Search CTL/CD8+ T-Cell Epitope Database

Found 19 matching records:

Displaying record number 57301

HXB2 Location	Gag(71-79) p17(71-79) DNA(1000..1026)	Gag Epitope Map
Author Location	p17(71-79)
Epitope	`GSEELRSLY`	Epitope Alignment
Epitope Name	GY9
Subtype	B
Species (MHC/HLA)	(A*01)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Epitope GY9, GSEELRSLY, overlaps epitopes SL9 (SLYNTVATL) and RY11 (RSLYNTVATLY) and may be affected by mutations in these epitopes under study especially since positions R76 and Y79 are anchor residues.
Only immuno-proteasomal digestion generated substantial quantities of GY9.

References

Tenzer2009 Stefan Tenzer, Edmund Wee, Anne Burgevin, Guillaume Stewart-Jones, Lone Friis, Kasper Lamberth, Chih-hao Chang, Mikkel Harndahl, Mirjana Weimershaus, Jan Gerstoft, Nadja Akkad, Paul Klenerman, Lars Fugger, E. Yvonne Jones, Andrew J. McMichael, Søren Buus, Hansjörg Schild, Peter van Endert, and Astrid K. N. Iversen. Antigen Processing Influences HIV-Specific Cytotoxic T Lymphocyte Immunodominance. Nat. Immunol., 10(6):636-646, Jun 2009. PubMed ID: 19412183. Show all entries for this paper.

Displaying record number 57302

HXB2 Location	Gag(74-82) p17(74-82) DNA(1009..1035)	Gag Epitope Map
Author Location	p17(74-82)
Epitope	`ELRSLYNTV`	Epitope Alignment
Epitope Name	EV9
Subtype	B
Species (MHC/HLA)	(B*08)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Epitope EV9, ELRSLYNTV, overlaps epitopes SL9 (SLYNTVATL) and RY11 (RSLYNTVATLY) and may be affected by mutations in these epitopes especially since positions R76 and Y79 are anchor residues.
Subdominant EV9 was produced in ample quantities by both constitutive- and immuno-proteasomal digestion, but TAP transport disfavored its accumulation in the ER.

References

Displaying record number 57300

HXB2 Location	Gag(76-86) p17(76-86) DNA(1015..1047)	Gag Epitope Map
Author Location	p17(76-86)
Epitope	`RSLYNTVATLY`	Epitope Alignment
		Show epitope variants
Epitope Name	RY11
Subtype	B
Species (MHC/HLA)	human(A0201, A3002)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
RY11 was produced in relatively large amounts in precursor form by proteasomal digestion.
Immunodominant epitope RY11, RSLYNTVATLY, had several single variants - R76K, kSLYNTVATLY; Y79F, RSLfNTVATLY; T84V RSLYNTVAvLY; V82I, RSLYNTiATLY; and combined variants kSLfNTVATLY, kSLfNTiATLY, kSLfNTVAvLY and kSLfNTiAvLY.
N-terminally extended 10-mer peptides RSLYNTVATL and its R76K variant, kSLYNTVATL bound HLA-A*02 less well than 9-mers or C-terminally extended peptides.
Substitution Y79F resulted in minor proteasomal cleavage variations. The R76K substitution had a greater effect on cleavage when combined with Y79F or with Y79F, V82I, T84V than when combined with Y79F, T84V or Y79F, V82I.
TAP selectivity transported abundant amounts of A*30-RY11 into the ER; and ERAAP1,2-mediated trimming resulted in greater amounts of this A*30-RY11 than of the shorter A*29,B*44-LY9, LYNTVATLY.

References

Displaying record number 57182

HXB2 Location	Gag(77-85) p17(77-85) DNA(1018..1044)	Gag Epitope Map
Author Location	p17(77-85)
Epitope	`SLYNTVATL`	Epitope Alignment
		Show epitope variants
Epitope Name	SL9
Subtype	B
Species (MHC/HLA)	human(A*0201)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Immunodominant epitope, SL9, SLYNTVATL has common mutations at Y79F, SLfNTVATL; V82I, SLYNTiATL; and T84V, SLYNTVAvL; as well as combinations SLfNTVAvL, SLfNTiATL, SLYNTiAvL and SLfNTiAvL . These may be combined with the upstream substitution R76K.
SL9 was sparsely produced in its precursor forms (LL18 or R-SL9 or K-SL9) by proteasomal digestion.
While magnitude of response varied inter-patient, similar response was seen to all SL9 variants within one patient, regardless of HLA-A*0201-binding affinity. C-terminal extended SL9 variants, however, were recognized more often than N-terminal-extended variants showing that different length variants were differentially targeted within one patient.

