Comparative immunopeptidomics of humans and their pathogens
Proceedings of the National Academy of Sciences, 2004•National Acad Sciences
Major histocompatibility complex class I molecules present peptides of 8-10 residues to
CD8+ T cells. We used 19 predicted proteomes to determine the influence of CD8+ T cell
immune surveillance on protein evolution in humans and microbial pathogens by predicting
immunopeptidomes, ie, sets of class I binding peptides present in proteomes. We find that
class I peptide binding specificities (i) have had little, if any, influence on the evolution of
immunopeptidomes and (ii) do not take advantage of biases in amino acid distribution in …
CD8+ T cells. We used 19 predicted proteomes to determine the influence of CD8+ T cell
immune surveillance on protein evolution in humans and microbial pathogens by predicting
immunopeptidomes, ie, sets of class I binding peptides present in proteomes. We find that
class I peptide binding specificities (i) have had little, if any, influence on the evolution of
immunopeptidomes and (ii) do not take advantage of biases in amino acid distribution in …
Major histocompatibility complex class I molecules present peptides of 8-10 residues to CD8+ T cells. We used 19 predicted proteomes to determine the influence of CD8+ T cell immune surveillance on protein evolution in humans and microbial pathogens by predicting immunopeptidomes, i.e., sets of class I binding peptides present in proteomes. We find that class I peptide binding specificities (i) have had little, if any, influence on the evolution of immunopeptidomes and (ii) do not take advantage of biases in amino acid distribution in proteins other than the concentration of hydrophobic residues in NH2-terminal leader sequences.
National Acad Sciences