MHC molecules protect T cell epitopes against proteolytic destruction
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MHC molecules protect T cell epitopes against proteolytic destruction. / Mouritsen, S; Meldal, M; Werdelin, O; Buus, Anette Stryhn; Buus, S.
I: Journal of Immunology, Bind 149, Nr. 6, 1992, s. 1987-93.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - MHC molecules protect T cell epitopes against proteolytic destruction
AU - Mouritsen, S
AU - Meldal, M
AU - Werdelin, O
AU - Buus, Anette Stryhn
AU - Buus, S
N1 - Keywords: Amino Acid Sequence; Animals; Cell-Free System; Endopeptidases; Epitopes; Histocompatibility Antigens Class II; Mice; Molecular Sequence Data; Muramidase; Peptides; Protein Binding; T-Lymphocytes
PY - 1992
Y1 - 1992
N2 - There is a subtle duality in the role of proteolytic enzymes in Ag processing. They are required to fragment protein Ag ingested by APC. However, prolonged exposure to proteolytic enzymes may lead to a complete degradation of the Ag, leaving nothing for the T cell system to recognize. What ensures that some of the Ag is salvaged? Using a cell-free system we demonstrate that an Ag fragment, once bound to a MHC class II molecule, is effectively protected against proteolytic destruction by cathepsin B and pronase E. The bound fragment, however, can be modified by aminopeptidase N. We suggest that MHC class II molecules play an important regulatory role in the physiologic processing of Ag.
AB - There is a subtle duality in the role of proteolytic enzymes in Ag processing. They are required to fragment protein Ag ingested by APC. However, prolonged exposure to proteolytic enzymes may lead to a complete degradation of the Ag, leaving nothing for the T cell system to recognize. What ensures that some of the Ag is salvaged? Using a cell-free system we demonstrate that an Ag fragment, once bound to a MHC class II molecule, is effectively protected against proteolytic destruction by cathepsin B and pronase E. The bound fragment, however, can be modified by aminopeptidase N. We suggest that MHC class II molecules play an important regulatory role in the physiologic processing of Ag.
M3 - Journal article
C2 - 1381392
VL - 149
SP - 1987
EP - 1993
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 6
ER -
ID: 9946257