larger pot. Roots begin growing out the bottom of the pot.The soil dries out very quickly after watering.The plant produces less flowers or stops flowering altogether.You’ll know it’s time to divide your peace lily when: Peace lilies (Spathiphyllum) can live happily in the same pot for many years but eventually they’ll outgrow the pot. ![]()
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