Recognition of HIV-derived B and T cell epitopes displayed on filamentous phages.
The amino acid sequence of HIV reverse transcriptase (RT) from residue 248 to residue 262 was expressed on the surface of filamentous phage fd, fused to the major coat protein gVIIIp. The chimeric phage was used to assess the ability of anti-RT (248-262) human T cell lines and clones to become activated by the phage-displayed peptide. The RT peptide displayed on phage was recognized by the T-cells and induced production of Abs. However, not all T cells raised against the synthetic RT (248-262) peptide could respond. Lack of recognition did not depend on differences in the ability of different APCs to present the phage, but was apparently determined by the TCR specificity. The results presented here may be relevant to the design of recombinant protein-based subunit vaccines.
De Berardinis
P
P
Institute of Protein Biochemistry and Enzymology, CNR, Naples, Italy.
D'Apice
L
L
Prisco
A
A
Ombra
M N
MN
Barba
P
P
Del Pozzo
G
G
Petukhov
S
S
Malik
P
P
Perham
R N
RN
Guardiola
J
J
D000818:Animals; D002478:Cells, Cultured; D018985:Epitopes, B-Lymphocyte / Q000276:immunology*; D018984:Epitopes, T-Lymphocyte / Q000276:immunology*; D005260:Female; D054303:HIV Reverse Transcriptase / Q000276:immunology*; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D010446:Peptide Fragments / Q000276:immunology; D011948:Receptors, Antigen, T-Cell / Q000276:immunology; D013601:T-Lymphocytes / Q000276:immunology* / Q000821:virology
D018985:Epitopes, B-Lymphocyte; D018984:Epitopes, T-Lymphocyte; D010446:Peptide Fragments; D011948:Receptors, Antigen, T-Cell; D054303:HIV Reverse Transcriptase