- 1) Collawn, J. F., Wallace, C. J., Proudfoot, A. E., and Paterson, Y., Monoclonal antibodies as probes of conformational changes in protein-engineered cytochrome c. J. Biol. Chem., 263, 8625-8634 (1988).
- 2) Hoylaerts, M. F., and Millan, J. L., Site-directed mutagenesis and epitope-mapped monoclonal antibodies define a catalytically important conformational difference between human placental and germ cell alkaline phosphatase. Eur. J. Biochem., 202, 605-616 (1991).
- 3) Prasad, L., Sharma, S., Vandonselaar, M., Quail, J. W., Lee, J. S., Waygood, E. B., Wilson, K. S., Dauter, Z., and Delbaere, L. T., Evaluation of mutagenesis for epitope mapping. Structure of an antibody-protein antigen complex. J. Biol. Chem., 268, 10705-10708 (1993).
- 4) Moudgil, K. D., Sercarz, E. E., and Grewal, I. S., Modulation of the immunogenicity of antigenic determinants by their flanking residues. Immunol. Today, 19, 217-220 (1998).
- 5) Shastri, N., Miller, A., and Sercarz, E. E., Amino acid residues distant from the determinant region can profoundly affect activation of T cell clones by related antigens. J. Immunol., 136, 371-376 (1986).
- 6) Bhayani, H., Carbone, F. R., and Paterson, Y., The activation of pigeon cytochrome c-specific T cell hybridomas by antigenic peptides is influenced by non-native sequences at the amino terminus of the determinant. J. Immunol., 141, 377-382 (1988).
- 7) Vacchio, M. S., Berzofsky, J. A., Krzych, U., Smith, J. A., Hodes, R. J., and Finnegan, A., Sequences outside a minimal immunodominant site exert negative effects on recognition by staphylococcal nuclease-specific T cell clones. J. Immunol., 143, 2814-2819 (1989).
- 8) Liu, Z., Williams, K. P., Chang, Y.-H., and Smith, J. A., Single amino acid substitution alters T cell determinant selection during antigen processing of Staphylococcus aureus nuclease. J. Immunol., 146, 438-443 (1991).
- 9) Kim, B. S., and Jang, Y.-S., Constraints in antigen processing result in unresponsiveness to a T cell epitope of hen egg lysozyme in C57BL/6 mice. Eur. J. Immunol., 22, 775-782 (1992).
- 10) Hisatsune, T., Ametani, A., Nishijima, K., Enomoto, A., and Kaminogawa, S., Strong influence of the processing of the antigen on negative effects on T cell activation by regions outside the determinant area of bovine αs1-casein. Biosci. Biotechnol. Biochem., 56, 1616-1618 (1992).
- 11) Godkin, A. J., Davenport, M. P., Willis, A., Jewell, D. P., and Hill, A. V. S., Use of complete eluted peptide sequence data from HLA-DR and -DQ molecules to predict T cell epitopes, and the influence of the nonbinding terminal regions of ligands in epitope selection. J. Immunol., 161, 850-858 (1998).
- 12) Antoniou, A. N., Blackwood, S.-L., Mazzeo, D., and Watts, C., Control of antigen presentation by a single protease cleavage site. Immunity, 12, 391-398 (2000).
- 13) Schneider, S. C., Ohmen, J., Fosdick, L., Gladstone, B., Guo, J., Ametani, A., Sercarz, E. E., and Deng, H., 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., 165, 20-23 (2000).
- 14) Deng, H., Apple, R., Clare-Salzler, M., Trembleau, S., Mathis, D., Adorini, L., and Sercarz, E., Determinant capture as a possible mechanism of protection afforded by major histocompatibility complex class II molecules in autoimmune disease. J. Exp. Med., 178, 1675-1680 (1993).
- 15) Moudgil, K. D., Grewal, I. S., Jensen, P. E., and Sercarz, E. E., Unresponsiveness to a self-peptide of mouse lysozyme owing to hindrance of T cell receptor-major histocompatibility complex/peptide interaction caused by flanking epitopic residues. J. Exp. Med., 183, 535-546 (1996).
