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Volume 551 Issue 7681, 23 November 2017

The cover image shows the structure of the human peptide-loading complex (PLC) spanning the endoplasmic reticulum membrane of a cell (grey). As a key component of the immune response, the PLC is a dynamic complex responsible for loading peptide fragments from foreign bodies such as viruses onto major histocompatibility complex class I (MHC-I) molecules. These in turn present the fragments to the body’s immune cells to initiate the system’s fight back against the invaders. Robert Tamp㩠and his colleagues used electron cryo-microscopy to reveal the structure of the PLC, showing how the editing modules of the complex are centred around the peptide transporter TAP. They also find that loading the antigenic peptides onto MHC-I induces changes in its structure, thereby facilitating the release of stable peptide–MHC-I complexes to start the immune response. This allows the researchers to offer a glimpse of the mechanism behind the PLC, antigen processing and the way immunity mediated by MHC-I is induced. Cover image: Arne Moeller (MPI of Biophysics), Simon Trowitzsch and Robert Tamp㩠(Goethe Univ.)

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  • A large-scale study has been assessing microbial diversity by analysing DNA sequences from samples submitted by scientists around the globe. The initial results are now being used to create an open-access resource. See Article p.457

    • Jeroen Raes
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