Table 1.

MHC Class I K^b-binding, Peptide Competition, and TAP-dependent Transport of Seven wt p53 Peptides

Kb binding peptides		UC50		CC50		IC50
		μg/ml		μg/ml		μg/ml
aa 119–127: VMCYSPPL		18		12		2.5
aa 122–130: TYSPLNKL		20		14		6
aa 123–131: YSPPLNKLF		4		0.5		>100
aa 127–134: LNKLFCQL		4		2		7
aa 158–166: AIYKKSQHM		2.7		0.3		4.5
aa 222–229: AGSEYTTI		100		18		70
aa 227–234: TTIHYKYM		7		1.1		6
SV9: FAPGNYPAL		0.1		0.2		ND

Seven wt p53-derived were characterized in an MHC class I binding assay (column 1; reference 42), peptide competition cytotoxicity assay (column 2; reference 41), and TAP-dependent translocation assay (column 3; reference 44). (UC₅₀) Peptide concentration resulting in 50% of the maximal upregulation of H-2K^b in the presence of the known H-2K^b-binding peptide Sendai virus NP 324–332 (61). (CC₅₀) Peptide concentration that inhibits 50% of the maximal lysis by CTL clone BTM recognizing the reference peptide KSPWFTTL derived from the MCF1233 virus (39). (IC₅₀) Concentration of competitor peptide that decreased the maximal amount of recovered glycosylated reporter peptide by 50% (44, 45). Indicated in bold are so-called anchor residues in the H-2K^b–binding motif described by Falk et al. (49).