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Current Drug Discovery Technologies

Editor-in-Chief

ISSN (Print): 1570-1638
ISSN (Online): 1875-6220

Research Article

Oligopeptides for Immunotherapy Approaches in Ovarian Cancer Treatment

Author(s): Darja Kanduc*

Volume 16, Issue 3, 2019

Page: [285 - 289] Pages: 5

DOI: 10.2174/1570163815666180525071740

Price: $65

Abstract

Background: Anti-ovarian cancer vaccines based on minimal immune determinants uniquely expressed in ovarian cancer biomarkers appear to promise a high level of sensitivity and specificity for ovarian cancer immunodiagnostics, immunoprevention, and immunotherapy.

Methods: Using the Pir Peptide Match program, three ovarian cancer biomarkers – namely, sperm surface protein Sp17, WAP four-disulfide core domain protein 2, and müllerian-inhibiting substance – were searched for unique peptide segments not shared with other human proteins. Then, the unique peptide segments were assembled to define oligopeptides potentially usable as synthetic ovarian cancer antigens.

Results and Conclusion: This study describes a methodology for constructing ovarian cancer biomarkerderived oligopeptide constructs that might induce powerful, specific, and non-crossreactive immune responses against ovarian cancer.

Keywords: Sperm surface protein Sp17, WAP four-disulfide core domain protein 2, müllerian-inhibiting substance, human proteome, low-similarity peptides, synthetic oligopeptide constructs, anti-ovarian cancer vaccines.

