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Volume 271, Number 44, Issue of November 1, 1996 pp. 27360-27365
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of a Lysozyme-Major Histocompatibility Complex Class II Molecule-loading Compartment as a Specialized Recycling Endosome in Murine B Lymphocytes

(Received for publication, June 4, 1996, and in revised form, August 5, 1996)

Jean-Michel Escola , Fabienne Deleuil , Espen Stang , Joëlle Boretto , Philippe Chavrier and Jean-Pierre Gorvel

From the  Centre d'Immunologie, INSERM-CNRS de Marseille-Luminy, Case 906, 13288 Marseille Cedex 09, France and the  Electron Microscopy Unit for Biological Sciences, Department of Biology, University of Oslo, Pb. 1062 Blindern, 0316 Oslo, Norway

We have previously identified an intracellular compartment involved in the association between processed lysozyme and IA^k major histocompatibility complex class II molecules (called the lysozyme-loading compartment (LLC)). Here, we show that the LLC polypeptide composition analyzed by two-dimensional gel electrophoresis shares similarities with that of early endosomes, but not with that of late endosomes. The transferrin receptor, a well known marker for both early and recycling endosomes, colocalizes with IA^k molecules in LLC. Moreover, both transferrin and fluid-phase markers have access to LLC after 15 min of internalization. In the presence of concanamycin B, SDS-stable dimer formation and transport of class II molecules out of LLC are impaired. In contrast, nocodazole treatment has no effect. These results suggest that LLC is a specialized compartment of the recycling pathway involved in lysozyme loading and in the targeting of lysozyme-major histocompatibility class II complexes toward the cell surface.

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