- 16) Manca, F., Dessi, V., Shastri, N., Oki, A., Kaplan, M., Clarke, J., Miller, A., and Sercarz, E. E., Isolation of lysozyme-specific T cell clones that discriminate between native and denatured antigen. Cell. Immunol., 154, 420-429 (1994).
- 17) So, T., Ito, H.-O., Koga, T., Watanabe, S., Ueda, T., and Imoto, T., Depression of T-cell epitope generation by stabilizing hen lysozyme. J. Biol. Chem., 272, 32136-32140 (1997).
- 18) Achaffenburg, R., and Drewry, J., Genetics of the β-lactoglobulins of cow's milk. Nature, 180, 376-378 (1957).
- 19) Komatsu, M., Abe, T., and Oishi, T., Relationships between β-lactoglobulin types and the concetrations of β-lactoglobulin and α-lactalbumin in milk. Jap. J. Zootech. Sci., 48, 237-242 (1977).
- 20) Eigel, W. N., Butler, J. E., Ernstrom, C. A., Farrell Jr., H. M., Harwalkar, V. R., Jenness, R., and Whitney, R. McL., Nomenclature of proteins of cow's milk: Fifth Revision. J. Dairy Sci., 67, 1599-1631 (1984).
- 21) Taylor, S. L., Immunologic and allergic properties of cows' milk proteins in humans. J. Food Prot., 49, 239-250 (1986).
- 22) Virtanen, T., Zeiler, T., Rautiainen, J., and Mantyjarvi, R., Allergy to lipocalins: a consequence of misguided T-cell recognition of self and nonself? Immunol. Today, 20, 398-400 (1999).
- 23) Ferreira, F., Hirtenlehner, K., Jilek, A., Godnik-Cvar, J., Breiteneder, H., Grimm, R., Hoffmann-Sommergruber, K., Scheiner, O., Kraft, D., Breitenbach, M., Rheinberger, H.-J., and Ebner, C., Dissection of immunoglobulin E and T lymphocyte reactivity of isoforms of the major birch pollen allergen Bet v 1: potential use of hypoallergenic isoforms for immunotherapy. J. Exp. Med., 183, 599-609 (1996).
- 24) McKenzie, H. A., Ralston, G. B., and Shaw, D. C., Location of sulfhydryl and disulfide groups in bovine β-lactoglobulins and effects of urea. Biochemistry, 11, 4539-4547 (1972).
- 25) Kaminogawa, S., Hattori, M., Ando, O., Kurisaki, J., and Yamauchi, K., Preparation of monoclonal antibody against bovine β-lactoglobulin and its unique binding affinity. Agric. Biol. Chem., 51, 797-802 (1987).
- 26) Hattori, M., Ametani, A., Katakura, Y., Shimizu, M., and Kaminogawa, S., Unfolding/refolding studies on bovine β-lactoglobulin with monoclonal antibodies as probes: Does a renatured protein completely refold? J. Biol. Chem., 268, 22414-22419 (1993) (publish corrections appeared in J. Biol. Chem., 269, 10964 (1994)).
- 27) Qin, B. Y., Bewley, M. C., Creamer, L. K., Baker, H. M., Baker, E. N., and Jameson, G. B., Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochemistry, 37, 14014-14023 (1998).
- 28) Qin, B. Y., Bewley, M. C., Creamer, L. K., Baker, E. N., and Jameson, G. B., Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Protein Sci., 8, 75-83 (1999).
- 29) Sakurai, T., Ametani, A., Nakamura, Y., Shimizu, M., Idota, T., and Kaminogawa, S., Cryptic B cell determinant in a short peptide: T cells do not induce antibody response of B cells when their determinants entirely overlap each other. Int. Immunol., 5, 793-800 (1993).
- 30) Lanzavecchia, A., Antigen-specific interaction between T and B cells. Nature, 314, 537-539 (1985).