References

Displaying record number 57298

HXB2 Location	Gag(77-86) p17(77-86) DNA(1018..1047)	Gag Epitope Map
Author Location	p17(77-86)
Epitope	`SLYNTVATLY`	Epitope Alignment
		Show epitope variants
Epitope Name	SY10
Subtype	B
Species (MHC/HLA)	human(A*02)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
HLA-A*02 binding to epitope SY10, SLYNTVATLY, was determined here. SY10 overlaps epitopes SL9 (SLYNTVATL) and RY11 (RSLYNTVATLY) and may be affected by mutations in these epitopes under study.
Variant SLfNTVATLY binds HLA-A*0201 more similarly to SL9, SLYNTVATL, and SLfNTiAvL than the exact same peptide lacking C-terminal Y, SLFNTVATL, does to HLA-A*0201. The C-terminal Y of SY10 profoundly affects peptide conformation.
ERAAP1,2-mediated trimming results in greater amounts of SY10 than of A*29,B*44-LY9, LYNTVATLY.

References

Displaying record number 57299

HXB2 Location	Gag(78-86) p17(78-86) DNA(1021..1047)	Gag Epitope Map
Author Location	p17(78-85)
Epitope	`LYNTVATLY`	Epitope Alignment
Epitope Name	LY9
Subtype	B
Species (MHC/HLA)	(A29, B44)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Epitope LY9, LYNTVATLY, overlaps epitopes SL9 (SLYNTVATL) and RY11 (RSLYNTVATLY) and may be affected by mutations in these epitopes under study.
Subdominant LY9 was consistently produced in relatively large amounts by proteasomal digestion; and high TAP selectivity transported it to the ER but ERAAP1,2-trimming was rapid, decreasing its concentration.

References

Displaying record number 57304

HXB2 Location	Gag(82-91) p17(82-91) DNA(1033..1062)	Gag Epitope Map
Author Location	p17(82-91)
Epitope	`IAVLYCVHQR`	Epitope Alignment
		Show epitope variants
Epitope Name	IR10
Subtype	B
Species (MHC/HLA)	(A*11)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
A variant of this epitope, IR10, IAVLYCVHQR is VR10, vAVLYCVHQR. IR10 and VR10 overlap epitopes SL9 (SLYNTVATL) and RY11 (RSLYNTVATLY) and may be affected by mutations in these epitopes under study.
Subdominant IR10 was rarely produced by either consitutive- or immuno-proteasomal digestion.

References

Displaying record number 57303

HXB2 Location	Gag(84-92) p17(84-92) DNA(1039..1065)	Gag Epitope Map
Author Location	p17(84-92)
Epitope	`TLYCVHQRI`	Epitope Alignment
Epitope Name	TI9
Subtype	B
Species (MHC/HLA)	(A*11)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Epitope TI9, TLYCVHQRI, overlaps epitopes SL9 (SLYNTVATL) and RY11 (RSLYNTVATLY) and may be affected by mutations in these epitopes under study.
Subdominant TI9 was produced in ample quantities by both constitutive- and immuno-proteasomal digestion.

References

Displaying record number 57311

HXB2 Location	Gag(259-267) p24(127-135) DNA(1564..1590)	Gag Epitope Map
Author Location	p24(127-135)
Epitope	`GEIYKRWII`	Epitope Alignment
Epitope Name	GI9
Subtype	B
Species (MHC/HLA)	human(B*08)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
GI9, GEIYKRWII, was produced by proteasomal cleavage and elicited CTL response.

References

Displaying record number 57309

HXB2 Location	Gag(259-268) p24(127-136) DNA(1564..1593)	Gag Epitope Map
Author Location	p24(127-136)
Epitope	`GEIYKRWIIL`	Epitope Alignment
Epitope Name	GL10
Subtype	B
Species (MHC/HLA)	human(A24, B08)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
GL10, GEIYKRWIIL, a KK10 minitope, was produced by proteasomal cleavage and elicited CTL response.

References

Displaying record number 57305

HXB2 Location	Gag(259-275) p24(127-143) DNA(1564..1614)	Gag Epitope Map
Author Location	p24(127-143)
Epitope	`GEIYKRWIILGLNKIVR`	Epitope Alignment
Epitope Name	GR16
Subtype	B
Species (MHC/HLA)	human(B*27)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Immunodominant epitope, GR16, GEIYKRWIILGLNKIVR, was produced by proteasomal cleavage and elicited CTL response.