Graphical Abstract
[1]
Ferlay J, Soerjomataram I, Dikshit R, et al. Cancer incidence and mortality worldwide: Sources, methods and major patterns in GLOBOCAN 2012. Int J Cancer 2015; 136: E359-86.
[2]
Jayson GC, Kohn EC, Kitchener HC, Ledermann JA. Ovarian cancer. Lancet 2014; 384: 1376-88.
[3]
Berek J, Taylor P, McGuire W, Smith LM, Schultes B, Nicodemus CF. Oregovomab maintenance monoimmunotherapy does not improve outcomes in advanced ovarian cancer. J Clin Oncol 2009; 27: 418-25.
[4]
Sabbatini P, Harter P, Scambia G, et al. Abagovomab as maintenance therapy in patients with epithelial ovarian cancer: a phase III trial of the AGO OVAR, COGI, GINECO, and GEICO--the MIMOSA study. J Clin Oncol 2013; 31: 1554-61.
[5]
Leffers N, Daemen T, Helfrich W, et al. Antigen-specific active immunotherapy for ovarian cancer. Cochrane Database Syst Rev 2014; (9): CD007287
[6]
Oza AM, Cook AD, Pfisterer J, et al. Standard chemotherapy with or without bevacizumab for women with newly diagnosed ovarian cancer (ICON7): Overall survival results of a phase 3 randomised trial. Lancet Oncol 2015; 16: 928-36.
[7]
Longuespée R, Boyon C, Desmons A, et al. Ovarian cancer molecular pathology. Cancer Metastasis Rev 2012; 31: 713-32.
[8]
Sölétormos G, Duffy MJ, Hassan SOA, et al. Clinical use of cancer biomarkers in epithelial ovarian cancer: Updated guidelines from the European Group on Tumor Markers (EGTM). Int J Gynecol Cancer 2016; 26: 43-51.
[9]
Markman M. Limitations to the use of the CA-125 antigen level in ovarian cancer. Curr Oncol Rep 2003; 5: 263-4.
[10]
Karlan BY, Alvarez RD, Strauss JF III. Evolving paradigms in research and care in ovarian cancers. Obstet Gynecol 2016; 128: 771-4.
[11]
Kanduc D. Immunogenicity, immunopathogenicity, and immunotolerance in one graph. Anticancer Agents Med Chem 2015; 15: 1264-8.
[12]
Huang J, Hu W, Sood AK. Prognostic biomarkers in ovarian cancer. Cancer Biomark 2010; 8: 231-51.
[13]
Spinosa JP, Kanduc D. Ovarian cancer: designing effective vaccines and specific diagnostic tools. Immunotherapy 2014; 6: 35-41.
[14]
Kanduc D. Immunogenicity in peptide-immunotherapy: From self/nonself to similar/dissimilar sequences. Adv Exp Med Biol 2008; 640: 198-207.
[15]
Kanduc D. Epitopic peptides with low similarity to the host proteome: towards biological therapies without side effects. Expert Opin Biol Ther 2009; 9: 45-53.
[16]
Lucchese G, Stufano A, Kanduc D. Proposing low-similarity peptide vaccines against Mycobacterium tuberculosis. J Biomed Biotechnol 2010; 2010832341
[17]
Lucchese A, Serpico R, Crincoli V, Shoenfeld Y, Kanduc D. Sequence uniqueness as a molecular signature of HIV-1-derived B-cell epitopes. Int J Immunopathol Pharmacol 2009; 22: 639-46.
[18]
Lucchese G, Stufano A, Kanduc D. Proteome-guided search for influenza A B-cell epitope. FEMS Immunol Med Microbiol 2009; 57: 88-92.
[19]
Kanduc D, Fanizzi FP, Lucchese G, Stevanovic S, Sinha AA, Mittelman A. NMR probing of in silico identification of anti-HPV16 E7 mAb linear peptide epitope. Peptides 2004; 25: 243-50.
[20]
Dummer R, Mittelman A, Fanizzi FP, Lucchese G, Willers J, Kanduc D. Non-self-discrimination as a driving concept in the identification of an immunodominant HMW-MAA epitopic peptide sequence by autoantibodies from melanoma cancer patients. Int J Cancer 2004; 111: 720-6.
[21]
Willers J, Lucchese A, Mittelman A, Dummer R, Kanduc D. Definition of anti-tyrosinase MAb T311 linear determinant by proteome-based similarity analysis. Exp Dermatol 2005; 14: 543-50.
[22]
Lucchese A, Mittelman A, Tessitore L, Serpico R, Sinha AA, Kanduc D. Proteomic definition of a desmoglein linear determinant common to Pemphigus vulgaris and Pemphigus foliaceous. J Transl Med 2006; 4: 37.
[23]
Lucchese A, Stevanovic S, Sinha AA, Mittelman A, Kanduc D. Role of MHC II affinity and molecular mimicry in defining anti-HER-2/neu MAb-3 linear peptide epitope. Peptides 2003; 24: 193-7.
[24]
Mittelman A, Tiwari R, Lucchese G, Willers J, Dummer R, Kanduc D. Identification of monoclonal anti-HMW-MAA antibody linear peptide epitope by proteomic database mining. J Invest Dermatol 2004; 123: 670-5.
[25]
Kanduc D, Tessitore L, Lucchese G, Kusalik A, Farber E, Marincola FM. Sequence uniqueness and sequence variability as modulating factors of human anti-HCV humoral immune response. Cancer Immunol Immunother 2008; 57: 1215-23.
[26]
La Marca A, Volpe A. The anti-Mullerian hormone and ovarian cancer. Hum Reprod Update 2007; 13: 265-73.
[27]
Abdel-Azeez HA, Labib HA, Sharaf SM, Refai AN. HE4 and mesothelin: novel biomarkers of ovarian carcinoma in patients with pelvic masses. Asian Pac J Cancer Prev 2010; 11: 111-6.
