Characterization of an incompletely assembled major histocompatibility class I molecule (H-2Kb) associated with unusually long peptides: Implications for antigen processing and presentation

Sebastian Joyce, Kiyotaka Kuzushima, Gilbert Kepecs, Ruth Hogue Angeletti, Stanley G. Nathenson

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)4145-4149
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue number10
StatePublished - May 10 1994

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Histocompatibility
Antigen Presentation
Peptides
Major Histocompatibility Complex
Cell Line
Antibodies
Endoplasmic Reticulum
Tail
Immune Sera
Amino Acids

Keywords

  • β-microglobulin
  • β-microglobulin class I
  • β-microglobulin class I
  • Peptides

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Characterization of an incompletely assembled major histocompatibility class I molecule (H-2Kb) associated with unusually long peptides : Implications for antigen processing and presentation. / Joyce, Sebastian; Kuzushima, Kiyotaka; Kepecs, Gilbert; Angeletti, Ruth Hogue; Nathenson, Stanley G.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, No. 10, 10.05.1994, p. 4145-4149.

Research output: Contribution to journalArticle

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