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High-containment laboratories (HCLs) conduct critical research on infectious diseases, provide diagnostic services, and produce vaccines for the world's most dangerous pathogens, often called high-consequence pathogens (HCPs). The modernization of HCLs has led to an increasingly cyber-connected laboratory infrastructure. The unique cyberphysical elements of these laboratories and the critical data they generate pose cybersecurity concerns specific to these laboratories. Cyberbiosecurity, the discipline devoted to the study of cybersecurity risks in conjunction with biological risks, is a relatively new field for which few approaches have been developed to identify, assess, and mitigate cyber risks in biological research and diagnostic environments. This study provides a novel approach for cybersecurity risk assessment and identification of risk mitigation measures by applying an asset-impact analysis to the unique environment of HCLs. First, we identified the common cyber and cyberphysical systems in HCLs, summarizing the typical cyber-workflow. We then analyzed the potential adverse outcomes arising from a compromise of these cyber and cyberphysical systems, broadly categorizing potential consequences as relevant to scientific advancement, public health, worker safety, security, and the financial wellbeing of these laboratories. Finally, we discussed potential risk mitigation strategies, leaning heavily on the cybersecurity materials produced by the Center for Internet Security (CIS), including the CIS Controls®, that can serve as a guide for HCL operators to begin the process of implementing risk mitigation measures to reduce their cyberbiorisk and considering the integration of cyber risk management into existing biorisk management practices. This paper provides a discussion to raise awareness among laboratory decision-makers of these critical risks to safety and security within HCLs. Furthermore, this paper can serve as a guide for evaluating cyberbiorisks specific to a laboratory by identifying cyber-connected assets and the impacts associated with a compromise of those assets.
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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.
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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.