Immunization with a novel chimeric peptide representing B and T cell epitopes from HER2 extracellular domain (HER2 ECD) for breast cancer

Tumor Biology

Volumn 35, Issue 12, 2014, Pages 12049-12057

  Mahdavi, Manijeh ^a   Keyhanfar, Mehrnaz ^b   Jafarian, Abbas ^a   Mohabatkar, Hassan ^b   Rabbani, Mohammad ^a  

^a ISFAHAN UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^b UNIVERSITY OF ISFAHAN   (Iran)

Author keywords

Breast cancer; Discontinuous B cell epitope; HER2 receptor; Peptide vaccines; T cell epitope

Indexed keywords

CANCER VACCINE; CHIMERIC PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPITOPE; PEPTIDE ANTIBODY; TRASTUZUMAB; MONOCLONAL ANTIBODY; PEPTIDE; PROTEIN BINDING;

ACTIVE IMMUNIZATION; AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIBODY RESPONSE; ANTIBODY TITER; ANTIGENICITY; ARTICLE; B LYMPHOCYTE; BIOINFORMATICS; BREAST CANCER; CANCER IMMUNIZATION; CANCER INHIBITION; CELL PROLIFERATION; CELL SUSPENSION; CHIMERA; CONTROLLED STUDY; CROSS REACTION; CRYSTAL STRUCTURE; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; IMMUNOGENICITY; MEASLES VIRUS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; T LYMPHOCYTE; TUMOR GROWTH; ANIMAL; BREAST TUMOR; CHEMICAL STRUCTURE; CHEMISTRY; IMMUNIZATION; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN DOMAIN; TUMOR CELL LINE;

ANIMALS; ANTIBODIES, MONOCLONAL; BASE SEQUENCE; BREAST NEOPLASMS; CELL LINE, TUMOR; CELL PROLIFERATION; EPITOPES, B-LYMPHOCYTE; EPITOPES, T-LYMPHOCYTE; FEMALE; IMMUNIZATION; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; RECEPTOR, ERBB-2;

EID: 84925285768     PISSN: 10104283     EISSN: 14230380     Source Type: Journal    
DOI: 10.1007/s13277-014-2503-y     Document Type: Article

References (47)

