TY - JOUR
T1 - Characterization of an incompletely assembled major histocompatibility class I molecule (H-2Kb) associated with unusually long peptides
T2 - Implications for antigen processing and presentation
AU - Joyce, Sebastian
AU - Kuzushima, Kiyotaka
AU - Kepecs, Gilbert
AU - Angeletti, Ruth Hogue
AU - Nathenson, Stanley G.
PY - 1994/5/10
Y1 - 1994/5/10
N2 - We have identified two forms of a major histocompatibility complex (MHC) class I molecule, H-2Kb, distinguishable by specific antibodies through a study of a genetically engineered mouse cell line that overexpresses these molecules. One form, a complex associated with β2-microglobulin (native, β2m+ class I), is detectable by conformation-dependent antibodies. The other form, which remains after preclearing cell lysates of native class I, is only poorly, if at all, associated with β2-microglobulin (β2m- class I) and is detectable by an antiserum against the cytoplasmic tail region of H-2K molecules. Both forms are also present in normal cell lines. The affinity-purified native class I molecules bind short peptides (8 or 9 residues) and assemble tightly with β2-microglobulin. In striking contrast, the β2m- class I molecules bind peptides that are longer (>15 residues) than those bound to native class I molecules. This finding is consistent with the recent evidence that peptides longer than 8-10 amino acid residues are transported into the endoplasmic reticulum and suggests the possibility of a control step for peptide presentation by MHC in which the incompletely processed peptides bind to the heavy chain and a selected fraction undergoes final processing and presentation on the cell surface.
AB - We have identified two forms of a major histocompatibility complex (MHC) class I molecule, H-2Kb, distinguishable by specific antibodies through a study of a genetically engineered mouse cell line that overexpresses these molecules. One form, a complex associated with β2-microglobulin (native, β2m+ class I), is detectable by conformation-dependent antibodies. The other form, which remains after preclearing cell lysates of native class I, is only poorly, if at all, associated with β2-microglobulin (β2m- class I) and is detectable by an antiserum against the cytoplasmic tail region of H-2K molecules. Both forms are also present in normal cell lines. The affinity-purified native class I molecules bind short peptides (8 or 9 residues) and assemble tightly with β2-microglobulin. In striking contrast, the β2m- class I molecules bind peptides that are longer (>15 residues) than those bound to native class I molecules. This finding is consistent with the recent evidence that peptides longer than 8-10 amino acid residues are transported into the endoplasmic reticulum and suggests the possibility of a control step for peptide presentation by MHC in which the incompletely processed peptides bind to the heavy chain and a selected fraction undergoes final processing and presentation on the cell surface.
KW - Peptides
KW - β-microglobulin
KW - β-microglobulin class I
UR - http://www.scopus.com/inward/record.url?scp=0028296704&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028296704&partnerID=8YFLogxK
M3 - Article
C2 - 8183884
AN - SCOPUS:0028296704
SN - 0027-8424
VL - 91
SP - 4145
EP - 4149
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 10
ER -