The COVID-19 pandemic has shone a spotlight on how health outcomes are unequally distributed among different population groups, with disadvantaged communities and individuals being disproportionality affected in terms of infection, morbidity and mortality, as well as vaccine access. Recently, there has been considerable debate about how social disadvantage and inequality intersect with developmental processes to result in a heightened susceptibility to environmental stressors, economic shocks and large-scale health emergencies. We argue that DOHaD Society members can make important contributions to addressing issues of inequality and improving community resilience in response to COVID-19. In order to do so, it is beneficial to engage with and adopt a social justice framework. We detail how DOHaD can align its research and policy recommendations with a social justice perspective to ensure that we contribute to improving the health of present and future generations in an equitable and socially just way.

Flagellar dyneins are the molecular motors responsible for producing the propagating bending motions of cilia and flagella. They are located within a densely packed and highly organised super-macromolecular cytoskeletal structure known as the axoneme. Using the mesoscale simulation technique Fluctuating Finite Element Analysis (FFEA), which represents proteins as viscoelastic continuum objects subject to explicit thermal noise, we have quantified the constraints on the range of molecular conformations that can be explored by dynein-c within the crowded architecture of the axoneme. We subsequently assess the influence of crowding on the 3D exploration of microtubule-binding sites, and specifically on the axial step length. Our calculations combine experimental information on the shape, flexibility and environment of dynein-c from three distinct sources; negative stain electron microscopy, cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET). Our FFEA simulations show that the super-macromolecular organisation of multiple protein complexes into higher-order structures can have a significant influence on the effective flexibility of the individual molecular components, and may, therefore, play an important role in the physical mechanisms underlying their biological function.