Katharine H. Wrighton

Cellular microbiology: Tagging proteins for the Clp protease

This study reveals that arginine phosphorylation tags proteins for degradation by the ClpCP protease

Bacterial physiology: Bridging the gap for lipopolysaccharides

This study provides evidence that lipopolysaccharides are pushed from the inner membrane to the outer membrane of the bacterial cell envelope over a protein bridge.

Correction: Bridging the gap for lipopolysaccharides

The image that accompanies this article was wrongly credited to Macmillan Publishers Limited in the online version. The correct credit is iStockphoto. This has now been corrected online. We apologize to the readers for any confusion caused.

The STING behind dengue virus infection

Stabell et al. have revealed why human dengue viruses do not replicate to high titres in primate models. They found that the stimulator of interferon genes (STING) protein, which induces the production of type I interferon in infected cells to reduce viral titres, is cleaved by the dengue virus protease NS2B3 in humans but not in key primate models. STING cleavage occurred at an RG motif at amino acids 78 and 79, decreasing markers of an innate immune response and increasing viral replication in human cells. The analyses of STING sequences from all placental animals in Genbank, as well as from 16 non-human primate cell lines, revealed that only STING from three small apes and three small rodents encodes this RG motif. As introducing this RG motif into STING from rhesus macaque, marmoset and mouse rendered it susceptible to cleavage by dengue virus NS2B3, engineering model organisms so that their STING contains this motif could enhance the study of dengue viruses in animals.

Viral infection: How histones go viral.

This study shows that histones are loaded onto unintegrated Moloney murine leukemia virus DNAs shortly after they have entered the nucleus.

Bacterial secretion: Reusing injected proteins

This study shows that T6SS components that are transferred between cells can be reused to assemble a fucntional T6SS system in the recipient.