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Antigen1
*
Laboratory of Molecular and Cellular Immunology, Fondazione Andrea Cesalpino, Istituto I Clinica Medica, Università degli Studi di Roma "La Sapienza", Rome, Italy;
Laboratory of Medical Bacteriology and Mycology, Istituto Superiore di Sanità, Rome, Italy;
Division of Gastroenterology, Ospedale Molinette, Turin, Italy;
§
Chiron Corporation, Emeryville, CA 94608; and
¶
Institute Pasteur-Cenci Bolognetti, Rome, Italy
Hepatitis 
virus is a human pathogen that is responsible for a
severe form of hepatitis affecting hepatitis B envelope Ag carriers. We
have previously identified a series of hepatitis Ag (HDAg) epitopes
that are recognized by CD4+ T cell clones isolated
from infected subjects. Herein, we show that the presentation of
soluble HDAg to CD4+ T cell clones that are specific for
the HDAg(106–121) epitope was exceptionally
unaffected by the inhibition of the APC-processing machinery when APCs
were fixed with glutaraldehyde before Ag pulsing or treated with
chloroquine or brefeldin A. Interestingly, 5 h of pulsing was
strictly required for the efficient presentation of the
HDAg(106–121) epitope by fixed APCs, suggesting that some
form of extracellular processing had occurred. Indeed, fixed APCs were
able to present HDAg after only 1 h of pulsing when HDAg was
preincubated with serum for 5 h. More important, presentation was
completely abrogated when Ag was previously incubated in medium
containing serum in the presence of a potent inhibitor of trypsin
activity such as the secretory leukoprotease inhibitor. These results
show that HDAg may undergo extracellular processing and suggest that
the generation of immunogenic epitopes directly by serum proteases
could play a role in the immune response against hepatitis virus
during infection.
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