Carrier protein influences immunodominance of a known epitope: Implication in peptide vaccine design

Vaccine

Volumn 31, Issue 41, 2013, Pages 4682-4688

  Ghosh, Moumita ^a   Solanki, Ashish K ^b   Roy, Koushik ^a   Dhoke, Reema R ^b   Ashish, ^b   Roy, Syamal ^a  

^a INDIAN INSTITUTE OF CHEMICAL BIOLOGY   (India)

^b INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

Author keywords

Antigen processing; Antigen structure; Endoproteolysis; Immunodominance

Indexed keywords

AMINO TERMINAL KINETOPLASTID MEMBRANE PROTEIN 11; APICAL MEMBRANE ANTIGEN 1; BACTERIOPHAGE LAMBDA REPRESSOR PROTEIN; CARBOXYL TERMINAL KINETOPLASTID MEMBRANE PROTEIN 11; EPITOPE; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G ANTIBODY; KINETOPLASTID MEMBRANE PROTEIN 11; MEMBRANE PROTEIN; OVALBUMIN; PEPTIDE VACCINE; REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANTIBODY RESPONSE; ANTIBODY TITER; ANTIGEN PRESENTATION; ANTIGEN PRESENTING CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; LYMPHOCYTE PROLIFERATION; MOUSE; NONHUMAN; PLASMODIUM YOELII; PRIORITY JOURNAL; PROTEIN TRANSPORT; PROTEIN UNFOLDING; T LYMPHOCYTE;

AMA-1; AN EPITOPE OF AMA-1((136-148)); ANTIGEN PRESENTING CELL; ANTIGEN PROCESSING; ANTIGEN STRUCTURE; APC; C-KMP-11; DOMINANT T-CELL EPITOPE OF OVALBUMIN PROTEIN; ENDOPROTEOLYSIS; IMMUNODOMINANCE; IMMUNODOMINANT SEQUENCE OF BACTERIOPHAGE LAMBDA REPRESSOR N-TERMINAL SEQUENCE; KINETOPLASTID MEMBRANE PROTEIN-11; KMP-11; N-KMP-11; OVA((323-339)); PLASMODIUM YOELII APICAL MEMBRANE PROTEIN 1; PY; ΛR((12-26)); ΛR((12-26)) ENGINEERED AT THE C TERMINI OF KMP-11; ΛR((12-26)) ENGINEERED AT THE N TERMINI OF KMP-11;

ANIMALS; ANTIBODIES; BACTERIOPHAGE LAMBDA; CARRIER PROTEINS; DRUG CARRIERS; IMMUNODOMINANT EPITOPES; IMMUNOGLOBULIN G; IMMUNOLOGIC FACTORS; LEISHMANIA; MICE; MICE, INBRED BALB C; MICE, INBRED CBA; OVALBUMIN; PLASMODIUM YOELII; PROTOZOAN PROTEINS; RECOMBINANT FUSION PROTEINS; VACCINES, SUBUNIT; VIRAL PROTEINS;

EID: 84883597820     PISSN: 0264410X     EISSN: 18732518     Source Type: Journal    
DOI: 10.1016/j.vaccine.2013.06.110     Document Type: Article

References (42)

