The inter-relationship between the age of carrot roots at harvest and infection by Mycocentrospora acerina in storage

Infection of carrot roots by Mycocenlrospora acerina in chill storage (3.5 °C) following inoculation with chlamydospores was studied in 1973–74 and 1974–75. AREAS of intact periderm were only rarely infected, and the high level of periderm resistance predominated over other variables. However, wound infection tended to increase with depth of wound and with increasing age of the plants at harvest. Irrespective of age of root or depth of wound, roots were comparatively resistant to infection at harvest and early in storage, resistance being expressed as a restriction of mycelial growth on the wound surface or localisation of the lesion. Increasing susceptibility with time in storage, depth of wounds, or age at harvest, resulted in larger numbers of inoculated sites becoming infected and a more rapid development from localised to progressive lesions.     

The cytokine interleukin-5 (IL-5) effects cotransport of its receptor subunits to the nucleus in vitro

Interleukin (IL)-5 is central in regulating eosinophilia in allergic disease and parasitic infections. We have recently shown that human (h) IL-5 both possesses a functional nuclear localization signal capable of targeting a heterologous protein to the nucleus and localises to the nucleus of intact receptor-expressing cells. In this study, the extracellular domains of the hIL-5 α- and β-receptor subunits were expressed in baculovirus, fluorescently labelled and assayed for nuclear targeting in vitro in the absence and presence of IL-5. The β-subunit, which lacks IL-5 binding activity, only accumulated in the nucleus in the presence of both the hIL-5 binding α-subunit and hIL-5. The IL-5-binding α-subunit showed similar results. IL-5 thus effected nuclear transport of its α- and β-receptor subunits apparently through a ‘piggy back' mechanism, raising the possibility that IL-5's nuclear signalling role may be to cotarget its receptor subunits to the nucleus. This is the first demonstration of nuclear protein piggy back transport in vitro.