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BACKGROUND: A poor diet can result from adverse social determinants of health and increases the risk of adverse pregnancy outcomes. OBJECTIVE: We aimed to assess, using data from the Nulliparous Pregnancy Outcomes Study: Monitoring Mothers-to-Be prospective cohort, whether nulliparous pregnant individuals who lived in a food desert were more likely to experience poorer periconceptional diet quality compared with those who did not live in a food desert. METHODS: The exposure was living in a food desert based on a spatial overview of food access indicators by income and supermarket access per the Food Access Research Atlas. The outcome was periconceptional diet quality per the Healthy Eating Index (HEI)-2010, analyzed by quartile (Q) from the highest or best (Q4, reference) to the lowest or worst dietary quality (Q1); and secondarily, nonadherence (yes or no) to 12 key aspects of dietary quality. RESULTS: Among 7,956 assessed individuals, 24.9% lived in a food desert. The mean HEI-2010 score was 61.1 of 100 (SD: 12.5). Poorer periconceptional dietary quality was more common among those who lived in a food desert compared with those who did not live in a food desert (Q4: 19.8%, Q3: 23.6%, Q2: 26.5%, and Q1: 30.0% vs. Q4: 26.8%, Q3: 25.8%, Q2: 24.5%, and Q1: 22.9%; overall P < 0.001). Individuals living in a food desert were more likely to report a diet in lower quartiles of the HEI-2010 (i.e., poorer dietary quality) (aOR: 1.34 per quartile; 95% CI: 1.21, 1.49). They were more likely to be nonadherent to recommended standards for 5 adequacy components of the HEI-2010, including fruit, total vegetables, greens and beans, seafood and plant proteins, and fatty acids, and less likely to report excess intake of empty calories. CONCLUSIONS: Nulliparous pregnant individuals living in a food desert were more likely to experience poorer periconceptional diet quality compared with those who did not live in a food desert.

Objective: To examine participants' experiences with nutrition education classes that were implemented with and designed to complement a cost-offset community-supported agriculture (CSA) programme.Design: Qualitative analysis of data from twenty-eight focus groups with ninety-six participants enrolled in Farm Fresh Foods for Healthy Kids (F3HK). Transcribed data were coded and analysed by a priori and emergent themes.Setting: Rural and micropolitan communities in New York, North Carolina, Vermont and Washington (USA).Participants: Ninety-six F3HK participants.Results: Participants found recipes and class activities helpful and reported improvements in nutrition knowledge, food preservation skills and home cooking behaviours for themselves and their children; they also reported that classes promoted a sense of community. Some educators better incorporated CSA produce into lessons, which participants reported as beneficial. Other obligations and class logistics were barriers to attendance; participants recommended that lessons be offered multiple times weekly at different times of day. Other suggestions included lengthening class duration to encourage social engagement; emphasising recipes to incorporate that week's CSA produce and pantry staples and offering additional strategies to incorporate children in classes.Conclusion: Complementing a cost-offset CSA with nutrition education may enhance programme benefits to low-income families by improving nutrition knowledge and cooking behaviours. However, future interventions will benefit from ongoing coordination between educators and local growing trajectories to maximise timely coverage of unfamiliar produce in lessons; synchronous scheduling of CSA pick-up and classes for participant convenience and creative strategies to engage children and/or provide childcare. [ABSTRACT FROM AUTHOR]

Summary: Osmosensing by transporter ProP is modulated by its cardiolipin (CL)‐dependent concentration at the poles of Escherichia coli cells. Other contributors to this phenomenon were sought with the BACterial Two‐Hybrid System (BACTH). The BACTH‐tagged variants T18‐ProP and T25‐ProP retained ProP function and localization. Their interaction confirmed the ProP homo‐dimerization previously established by protein crosslinking. YdhP, YjbJ and ClsA were prominent among the putative ProP interactors identified by the BACTH system. The functions of YdhP and YjbJ are unknown, although YjbJ is an abundant, osmotically induced, soluble protein. ClsA (CL Synthase A) had been shown to determine ProP localization by mediating CL synthesis. Unlike a deletion of clsA, deletion of ydhP or yjbJ had no effect on ProP localization or function. All three proteins were concentrated at the cell poles, but only ClsA localization was CL‐dependent. ClsA was shown to be N‐terminally processed and membrane‐anchored, with dual, cytoplasmic, catalytic domains. Active site amino acid replacements (H224A plus H404A) inactivated ClsA and compromised ProP localization. YdhP and YjbJ may be ClsA effectors, and interactions of YdhP, YjbJ and ClsA with ProP may reflect their colocalization at the cell poles. Targeted CL synthesis may contribute to the polar localization of CL, ClsA and ProP. [ABSTRACT FROM AUTHOR]

Osmosensing transporter ProP protects bacteria from osmotically induced dehydration by mediating the uptake of zwitterionic osmolytes. ProP activity is a sigmoidal function of the osmolality. ProP orthologues share an extended, cytoplasmic C-terminal domain. Orthologues with and without a C-terminal, α-helical coiled-coil domain respond similarly to the osmolality. ProP concentrates at the poles and septa of Escherichia coli cells in a cardiolipin (CL)-dependent manner. The roles of phospholipids and the C-terminal domain in subcellular localization of ProP were explored. Liposome association of peptides representing the C-terminal domains of ProP orthologues and variants in vitro was compared with subcellular localization of the corresponding orthologues and variants in vivo. In the absence of coiled-coil formation, the C-terminal domain bound liposomes and ProP concentrated at the cell poles in a CL-independent manner. The presence of the coiled-coil replaced those phenomena with CL-dependent binding and localization. The effects of amino acid replacements on lipid association of the C-terminal peptide fully recapitulated their effects on the subcellular localization of ProP. These data suggest that polar localization of ProP results from association of its C-terminal domain with the anionic lipid-enriched membrane at the cell poles. The coiled-coil domain present on only some orthologues renders that phenomenon CL-dependent. [ABSTRACT FROM AUTHOR]