"A series of 15-mer peptides overlapping each other by 10 amino acids and a series of 9-mer peptides overlapping each other by 8 amino acids covering the HPV16 E6 protein have been described (20). To define the minimal and optimal amino acid sequences of the CD8 T-cell epitope, 8-mer, 10-mer, 11-mer, and homologous peptides (see Table 1) were synthesized as needed (CPC Scientific, Inc., San Jose, CA)."
Abstract
Human papillomavirus (HPV)-specific T-cell response to the HPV type 16 (HPV16) E6 protein has been shown to be associated with successful viral clearance. The patterns of CD8 T-cell epitopes within HPV16 E6 protein were previously studied in two women with HPV16 clearance. The goal of this study was to characterize these epitopes in terms of their minimal and optimal amino acid sequences and the human leukocyte antigen (HLA) restriction molecules. The presence of the epitope-specific memory T cells after viral clearance was also examined. In subject A, the dominant epitope was characterized to be E6 75-83 (KFYSKISEY), restricted by the HLA-B62 molecule, while that of subject B was E6 133-142 (HNIRGRWTGR), restricted by the HLA-A6801 molecule. Homologous epitopes were identified in five other high-risk HPV types for both of these epitopes, but they were not recognized by respective T-cell clone cells. An enzyme-linked immunospot assay or tetramer analysis was performed on peripheral blood mononuclear cells from blood samples collected after viral clearance but prior to isolation of the T-cell clones. The presence of epitope-specific memory T cells was demonstrated. These data suggest that HPV-specific memory T cells were generated in vivo and that they may remain in circulation many months, if not years, after viral clearance. Our findings broaden the spectrum of the CD8 T-cell epitopes of the HPV16 E6 protein. The characterization of novel T-cell epitopes and long-lasting epitope-specific memory T cells may be useful for the development of a potential epitope-based vaccine.
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Cesaro, Angela, Marcelo DT Torres, Rosa Gaglione, Eliana Dell’Olmo, Rocco Di Girolamo, Andrea Bosso, Elio Pizzo et al. ACS Nano 16, no. 2 (2022): 1880-1895.
Expression and isolation of recombinant peptides were carried out as previously described.20 CATH-2 and (ri)-r(P)ApoBSPro peptides were obtained from CPC Scientific Inc. (Sunnyvale, CA) and CASLO ApS (Kongens Lyngby, Denmark), respectively.
SAN JOSE, CA., Dec. 7, 2021/CPCNewswire/ — CPC Scientific Inc. has reached an exciting milestone as the company celebrates 20 years of delivering innovation and service to the peptide industry. Throughout the past two decades, CPC Scientific has provided consistent and quality peptide products to biotechnology and pharmaceutical industries to help bring life-changing therapeutics and […]
Liao, Z., Zhang, C., Ding, L., Moyers, J.S., Tang, J.X. and Beals, J.M. The FEBS Journal 289, no. 9 (2022): 2657-2671.
- Lilly Research Laboratories, Eli Lilly and Company, Lilly Corporate Center, Indianapolis, IN, USA.
Synthetic peptides of hIR-B were purchased from CPC Scientific..
Cazanave, S.C., Warren, A.D., Pacula, M., Touti, F., Zagorska, A., Gural, N., Huang, E.K., Sherman, S., Cheema, M., Ibarra, S. and Bates, J. Science Translational Medicine 13, no. 616 (2021): eabe8939.
All peptides were synthesized by CPC Scientific Inc. For fluorogenic assays, peptides were flanked with the fluorophore-quencher pair 5-FAM-CPQ2. For in vivo urine experiments, peptides were barcoded with Glu-Fib–derived and heavy isotope–labeled peptides. PEGylated peptides were pooled prepared before in vivo experiments and stored at 4°C in phosphate-buffered saline.
Diao, J., Komura, R., Sano, T., Pantua, H., Storek, K.M., Inaba, H., Ogawa, H., Noland, C.L., Peng, Y., Gloor, S.L. and Yan, D. Journal of Bacteriology 203, no. 13 (2021): 10-1128.
- Departments of Infectious Diseases, Structural Biology, Biochemical and Cellular Pharmacology, Translational Immunology, Pathology, Protein Chemistry, Early Discovery Biochemistry, Genentech, South San Francisco, California, USA
For the Lgt biochemical assay, the Pal-IAAC and Pal-IAAA peptides were synthesized by CPC Scientific.
Axiak-Bechtel, Sandra M., Stacey B. Leach, David G. Scholten, Jessica R. Newton-Northup, Brendan J. Johnson, H. E. Durham, Kenneth A. Gruber, and Michael F. Callahan. Pharmacology Research & Perspectives 9, no. 3 (2021): e00777.
TCMCB07 [a cyclic substituted melanocortin antagonist with the structure Ac- Nle- cyclo[Asp- Pro- DNal(2’)-Arg- Trp- Lys]- DVal- DPro- NH2] was manufactured by CPC Scientific Inc. under cGMP conditions. Active pharmaceutical ingredient was dissolved in milliQ water at 10 mg ml−1, sterile filtered [..]”
Olsson, N., Heberling, M.L., Zhang, L., Jhunjhunwala, S., Phung, Q.T., Lin, S., Anania, V.G., Lill, J.R. and Elias, J.E. Frontiers in Immunology 12 (2021): 662443.
- Department of Microchemistry, Proteomics and Lipidomics, Genentech, South San Francisco, CA, United States
- Department of OMNI Biomarker Development, Genentech, South San Francisco, CA, United States
In total 30 synthetic peptides covering a total of 22 SNP sites and two potential neoantigens, were purchased from CPC Scientific (Sunnyvale, CA) with a purity of >70%, dissolved in 0.1% FA and quality checked at a concentration of 250 fmol by mass spectrometry.