References

Displaying record number 57306

HXB2 Location	Gag(259-277) p24(127-145) DNA(1564..1620)	Gag Epitope Map
Author Location	p24(127-145)
Epitope	`GEIYKRWIILGLNKIVRMY`	Epitope Alignment
Epitope Name	GR19
Subtype	B
Species (MHC/HLA)	human(B*27)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Immunodominant epitope, GR19, GEIYKRWIILGLNKIVRMY, was produced by proteasomal cleavage and elicited CTL response.

References

Displaying record number 57310

HXB2 Location	Gag(260-268) p24(128-136) DNA(1567..1593)	Gag Epitope Map
Author Location	p24(128-136)
Epitope	`EIYKRWIIL`	Epitope Alignment
Epitope Name	EL9
Subtype	B
Species (MHC/HLA)	human(A24, B08)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
EL9, EIYKRWIIL, a KK10 minitope, was produced by proteasomal cleavage and elicited CTL response.

References

Displaying record number 57308

HXB2 Location	Gag(261-268) p24(129-136) DNA(1570..1593)	Gag Epitope Map
Author Location	p24(129-136)
Epitope	`IYKRWIIL`	Epitope Alignment
Epitope Name	IL8
Subtype	B
Species (MHC/HLA)	human(A24, B08)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
IL8, IYKRWIIL, was produced by proteasomal cleavage and elicited CTL response.

References

Displaying record number 57307

HXB2 Location	Gag(261-270) p24(129-138) DNA(1570..1599)	Gag Epitope Map
Author Location	p24(129-138)
Epitope	`IYKRWIILGL`	Epitope Alignment
Epitope Name	IL10
Subtype	B
Species (MHC/HLA)	human(A24, B27)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Immunodominant KK10 minitope IL10, IYKRWIILGL,, was produced by proteasomal cleavage and elicited CTL response.

References

Displaying record number 57296

HXB2 Location	Gag(263-272) p24(131-140) DNA(1576..1605)	Gag Epitope Map
Author Location	p24(131-140)
Epitope	`KRWIILGLNK`	Epitope Alignment
Epitope Name	KK10
Subtype	B
Species (MHC/HLA)	human(B*27)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Immunodominant epitope KK10, KRWIILGLNK was the optimal peptide of all naturally occurring B-27-restricted p24 peptide forms as far as IFN-gamma production. Upon proteasomal processing, 11 KK10-containing peptides and 2 KK10 minitopes (variants ending at L138) were produced.

References

Displaying record number 57297

HXB2 Location	Gag(263-274) p24(131-142) DNA(1576..1611)	Gag Epitope Map
Author Location	p24(131-142)
Epitope	`KRWIILGLNKIV`	Epitope Alignment
Epitope Name	KV12
Subtype	B
Species (MHC/HLA)	human(B*27)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
Immunodominant epitope, KK12, KRWIILGLNKIV, was produced by proteasomal cleavage and elicited CTL response.

References

Displaying record number 57313

HXB2 Location	Gag(266-274) p24(134-142) DNA(1585..1611)	Gag Epitope Map
Author Location	p24(134-142)
Epitope	`IILGLNKIV`	Epitope Alignment
Epitope Name	IV9
Subtype	B
Species (MHC/HLA)	human(A*02)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
IV9, IILGLNKIV, was produced by proteasomal cleavage and elicited CTL response.

References

Displaying record number 57312

HXB2 Location	Gag(266-275) p24(134-143) DNA(1585..1614)	Gag Epitope Map
Author Location	p24(134-143)
Epitope	`IILGLNKIVR`	Epitope Alignment
Epitope Name	IR10
Subtype	B
Species (MHC/HLA)	human(A03, A11)
Immunogen	peptide-HLA interaction
Experimental methods	CD8 T-cell Elispot - IFNγ, HLA binding, Other
Keywords	epitope processing

Notes

Proteasomal cleavage effects on immunodominance were studied using 8 p17 and 11 p24 peptide variants. Epitope abundance due to Antigen processing was the prime influence on CTL dominance while HLA affinity was a moderate influence. Viral mutations modified processing [proteasomal digestion, transporter protein (TAP) affinity, Endoplasmic Reticulum Aminopeptidase (ERAAP) trimming].
IR10, IILGLNKIVR, was produced by proteasomal cleavage and elicited CTL response.