NEST 2014: views from the trainees-talking about what matters in efforts to diversify the STEM workforce.

This paper summarizes the outcomes of a retreat designed to cultivate interactions between trainees at various training levels and provide them opportunities to share their training perspectives and expectations. Retreat outcomes are used to support the development of better science, technology, engineering, and mathematics training practices by informing the trainers’ perspective.

Apoptotic cells can deliver chemotherapeutics to engulfing macrophages and suppress inflammatory cytokine production.

Immunosuppression via cell-cell contact with apoptotic cells is a well studied immunological phenomenon. Although the original studies of immune repression used primary cells, which undergo spontaneous cell death or apoptosis in response to irradiation, more recent studies have relied on chemotherapeutic agents to induce apoptosis in cell lines. In this work, we demonstrate that Jurkat cells induced to die with actinomycin D suppressed inflammatory cytokine production by macrophages, whereas cells treated with etoposide did not.

Is the CvaA protein, encoded within the colicin V export gene cvaA, required for colicin V transport?

The antibacterial peptide toxin colicin V is exported from Escherichia coli cells by a signal sequence-independent, ABC export system. Export requires at least three proteins-membrane fusion protein CvaA, ABC export protein CvaB, and outer membrane protein TolC. The cvaA gene also encodes a second protein, CvaA, initiated from an in-frame translational re-start within the cvaA coding sequence.

Topology analysis of the colicin V export protein CvaA in Escherichia coli.

The antibacterial protein toxin colicin V is secreted from Escherichia coli cells by a dedicated export system that is a member of the multicomponent ATP-binding cassette (ABC) transporter family. At least three proteins, CvaA, CvaB, and TolC, are required for secretion via this signal sequence-independent pathway. In this study, the subcellular location and transmembrane organization of membrane fusion protein CvaA were investigated.

Functional complementation between bacterial MDR-like export systems: colicin V, alpha-hemolysin, and Erwinia protease.

The antibacterial protein Colicin V (ColV) is secreted from gram-negative bacteria by a signal sequence-independent pathway. The proteins that mediate the export of ColV share sequence similarities with components from other signal sequence-independent export systems such as those for alpha-hemolysin (Hly) and Erwinia protease (Prt). We report here that the intact HlyBD export system can export active ColV from Escherichia coli strains lacking the ColV export proteins CvaA and CvaB.