[28]
Haltia UM, Hallamaa M, Tapper J, et al. Roles of human epididymis protein 4, carbohydrate antigen 125, inhibin B and anti-Müllerian hormone in the differential diagnosis and follow-up of ovarian granulosa cell tumors. Gynecol Oncol 2017; 144: 83-9.
[29]
Färkkilä A, Koskela S, Bryk S, et al. The clinical utility of serum anti-Müllerian hormone in the follow-up of ovarian adult-type granulosa cell tumors. A comparative study with inhibin B. Int J Cancer 2015; 137: 1661-71.
[30]
Geerts I, Vergote I, Neven P, Billen J. The role of inhibins B and antimüllerian hormone for diagnosis and follow-up of granulosa cell tumors. Int J Gynecol Cancer 2009; 19: 847-55.
[31]
Hamed EO, Ahmed H, Sedeek OB, Mohammed AM, Abd-Alla AA, Abdel Ghaffar HM. Significance of HE4 estimation in comparison with CA125 in diagnosis of ovarian cancer and assessment of treatment response. Diagn Pathol 2013; 8: 11.
[32]
Fujiwara H, Suzuki M, Takeshima N, et al. Evaluation of human epididymis protein 4 (HE4) and Risk of Ovarian Malignancy Algorithm (ROMA) as diagnostic tools of type I and type II epithelial ovarian cancer in Japanese women. Tumour Biol 2015; 36: 1045-53.
[33]
Kristjansdottir B, Levan K, Partheen K, Sundfeldt K. Diagnostic performance of the biomarkers HE4 and CA125 in type I and type II epithelial ovarian cancer. Gynecol Oncol 2013; 131: 52-8.
[34]
Chiriva-Internati M, Grizzi F, Weidanz JA, et al. A NOD/SCID tumor model for human ovarian cancer that allows tracking of tumor progression through the biomarker Sp17. J Immunol Methods 2007; 321: 86-93.
[35]
Straughn JM Jr, Shaw DR, Guerrero A, et al. Expression of sperm protein 17 (Sp17) in ovarian cancer. Int J Cancer 2004; 108: 805-11.
[36]
Nakazato T, Kanuma T, Tamura T, Faried LS, Aoki H, Minegishi T. Sperm protein 17 influences the tissue-specific malignancy of clear cell adenocarcinoma in human epithelial ovarian cancer. Int J Gynecol Cancer 2007; 17: 426-32.
[37]
Skates SJ, Horick N, Yu Y, et al. Preoperative sensitivity and specificity for early-stage ovarian cancer when combining cancer antigen CA-125II, CA 15-3, CA 72-4, and macrophage colony-stimulating factor using mixtures of multivariate normal distributions. J Clin Oncol 2004; 22: 4059-66.
[38]
Yin BW, Lloyd KO. Molecular cloning of the CA125 ovarian cancer antigen: identification as a new mucin, MUC16. J Biol Chem 2001; 276: 27371-5.
[39]
Scholler N, Urban N. CA125 in ovarian cancer. Biomarkers Med 2007; 1: 513-23.
[40]
Abd Hamid UM, Royle L, Saldova R, et al. A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression. Glycobiology 2008; 18: 1105-18.
[41]
Cornelissen LA, Van Vliet SJ. A bitter sweet symphony: Immune responses to altered O-glycan epitopes in cancer. Biomolecules 2016; 6(2)pii E26
[42]
The UniProt Consortium. UniProt: The universal protein knowledgebase. Nucleic Acids Res 2017; 45: D158-69.
[43]
Lucchese G, Stufano A, Trost B, Kusalik A, Kanduc D. Peptidology: short amino acid modules in cell biology and immunology. Amino Acids 2007; 33: 703-7.
[44]
Kanduc D. Homology, similarity, and identity in peptide epitope immunodefinition. J Pept Sci 2012; 18: 487-94.
[45]
Kanduc D. Pentapeptides as minimal functional units in cell biology and immunology. Curr Protein Pept Sci 2013; 14: 111-20.
[46]
Chen C, Li Z, Huang H, Suzek BE, Wu CH. UniProt Consortium. A fast Peptide Match service for UniProt Knowledgebase. Bioinformatics 2013; 29: 2808-9.
[47]
Källberg M, Wang H, Wang S, et al. Template-based protein structure modeling using the RaptorX web server. Nat Protoc 2012; 7: 1511-22.
[48]
Capone G, Novello G, Fasano C, et al. The oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strand. BMC Bioinformatics 2010; 11: 383.
[49]
Andreu D, Albericio F, Solé NA, Munson MC, Ferrer M, Barany G. Formation of disulfide bonds in synthetic peptides and proteins. Methods Mol Biol 1994; 35: 91-169.
[50]
Niu S, Huang T, Feng KY, et al. Inter- and intra-chain disulfide bond prediction based on optimal feature selection. Protein Pept Lett 2013; 20: 324-35.
[51]
Lucchese G, Kanduc D. Potential crossreactivity of human immune responses against HCMV glycoprotein B. Curr Drug Discov Technol 2016; 13: 16-24.
[52]
Kanduc D. Peptides for anti-Ebolavirus vaccines. Curr Drug Discov Technol 2016; 13: 225-31.
[53]
Kanduc D. Peptide cross-reactivity: the original sin of vaccines. Front Biosci 2012; 4: 1393-401.
[54]
Kanduc D, Shoenfeld Y. From HBV to HPV: Designing vaccines for extensive and intensive vaccination campaigns worldwide. Autoimmun Rev 2016; 15: 1054-61.

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