1. Davies M.N., Flower D.R. Harnessing bioinformatics to discover new vaccines. Drug Discovery Today 2007, 12:389-395.
2. Fournillier A., Dupeyrot P., Martin P., Parroche P., Pajot A., et al. Primary and memory T cell responses induced by hepatitis C virus multiepitope long peptides. Vaccine 2006, 24:3153-3164.
3. Kanto T., Hayashi N. Immunopathogenesis of hepatitis C virus infection: multifaceted strategies subverting innate and adaptive immunity. Intern Med 2006, 45:183-191.
4. Sette A., Fikes J. Epitope-based vaccines: an update on epitope identification, vaccine design and delivery. Curr Opin Immunol 2003, 15:461-470.
5. Sette A., Newman M., Livingston B., McKinney D., Sidney J., et al. Optimizing vaccine design for cellular processing, MHC binding and TCR recognition. Tissue Antigens 2002, 59:443-451.
6. Van Regenmortel M. Synthetic peptide vaccines and the search for neutralization B cell epitopes. The Open Vaccine Journal 2009, 2:33-44.
7. Barteling S.J. Possibilities and limitations of synthetic peptide vaccines. Adv Biotechnol Processes 1988, 10:25-60.
8. Bhattacharjya S., Awasthi S.K., Adiga P.R., Balaram P. Folded conformations of antigenic peptides from riboflavin carrier protein in aqueous hexafluoroacetone. Protein Sci 1998, 7:123-131.
9. Favre-Bonte S., Joly B., Forestier C. Consequences of reduction of Klebsiella pneumoniae capsule expression on interactions of this bacterium with epithelial cells. Infect Immun 1999, 67:554-561.
10. Lowenadler B., Lycke N., Svanholm C., Svennerholm A.M., Krook K., et al. T and B cell responses to chimeric proteins containing heterologous T helper epitopes inserted at different positions. Mol Immunol 1992, 29:1185-1190.
11. Weaver J.M., Lazarski C.A., Richards K.A., Chaves F.A., Jenks S.A., et al. Immunodominance of CD4 T cells to foreign antigens is peptide intrinsic and independent of molecular context: implications for vaccine design. J Immunol 2008, 181:3039-3048.
12. Carmicle S., Steede N.K., Landry S.J. Antigen three-dimensional structure guides the processing and presentation of helper T-cell epitopes. Mol Immunol 2007, 44:1159-1168.
13. Dai G., Carmicle S., Steede N.K., Landry S.J. Structural basis for helper T-cell and antibody epitope immunodominance in bacteriophage T4 Hsp10. Role of disordered loops. J Biol Chem 2002, 277:161-168.
14. Janssen R., Wauben M.H., Tommassen J. Quaternary structure of a carrier protein influences antigenicity and immunogenicity of an inserted T cell determinant. Int Immunol 1996, 8:829-836.
15. Landry S.J. Three-dimensional structure determines the pattern of CD4+ T-cell epitope dominance in influenza virus hemagglutinin. J Virol 2008, 82:1238-1248.
16. Lazarski C.A., Chaves F.A., Jenks S.A., Wu S., Richards K.A., et al. The kinetic stability of MHC class II:peptide complexes is a key parameter that dictates immunodominance. Immunity 2005, 23:29-40.
17. Leclerc C., Martineau P., Charbit A., Lo-Man R., Deriaud E., et al. Immunodominance of a recombinant T-cell epitope depends on its molecular environment. Mol Immunol 1993, 30:1561-1572.
18. Ma C., Whiteley P.E., Cameron P.M., Freed D.C., Pressey A., et al. Role of APC in the selection of immunodominant T cell epitopes. Journal of Immunology 1999, 163:6413-6423.
19. Schneider S.C., Ohmen J., Fosdick L., Gladstone B., Guo J., et al. Cutting edge: introduction of an endopeptidase cleavage motif into a determinant flanking region of hen egg lysozyme results in enhanced T cell determinant display. J Immunol 2000, 165:20-23.
20. Tietze C., Schlesinger P., Stahl P. Chloroquine and ammonium ion inhibit receptor-mediated endocytosis of mannose-glycoconjugates by macrophages: apparent inhibition of receptor recycling. Biochem Biophys Res Commun 1980, 93:1-8.
21. Sercarz E.E., Maverakis E. Mhc-guided processing: binding of large antigen fragments. Nat Rev Immunol 2003, 3:621-629.
22. Villadangos J.A., Ploegh H.L. Proteolysis in MHC class II antigen presentation: who's in charge?. Immunity 2000, 12:233-239.
23. Castellino F., Zappacosta F., Coligan J.E., Germain R.N. Large protein fragments as substrates for endocytic antigen capture by MHC class II molecules. J Immunol 1998, 161:4048-4057.
24. Lee P., Matsueda G.R., Allen P.M. T cell recognition of fibrinogen. A determinant on the A alpha-chain does not require processing. J Immunol 1988, 140:1063-1068.
25. Roy S., Leskowitz S. Structural requirements for T-cell recognition of tyrosine-azobenzene-arsonate in the rat and mouse. Mol Immunol 1984, 21:1031-1039.
26. Guillet J.G., Lai M.Z., Briner T.J., Smith J.A., Gefter M.L. Interaction of peptide antigens and class II major histocompatibility complex antigens. Nature 1986, 324:260-262.
27. Shimonkevitz R., Colon S., Kappler J.W., Marrack P., Grey H.M. Antigen recognition by H-2-restricted T cells. II. A tryptic ovalbumin peptide that substitutes for processed antigen. J Immunol 1984, 133:2067-2074.
28. Jardim A., Hanson S., Ullman B., McCubbin W.D., Kay C.M., et al. Cloning and structure-function analysis of the Leishmania donovani kinetoplastid membrane protein-11. Biochemical Journal 1995 Jan, 305-310.
29. Ziegler K., Unanue E.R. Identification of a macrophage antigen-processing event required for I-region-restricted antigen presentation to T lymphocytes. J Immunol 1981, 127:1869-1875.
30. Jackson L.R., Fox J.G. Institutional policies and guidelines on adjuvants and antibody production. ILAR journal/National Research Council. Institute of Laboratory Animal Resources 1995, 37:141-152.
31. Berridge M.V., Herst P.M., Tan A.S. Tetrazolium dyes as tools in cell biology: New insights into their cellular reduction. Biotechnol Ann Rev 2005, 11:127-152.
32. Coligan J.E., Tam J.P., Shao J. Production of antipeptide antisera. Curr Protoc Neurosci 2001, (chapter 5, unit 5.6).
33. Bailey G.S. The Chloramine T Method for Radiolabeling Protein. The Protein Protocols Handbook 1996, 66:5-66. 7.
34. Plasman N., Guillet J.G., Vray B. Impaired protein catabolism in Trypanosoma cruzi-infected macrophages: possible involvement in antigen presentation. Immunology 1995, 86:636-645.
35. Fields G.B., Noble R.L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int J Pept Protein Res 1990, 35:161-214.
36. Mimura Y., Mimura-Kimura Y., Doores K., Golgher D., Davis B.G., et al. Folding of an MHC class II-restricted tumor antigen controls its antigenicity via MHC-guided processing. Proc Natl Acad Sci USA 2007, 104:5983-5988.
37. Delamarre L., Pack M., Chang H., Mellman I., Trombetta E.S. Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate. Science 2005, 307:1630-1634.
38. Chapman H.A. Endosomal proteases in antigen presentation. Curr Opin Immunol 2006, 18:78-84.
39. Hubbard S.J., Eisenmenger F., Thornton J.M. Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci 1994, 3:757-768.
40. Cain C.C., Sipe D.M., Murphy R.F. Regulation of endocytic pH by the Na+, K+-ATPase in living cells. Proc Natl Acad Sci USA 1989, 86:544-548.
41. Blum J.S., Ma C., Kovats S. Antigen-presenting cells and the selection of immunodominant epitopes. Critical Reviews in Immunology 1997, 17:411-417.
42. Jorgensen J.L., Reay P.A., Ehrich E.W., Davis M.M. Molecular components of T-cell recognition. Annual Review of Immunology 1992, 10:835-873.