Assessing Performance of Contemporary Plant-Based Diets against the UK Dietary Guidelines: Findings from the Feeding the Future (FEED) Study.

Uncertainty remains about the composition of contemporary plant-based diets and whether they provide recommended nutrient intakes. We established Feeding the Future (FEED), an up-to-date online cohort of UK adults following different plant-based diets and diets containing meat and fish. We recruited 6342 participants aged 18-99 [omnivores (1562), flexitarians (1349), pescatarians (568), vegetarians (1292), and vegans (1571)] between February 2022 and December 2023, and measured diet using a food frequency questionnaire and free text. We compared personal characteristics and dietary intakes between diet groups and assessed compliance with dietary guidelines. Most participants met UK dietary recommendations for fruit and vegetables, sodium, and protein, although protein intakes were lowest among vegetarians and vegans. Omnivores did not meet the fibre recommendation and only vegans met the saturated fat recommendation. All diet groups exceeded the free sugars recommendation. Higher proportions of vegetarians and vegans were below the estimated average requirements (EARs) for zinc, iodine, selenium, and, in vegans, vitamins A and B12, whereas calcium intakes were similar across the diet groups. People following plant-based diets showed good compliance with most dietary targets, and their risk for inadequate intakes of certain nutrients might be mitigated by improved dietary choices and/or food fortification.

Probing the Solution Structure of IκB Kinase (IKK) Subunit γ and Its Interaction with Kaposi Sarcoma-associated Herpes Virus Flice-interacting Protein and IKK Subunit ß by EPR Spectroscopy.

Viral flice-interacting protein (vFLIP), encoded by the oncogenic Kaposi sarcoma-associated herpes virus (KSHV), constitutively activates the canonical nuclear factor κ-light-chain-enhancer of activated B cells (NF-κB) pathway. This is achieved through subversion of the IκB kinase (IKK) complex (or signalosome), which involves a physical interaction between vFLIP and the modulatory subunit IKKγ. Although this interaction has been examined both in vivo and in vitro, the mechanism by which vFLIP activates the kinase remains to be determined. Because IKKγ functions as a scaffold, recruiting both vFLIP and the IKKα/ß subunits, it has been proposed that binding of vFLIP could trigger a structural rearrangement in IKKγ conducive to activation. To investigate this hypothesis we engineered a series of mutants along the length of the IKKγ molecule that could be individually modified with nitroxide spin labels. Subsequent distance measurements using electron paramagnetic resonance spectroscopy combined with molecular modeling and molecular dynamics simulations revealed that IKKγ is a parallel coiled-coil whose response to binding of vFLIP or IKKß is localized twisting/stiffening and not large-scale rearrangements. The coiled-coil comprises N- and C-terminal regions with distinct registers accommodated by a twist: this structural motif is exploited by vFLIP, allowing it to bind and subsequently activate the NF-κB pathway. In vivo assays confirm that NF-κB activation by vFLIP only requires the N-terminal region up to the transition between the registers, which is located directly C-terminal of the vFLIP binding site.