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J. Exp. Med.,
Volume 188, Number 6, September 21, 1998 1105-1116
By
From the Centro Nacional de Biología Fundamental, Instituto de Salud Carlos III, 28220 Madrid,
Spain
Classical antigen presentation by major histocompatibility complex class I molecules involves
cytosolic processing of endogenously synthesized antigens by proteasomes and translocation of
processed peptides into the endoplasmic reticulum (ER) by transporters associated with antigen
presentation (TAP). Alternative pathways for processing of endogenous antigens, generally involving the ER, have been suggested but not fully proved. We analyzed the potential for class
I presentation of proteolytic maturation of secretory antigens in the exocytic pathway. We
found that hepatitis B (HB) virus secretory core protein HBe can efficiently deliver COOH-terminally located antigenic peptides for endogenous class I loading in the absence of TAP. Antigen presentation to specific cytotoxic T lymphocytes correlates with protein maturation at the
COOH terminus, since modification of maturation and transport of HBe through the secretory pathway alters antigen presentation. Both maturation and a necessary processing step occur in
the Golgi or post-Golgi compartment. Antigen presentation is independent of proteasome activity, but inhibitors of the trans-Golgi network resident protease furin inhibit both HBe maturation and antigen presentation. These results define a new antigen processing pathway located
in the secretory route, with a central role for proteolytic maturation mediated by the subtilisin
protease family member furin as an efficient source for antigen presentation.
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