Myriophyllum aquaticum is an aquatic plant of still or slow flowing waters. The species mostly occurs in its emerged growth form in dense stands, but submerged shoots can also be found. Due to its rapid growth, M. aquaticum is considered one of the most important aquatic weeds worldwide. In southern Europe, M. aquaticum occurs in irrigation and drainage systems, rice fields and lowland wetlands. In this study, root development and growth response of M. aquaticum to different water levels and nutrient availabilities were investigated in a rhizotron experiment under Central European climatic conditions. The species shows an ability to respond to drained soil conditions by a rapid root growth (up to >1 cm day )1 ), resulting in a deep root system under drained conditions. In waterlogged soil, the root system spreads more horizontally. Root density increased with increasing nutrient availability. Root:shoot ratio increased significantly with decreasing nutrient availability. In addition, total shoot length, shoot biomass, root biomass and total biomass differed significantly between different water levels and different nutrient availabilities. Relative growth rate increased with increasing water level and nutrient availability. Shoot porosity was higher in nutrient rich substrate than in nutrient low substrate. Root porosity increased with increasing water level. In conclusion, M. aquaticum shows a high tolerance to different water levels, which may be important for future habitat conditions in waterbodies and wetlands in Central Europe under the impact of global change with increased water level fluctuations.

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The transporter associated with antigen processing (TAP) translocates antigenic peptides into the endoplasmic reticulum (ER) lumen for loading onto MHC class I molecules. This is a key step in the control of viral infections through CD8+ T-cells. The herpes simplex virus type-1 encodes an 88 amino acid long species-specific TAP inhibitor, ICP47, that functions as a high affinity competitor for the peptide binding site on TAP. It has previously been suggested that the inhibitory function of ICP47 resides within the N-terminal region (residues 1–35). Here we show that mutation of the highly conserved 50PLL52 motif within the central region of ICP47 attenuates its inhibitory capacity. Taking advantage of the human cytomegalovirus-encoded TAP inhibitor US6 as a luminal sensor for conformational changes of TAP, we demonstrated that the 50PLL52 motif is essential for freezing of the TAP conformation. Moreover, hierarchical functional interaction sites on TAP dependent on 50PLL52 could be defined using a comprehensive set of human-rat TAP chimeras. This data broadens our understanding of the molecular mechanism underpinning TAP inhibition by ICP47, to include the 50PLL52 sequence as a stabilizer that tethers the TAP-ICP47 complex in an inward-facing conformation.

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