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Biomedical graduate research trainees are increasingly pursuing careers beyond academia in response to limited academic positions relative to the trainee population. Biomedical research training must therefore evolve alongside the shifting career landscape by circumventing a “hidden curriculum” to help trainees develop skills complementary to existing graduate training. Here, we describe an approach to implement “soft skills” training for a diverse population of biomedical graduate research trainees from the Duke University BioCoRE program. Qualitative data from the BioCoRE annual program survey revealed that trainees felt they were not meeting crucial benchmarks in areas often absent from graduate training. Responses to open-ended survey questions overwhelmingly focused on “soft skills,” including communication, conflict resolution, and time management. Using these themes as a guide, the BioCoRE Program Director and graduate student-led Professional Development Committee collaborated to design a monthly workshop series, enlisting support from human resources personnel, undergraduate student affairs offices, and senior graduate trainees with relevant expertise. The year-long workshop series covered a range of topics: personal branding, science communication, scientific storytelling, conflict resolution, time management, and job market preparation. Based on survey data, the inaugural series was well-received and cited as highly effective by attendees. Survey dissemination and analysis will continue in subsequent years to address new topics and anticipate emerging themes in the shifting career development landscape. Implementation of this workshop series demonstrates the ability of graduate programs to enhance trainee soft skills by leveraging the expertise of internal and local professional personnel.

The field of environmental epigenetics is uniquely suited to investigate biologic mechanisms that have the potential to link stressors to health disparities. However, it is common practice in basic epigenetic research to treat race as a covariable in large data analyses in a way that can perpetuate harmful biases without providing any biologic insight. In this article, we i) propose that epigenetic researchers open a dialogue about how and why race is employed in study designs and think critically about how this might perpetuate harmful biases; ii) call for interdisciplinary conversation and collaboration between epigeneticists and social scientists to promote the collection of more detailed social metrics, particularly institutional and structural metrics such as levels of discrimination that could improve our understanding of individual health outcomes; iii) encourage the development of standards and practices that promote full transparency about data collection methods, particularly with regard to race; and iv) encourage the field of epigenetics to continue to investigate how social structures contribute to biological health disparities, with a particular focus on the influence that structural racism may have in driving these health disparities.

Many viruses attach to target cells by binding to cell-surface glycans. To gain a better understanding of strategies used by viruses to engage carbohydrate receptors, we determined the crystal structures of reovirus attachment protein σ1 in complex with α-2,3-sialyllactose, α-2,6-sialyllactose, and α-2,8-di-siallylactose. All three oligosaccharides terminate in sialic acid, which serves as a receptor for the reovirus serotype studied here. The overall structure of σ1 resembles an elongated, filamentous trimer. It contains a globular head featuring a compact β-barrel, and a fibrous extension formed by seven repeating units of a triple β-spiral that is interrupted near its midpoint by a short α-helical coiled coil. The carbohydrate-binding site is located between β-spiral repeats two and three, distal from the head. In all three complexes, the terminal sialic acid forms almost all of the contacts with σ1 in an identical manner, while the remaining components of the oligosaccharides make little or no contacts. We used this structural information to guide mutagenesis studies to identify residues in σ1 that functionally engage sialic acid by assessing hemagglutination capacity and growth in murine erythroleukemia cells, which require sialic acid binding for productive infection. Our studies using σ1 mutant viruses reveal that residues 198, 202, 203, 204, and 205 are required for functional binding to sialic acid by reovirus. These findings provide insight into mechanisms of reovirus attachment to cell-surface glycans and contribute to an understanding of carbohydrate binding by viruses. They also establish a filamentous, trimeric carbohydrate-binding module that could potentially be used to endow other trimeric proteins with carbohydrate-binding properties.