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Introduction: During the coronavirus disease 2019 (COVID-19) vaccination campaign, non-English-communicating individuals have faced inequities in access to resources for vaccine education and uptake. We characterized the language translation status of states' COVID-19 vaccine websites to inform discussion on the sufficiency of translated information and strategies for expanding the availability of multilingual vaccine information. Methods: We identified the primary COVID-19 vaccine website for all 50 states, the District of Columbia, and the federal government ("jurisdictions") and determined the languages into which information about obtaining the vaccine (access) and vaccine safety and efficacy had been translated, as of October 2021. We compared these findings with data from the American Community Survey to determine how many individuals had these online resources available in their primary language. Results: Only 56% of jurisdictions provided professionally translated information about COVID-19 vaccine safety and efficacy, and only 50% provided professionally translated information about how to register for or obtain the COVID-19 vaccine, in at least one language. Consequently, â¼26 million Americans may not have accurate vaccine safety and efficacy information available, and â¼29 million Americans may not have vaccine access information available, from their jurisdiction in their primary language. Furthermore, translated information often was limited in scope and/or number of languages provided. Conclusion: Translation of COVID-19 vaccine information on state government websites currently is insufficient to meet the needs of non-English-communicating populations. This analysis can inform discussions about resource needs and operational considerations for adequate provision of multilingual, critical health information.
RESUMO
The mechanistic target of rapamycin (mTOR) kinase forms two multi-protein signaling complexes, mTORC1 and mTORC2, which are master regulators of cell growth, metabolism, survival and autophagy. Two of the subunits of these complexes are mLST8 and Raptor, ß-propeller proteins that stabilize the mTOR kinase and recruit substrates, respectively. Here we report that the eukaryotic chaperonin CCT plays a key role in mTORC assembly and signaling by folding both mLST8 and Raptor. A high resolution (4.0 Å) cryo-EM structure of the human mLST8-CCT intermediate isolated directly from cells shows mLST8 in a near-native state bound to CCT deep within the folding chamber between the two CCT rings, and interacting mainly with the disordered N- and C-termini of specific CCT subunits of both rings. These findings describe a unique function of CCT in mTORC assembly and a distinct binding site in CCT for mLST8, far from those found for similar ß-propeller proteins.