1. Correa I, Plunkett T. Update on HER-2 as a target for cancer therapy HER2/neu peptides as tumour vaccines for T cell recognition. Breast Cancer Res. 2001;3:399–403.
2. Carter PJ. Potent antibody therapeutics by design. Nat Rev Immunol. 2006;6:343–57.
3. Jager D, Knuth A. Antibodies and vaccines—hope or illusion? Breast. 2005;14:631–5.
4. Milani A, Sangiolo D, Montemurro F, Aglietta M, et al. Active immunotherapy in HER2 overexpressing breast cancer: current status and future perspectives. Ann Oncol. 2013;24(7):1740–8.
5. Garrett JT, Kaumaya P, Pei D, Dalbey R et al (2007). Peptide based B cell epitope vaccines targeting HER-2/Neu. Dissertation, Ohio State University
6. Ladjemi MZ, Jacot W, Pèlegrin A, Navarro-Teulon I. Vaccination anti-HER2: l’avenir du ciblage immunologique de HER2? Review Article. Pathol Biol. 2011;59:173–82.
7. Dakappagari NK, Pyles J, Parihar R, Carson WE, et al. Multi-human epidermal growth factor receptor-2 B cell epitope peptide vaccine mediates superior antitumour responses. J Immunol. 2003;170:4242–53.
8. Milich DR. Synthetic T and B cell recognition sites: implications for vaccine development. Adv Immunol. 1989;45:195–282.
9. Gangwara RS, Shil P, Sapkala GN, Khanc SA, et al. Induction of virus-specific neutralizing immune response against West Nile and Japanese encephalitis viruses by chimeric peptides representing T-helper and B-cell epitopes. Vir Res. 2012;163:40–50.
10. Miyako H, Kametani Y, Katano I, Ito R, et al. Antitumor effect of New HER2 peptide vaccination based on B cell epitope. Anticancer Res. 2011;31:3361–8.
11. Mahdavi M, Mohabatkar H, Keyhanfar M, Jafarian Dehkordi A, et al. Linear and conformational B cell epitope prediction of HER 2 ECD-subdomain III by in silico methods. Asian Pac J Cancer Prev. 2012;13:3053–9.
12. Mahdavi M, Keyhanfar M, Moreau V, Mohabatkar H, et al. In silico design of discontinuous peptides representative of B and T-cell epitopes from HER2-ECD as potential novel cancer peptide vaccines. Asian Pac J Cancer Prev. 2013;14:5973–81.
13. Jasinska J, Wagner S, Radauer C, Sedivy R, et al. Inhibition of tumour cell growth by antibodies induced after vaccination with peptides derived from the extracellular domain of HER-2/Neu. Int J Cancer. 2003;107:976–83.
14. Zhang AL, Xue H, Ling XG, Gao Y, et al. Anti-HER-2 engineering antibody ChA21 inhibits growth and induces apoptosis of SK-OV-3 cells. J Exp Clin Cancer Res. 2010;29:23–32.
15. Kaumaya PTP, Kobs-Conrad S, DiGeorge AM, Stevens V. De novo engineering of protein immunogenic and antigenic determinants. In: Anantharamaiah GM, Basava C, editors. Peptides, design, synthesis & biological activity. Boston: Birkhauser; 1994. p. 133–64.
16. Kaumaya PTP. Synthetic peptide vaccines: dream or reality. In: Schneider CH, editor. Peptides in immunology. United Kingdom: Wiley; 1996. p. 117–48.
17. Partidos CD, Steward MW. Prediction and identification of a T cell epitope in the fusion protein of measles virus immunodominant in mice and humans. J Gen Virol. 1990;71:2099–105.
18. Maupetit J, Derreumaux P, Tuffery P. PEP-FOLD: an online resource for de novo peptide structure prediction. Nucleic Acids Res. 2009;37:498–503.
19. DeLano WL. The PyMOL molecular graphics system. San Carlos: DeLano Scientific; 2002.
20. Scott WRP, Hünenberger PH, Tironi IG, Mark AE, et al. The GROMOS biomolecular simulation program package. J Phys Chem A. 1999;103:3596–607.
21. Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 1997;18:2714–23.
22. Yokoyama WM (1995) Production of monoclonal antibodies. In: Current Protocols in Immunology, John Wiley & Sonc
23. Tabll A, Khalil SB, El-Shenawy RM, Esmat G, et al. Establishment of hybrid cell lines producing monoclonal antibodies to a synthetic peptide from the E1 region of the hepatitis C virus. J Immunoass Immunochem. 2007;29:91–104.
24. Hornbeck P (1991) Enzyme-linked immunosorbent assays. In: Current Protocols in Immunology, John Wiley & Sonc
25. Larry M, Lantz BJ, Fowlkes IS, Janis VG (2001) Preparation of cells and reagents for flow cytometry. In: Current Protocols in Immunology, Wiley
26. Kolaskar AS, Tongaonkar PC. A semi-empirical method for prediction of antigenic determinants on protein antigens. FEBS Lett. 1990;276:172–4.
