Screening Children for Social Determinants of Health: A Systematic Review.

CONTEXT: Screening children for social determinants of health (SDOHs) has gained attention in recent years, but there is a deficit in understanding the present state of the science. OBJECTIVE: To systematically review SDOH screening tools used with children, examine their psychometric properties, and evaluate how they detect early indicators of risk and inform care. DATA SOURCES: Comprehensive electronic search of PubMed, Cumulative Index to Nursing and Allied Health Literature, Embase, Cochrane Central Register of Controlled Trials, and Web of Science Core Collection. STUDY SELECTION: Studies in which a tool that screened children for multiple SDOHs (defined according to Healthy People 2020) was developed, tested, and/or employed. DATA EXTRACTION: Extraction domains included study characteristics, screening tool characteristics, SDOHs screened, and follow-up procedures. RESULTS: The search returned 6274 studies. We retained 17 studies encompassing 11 screeners. Study samples were diverse with respect to biological sex and race and/or ethnicity. Screening was primarily conducted in clinical settings with a parent or caregiver being the primary informant for all screeners. Psychometric properties were assessed for only 3 screeners. The most common SDOH domains screened included the family context and economic stability. Authors of the majority of studies described referrals and/or interventions that followed screening to address identified SDOHs. LIMITATIONS: Following the Healthy People 2020 SDOH definition may have excluded articles that other definitions would have captured. CONCLUSIONS: The extent to which SDOH screening accurately assessed a child's SDOHs was largely unevaluated. Authors of future research should also evaluate if referrals and interventions after the screening effectively address SDOHs and improve child well-being.

Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5α.

Restriction factors and pattern recognition receptors are important components of intrinsic cellular defenses against viral infection. Mammalian TRIM5α proteins are restriction factors and receptors that target the capsid cores of retroviruses and activate ubiquitin-dependent antiviral responses upon capsid recognition. Here, we report crystallographic and functional studies of the TRIM5α B-box 2 domain, which mediates higher-order assembly of TRIM5 proteins. The B-box can form both dimers and trimers, and the trimers can link multiple TRIM5α proteins into a hexagonal net that matches the lattice arrangement of capsid subunits and enables avid capsid binding. Two modes of conformational flexibility allow TRIM5α to accommodate the variable curvature of retroviral capsids. B-box mediated interactions also modulate TRIM5α's E3 ubiquitin ligase activity, by stereochemically restricting how the N-terminal RING domain can dimerize. Overall, these studies define important molecular details of cellular recognition of retroviruses, and how recognition links to downstream processes to disable the virus.