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Influenza A virus RNA genome exists as eight-segmented ribonucleoprotein complexes containing viral RNA polymerase and nucleoprotein (vRNPs). Packaging of vRNPs and virus budding take place at the apical plasma membrane (APM). However, little is known about the molecular mechanisms of apical transport of newly synthesized vRNP. Transfection of fluorescent-labeled antibody and subsequent live cell imaging revealed that punctate vRNP signals moved along microtubules rapidly but intermittently in both directions, suggestive of vesicle trafficking. Using a series of Rab family protein, we demonstrated that progeny vRNP localized to recycling endosome (RE) in an active/GTP-bound Rab11-dependent manner. The vRNP interacted with Rab11 through viral RNA polymerase. The localization of vRNP to RE and subsequent accumulation to the APM were impaired by overexpression of Rab binding domains (RBD) of Rab11 family interacting proteins (Rab11-FIPs). Similarly, no APM accumulation was observed by overexpression of class II Rab11-FIP mutants lacking RBD. These results suggest that the progeny vRNP makes use of Rab11-dependent RE machinery for APM trafficking.

The genome of influenza type A virus consists of single-stranded RNAs of negative polarity. Progeny viral RNA (vRNA) replicated in the nucleus is nuclear-exported, and finally transported to the budding site beneath the plasma membrane. However, the precise process of the membrane targeting of vRNA is unclear, although viral proteins and cytoskeleton are thought to play roles. Here, we have visualized the translocation process of progeny vRNA using fluorescence in situ hybridization method. Our results provide an evidence of the involvement of vesicular trafficking in membrane targeting of progeny vRNA independent of that of viral membrane proteins.

Recent studies have demonstrated that kokumi substances, which enhance basic tastes and modify mouthfulness and continuity although they have no taste themselves, are perceived through the calcium-sensing receptor (CaSR). Screening by a CaSR assay and sensory evaluation have shown that γ-glutamyl-valyl-glycine (γ-Glu-Val-Gly) is a potent kokumi peptide. In our previous study, it was reported that the addition of γ-Glu-Val-Gly to chicken consomme significantly enhanced mouthfulness, continuity and thickness. In this study, the effect of γ-Glu-Val-Gly on reduced-fat peanut butter was investigated. Prior to the evaluation of the effect of γ-Glu-Val-Gly, a comparison test was conducted between full-fat model peanut butter and reduced-fat peanut butter. The sensory attributes in which the score of the full-fat model was significantly higher than that of the reduced-fat sample were used for the evaluation of the effect of γ-Glu-Val-Gly. The addition of γ-Glu-Val-Gly significantly enhanced thick flavour, aftertaste, and oiliness in the reduced-fat peanut butter. A kokumi peptide, γ-Glu-Val-Gly, can enhance thick flavour, aftertaste and oiliness in reduced-fat peanut butter. This suggests that addition of γ-Glu-Val-Gly can improve the flavour of low-fat foods.