27. Deulofeut H, Iglesias A, Mikael N, Bing DH, et al. Cellular recognition and HLA restriction of a midsequence HBsAg peptide in hepatitis B vaccinated individuals. Mol Immunol. 1993;30:941–8.
28. Dakappagari NK, Douglas DB, Triozzi PL, Stevens VC, et al. Prevention of mammary tumours with a chimeric Her-2 B-cell epitope peptide vaccine. Cancer Res. 2000;60:3782–9.
29. Wang B, Kaumaya PTP, Cohn DE. Immunization with synthetic VEGF peptides in ovarian cancer. Gyn Oncol. 2010;119:564–70.
30. Sundaram R, Lynch MP, Rawale SV, Sun Y, et al. De novo design of peptide immunogens that mimic the coiled coil region of human T-cell leukemia virus type-1 glycoprotein 21 transmembrane subunit for induction of native protein reactive neutralizing antibodies. J Biol Chem. 2004;279:141–51.
31. Boyer CM, Pusztai L, Wiener JR, Xu FJ, et al. Relative cytotoxic activity of immunotoxins reactive with different epitopes on the extracellular domain of the c-erbB-2 (HER-2/neu) gene product p185. Int J Cancer. 1999;82:525–31.
32. Wang JN, Feng JN, Yua M, Xua M, et al. Structural analysis of the epitopes on erbB2 interacted with inhibitory or non-inhibitor monoclonal antibodies. Mol Immunol. 2004;40:963–9.
33. Zhang W, Xiong Y, Zhao M, Zou H, et al. Prediction of conformational B-cell epitopes from 3D structures by random forests with a distance-based feature. BMC Bioinform. 2011;12:341–8.
34. Siyi H, Zhiqiang Z, Liangwei L, Liang C, et al. Epitope mapping and structural analysis of an anti-ErbB2 antibody A21: molecular basis for tumour inhibitory mechanism. Proteins. 2008;70:938–49.
35. Haro I, Gomara MJ. Design of synthetic peptidic constructs for the vaccine development against viral infections. Curr Protein Pept Sci. 2004;5:425–33.
36. Aguilar RM, Talamantes FJ, Bustamante J, Muñoz J, Treviño LR, et al. Multiple antigen peptide dendrimer elicits antibodies for detecting rat and mouse growth hormone binding proteins. J Pept Sci. 2009;15:78–88.
37. Jalali A, Sankian M, Tavakkol-Afshari J, Jaafari MR. Induction of tumour-specific immunity by multi-epitope rat HER2/neu-derived peptides encapsulated in LPD Nanoparticles. Nanomed Nanotech Biol Med. 2012;8:692–701.
38. Singh R, Rothman AL, Potts J, Guirakhoo F, et al. Sequential immunization with heterologous chimeric flaviviruses induces broad-spectrum cross-reactive CD8+ T cell responses. J Infect Dis. 2010;202:223–33.
39. Axelsena TV, Holma A, Christiansena G, Birkelund S. Identification of the shortest AB-peptide generating highly specific antibodies against the C-terminal end of amyloid-B42. Vaccine. 2011;29:3260–9.
40. Ripoll DR. Conformational study of a peptide epitope shows large preferences for beta-turn conformations. Int J Pept Protein Res. 1992;40:575–81.
41. Dakappagari NK, Lute KD, Rawale S, Steele JT, et al. Conformational HER-2/neu B-cell epitope peptide vaccine designed to incorporate two native disulfide bonds enhances tumour cell binding and antitumour activities. J Biol Chem. 2005;280:54–63.
42. Chen SW, Van Regenmortel MH, Pellequer JL. Structure-activity relationships in peptide-antibody complexes: implications for epitope prediction and development of synthetic peptide vaccines. Curr Med Chem. 2009;16:953–9.
43. Yarden Y, Peles E. Biochemical analysis of the ligand for the neu oncogenic receptor. Biochem. 1991;30:3543–50.
44. Lupu R, Colomer R, Zugmaier G, Sarup J, Shepard M, Slamon D, et al. Direct interaction of a ligand for the erbB2 oncogene product with the EGF receptor and p185erbB2. Sci. 1990;249:1552–5.
45. Stancovski I, Hurwitz E, Leitner O, Ullrich A, Yarden Y, Sela M. Mechanistic aspects of the opposing effects of monoclonal antibodies to the ERBB2 receptor on tumor growth. Proc Natl Acad Sci USA. 1991;88:8691–5.
46. Hurwitz E, Stancovski I, Sela M, Yarden Y. Suppression and promotion of tumor growth by monoclonal antibodies to ErbB-2 differentially correlate with cellular uptake. Proc Natl Acad Sci U S A. 1995;92:3353–7.
47. Courtenay-Luck NS, Epenetos AA, Moore R, Larche M, Pectasides D, Dhokia B, et al. Development of primary and secondary immune responses to mouse monoclonal antibodies used in the diagnosis and therapy of malignant neoplasms. Cancer Res. 1986;46(12 Pt 1):6489–93.