- 31) Manca, F., Fenoglio, D., Li Pira, G., Kunkl, A., and Celada, F., Effect of antigen/antibody ratio on macrophage uptake, processing and presentation to T cells of antigen complexed with polyclonal antibodies. J. Exp. Med., 173, 37-48 (1991).
- 32) Simitsek, P. D., Campbell, D. G., Lanzavecchia, A., Fairweather, N., and Watts, C., Modulation of antigen processing by bound antibodies can boost or suppress class II major histocompatibility complex presentation of different T cell determinants. J. Exp. Med., 181, 1957-1963 (1993).
- 33) Kaminogawa, S., Shimizu, M., Ametani, A., Hattori, M., Ando, O., Hachimura, S., Nakamura, Y., Totsuka, M., and Yamauchi, K., Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin. Biochim. Biophys. Acta, 998, 50-56 (1989).
- 34) Papiz, M. Z., Sawyer, L., Eliopoulos, E. E., North, A. C., Findlay, J. B., Sivaprasadarao, R., Jones, T. A., Newcomer, M. E., and Kraulis, P. J., The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature, 324, 383-385 (1986).
- 35) Monaco, H. L., Zanotti, G., Spadon, P., Bolognesi, M., Sawyer, L., and Eliopoulos, E. E., Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol., 197, 695-706 (1987).
- 36) Brownlow, S., Morais Cabral, J. H., Cooper, R., Flower, D. R., Yewdall, S. J., Polikarpov, I., North, A. C. T., and Sawyer, L., Bovine β-lactoglobulin at 1.8 Å resolution—still an enigmatic lipocalin. Structure, 5, 481-495 (1997).
- 37) Gough, P., and Jenness, R., Heat denaturation of β-lactoglobulin A and B. J. Dairy Sci., 45, 1033-1039 (1962).
- 38) Treece, J. M., Sheinson, R. S., and McMeekin, T. L., The solubilities of β-lactoglobulins A, B and AB. Arch. Biochem. Biophys., 108, 99-108 (1964).
- 39) Alexander, S. S., and Pace, C. N., A comparison of the denaturation of bovine β-lactoglobulins A and B and goat β-lactoglobulin. Biochemistry, 10, 2738-2742 (1971).
- 40) Sawyer, W. H., Norton, R. S., Nichol, L. W., and McKenzie, G. H., Thermodenaturation of bovine β-lactoglobulin: kinetics and the introduction of β-structure. Biochim. Biophys. Acta, 243, 19-30 (1971).
- 41) Hillier, R. M., and Lyster, R. L. J., Whey protein denaturation in heated milk and cheese whey. J. Dairy Res., 46, 95-102 (1979).
- 42) Imafadon, G. I., Ng-Kwai-Hang, K. F., Harwalkar, V. R., and Ma, C.-Y., Differential scanning calorimetric study of different genetic variants of β-lactoglobulin. J. Dairy Res., 58, 2416-2422 (1991).
- 43) Huang, X. L., Catignani, G. L., and Swaisgood, H. E., Relative stabilities of β-lactoglobulins A and B as determined by proteolytic susceptibility and differential scanning calorimetry. J. Agric. Food Chem., 42, 1276-1280 (1994).
- 44) McSwiney, M., Singh, H., Campanella, O., and Creamer, L. K., Thermal gelation and denaturation of bovine β-lactoglobulins A and B. J. Dairy Res., 61, 221-232 (1994).
- 45) Sette, A., Adorini, L., Colon, S. M., Buus, S., and Grey, H. M., Capacity of intact proteins to bind to MHC class II molecules. J. Immunol., 143, 1265-1267 (1989).
- 46) Jensen, P. E., Reduction of disulfide bonds during antigen processing: Evidence from a thiol-dependent insulin determinant. J. Exp. Med., 174, 1121-1130 (1991).
- 47) Landry, S. J., Local protein instability predictive of helper T-cell epitopes. Immunol. Today, 18, 527-532 (1997).
Full access
Amino Acid Residue Substitution at T-Cell Determinant-flanking Sites in β-Lactoglobulin Modulates Antigen Presentation to T Cells through Subtle Conformational Change
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.