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Volume 3 Issue 12, December 2002

Preparing peptides of appropriate length for class II major histocompatibility complex proteins takes place in the endoplasmic reticulum (yellow). The aminopeptidase responsible for trimming the peptides to eight or nine amino acids has been isolated and identified as ERAP1 (Saric et al., page 1169) and its function analyzed (York et al., page 1177). See also the News & Views by Falk and Rötschke on page 1121. Painting in acrylic on canvas by Katherine Ris.

Volume 3 Issue 12

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Editorial

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Correspondence

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Commentary

  • South Africa is in the throes of an AIDS epidemic compounded by tuberculosis. Nevertheless, responses to the recent launch of a colorful book promoting adolescent knowledge of HIV immunopathogenesis provide grounds for cautious optimism that education can induce a form of “social vaccination” in South Africa and elsewhere.

    • Siamon Gordon
    Commentary
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News & Views

  • Receptors in the immune system usually specialize in transmitting specific types of signals. However, by associating with two different signaling subunits, the receptor NKG2D can transmit distinct signals for either costimulation or full-fledged activation.

    • Eric O. Long
    News & Views

  • Proteolytic cleavage generates the peptide repertoire displayed by MHC class I. Now, an interferon-γ–inducible aminopeptidase in the endoplasmic reticulum has been identified as the final player in this complex process.

    • Kirsten Falk
    • Olaf Rötzschke
    News & Views

  • The recent demonstration that T cells can recognize a single foreign pMHC complex suggests that TCR triggering does not require aggregation. Or does it?

    • P.Anton van der Merwe
    News & Views

  • The source of Langerhans cells is controversial. New data show that the repopulation of these cells depends on how and to what extent, they are depleted from the skin.

    • Andrew Lucas
    • Gordon MacPherson
    News & Views
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