Insights into a conformational epitope of Hev b 6.02 (hevein)

Biochemical and Biophysical Research Communications

Volumn 314, Issue 1, 2004, Pages 123-130

  Reyes López, César A ^a   Hernández Santoyo, Alejandra ^a   Pedraza Escalona, Martha ^a   Mendoza, Guillermo ^b   Hernández Arana, Andrés ^c   Rodríguez Romero, Adela ^a  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^c DEPARTAMENTO DE QUÍMICA   (Mexico)

Author keywords

Allergens; Hev b 6.02; Hevein; IgE epitope; Latex; X ray structure

Indexed keywords

2 NITROPHENYLSULFENYL 3 METHYL 3' BROMOINDOLENINE; ALLERGEN; EPITOPE; HEVEIN; HEVEIN ANTIBODY; IMMUNOGLOBULIN E; INDOLE DERIVATIVE; LATEX; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY; RUBBER; SKATOLE; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANTIGEN RECOGNITION; ARTICLE; BINDING AFFINITY; CROSS REACTION; DOT HYBRIDIZATION; ENZYME LINKED IMMUNOSORBENT ASSAY; PRICK TEST; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

EID: 0346095164     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.12.068     Document Type: Article

References (39)

1. Sutton B.J., Gould H.J. The human IgE network. Nature. 366:1993;421-428.
2. Bufe A. The biological function of allergens: relevant for the induction of allergic diseases? Int. Arch. Allergy Immunol. 117:1998;215-219.
3. Huby D.J.R., Dearman J.R., Kimber I. Why are some proteins allergens? Toxicol. Sci. 55:2000;235-246.
4. Brehler R., Theissen U., Mohr C., Luger T. Latex-fruit syndrome: frequency of cross-reacting IgE antibodies. Allergy. 52:1997;404-410.
5. Fuchs T., Spitzauer S., Vente C., Hevler J., Kapiotis S., Rumpold H., Kraft D., Valenta R. Natural latex, grass pollen, and weed pollen share IgE epitopes. J. Allergy Clin. Immunol. 100:1997;356-364.
6. Berzofsky J.A. Intrinsic and extrinsic factors in protein antigenic structure. Science. 229:1985;932-940.
7. Aalberse R.C. Structural biology of allergens. J. Allergy Clin. Immunol. 106:2000;228-238.
8. van Parijs J., Broekaert W.F., Goldstein I.J., Peumans W.J. Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta. 183:1991;258-264.
9. Alenius H., Kalkkinen N., Reunala T., Turjanmaa K., Palosuo T. The main IgE-binding epitope of a major latex allergen, prohevein, is present in its N-terminal 43-amino acid fragment, hevein. J. Immunol. 156:1996;1618-1625.
10. Soedjanaatmadja U.M., Hofsteenge J., Jeronimus-Stratingh C.M., Bruins A.P., Beintema J.J. Demonstration by mass spectrometry that pseudo-hevein and hevein have ragged C-terminal sequences. Biochim. Biophys. Acta. 1209:1994;144-148.
11. Wright H.T., Sandrasegaram G., Wright C.S. Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin. J. Mol. Evol. 33:1991;283-294.
12. Harata K., Muraki M. Crystal structures of Urtica dioica agglutinin and its complex with tri-N-acetylchitotriose. J. Mol. Biol. 297:2000;673-681.
13. Rodriguez-Romero A., Ravichandran K.G., Soriano-Garcia M. Crystal structure of hevein at 2.8. Å resolution FEBS Lett. 291:1991;307-309.
14. Andersen N.H., Cao B., Rodriguez-Romero A., Arreguin B. Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin motif. Biochemistry. 32:1993;1407-1422.
15. Asensio J.L., Cañada F.J., Bruix M., Rodriguez-Romero A., Jimenez-Barbero J. The interaction of hevein with N-acetylglucosamine- containing oligosaccharides. Solution structure of hevein complexed to chitobiose. Eur. J. Biochem. 230:1995;621-633.
16. Omenn G.S., Fontana A., Anfinsen C.B. Modification of the single tryptophan residue of staphylococcal nuclease by a new mild oxidizing agent. J. Biol. Chem. 254:1970;1895-1902.
17. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
18. The CCP4 suite: programs for protein crystallography, Collaborative Computational Project, Number 4, Acta Crystallogr. D 50 (1994) 760-763.
19. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., Warren G.L. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D. 54:1998;905-921.
20. Brünger A.T. Free. R -value: a novel statistical quantity for assessing the accuracy of crystal structures Nature. 355:1992;472-474.
21. Kleywegt G.J., Jones T.A. Databases in protein crystallography. Acta Crystallogr. D. 54:1998;1119-1131.
22. T.J. Oldfield, Macromolecular refinement, in: Proceedings of the CCP4 Study Weekend, SRS Daresbury Laboratory, Warringtong, UK.
23. Sheldrick G.M., Schneider T.A. SHELXL: high-resolution refinement. Methods Enzymol. 277:1997;319-343.
24. Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A. 47:1991;392-400.
25. Patterson W.R., Anderson D.H., DeGrado W.F., Cascio D., Eisenberg D. Centrosymmetric bilayers in the 0.75. Å resolution structure of a designed alpha-helical peptide, D,L-alpha-1 Protein Sci. 8:1999;1410-1422.
26. Laskowski R.A., MacArthur M.W., Hutchinson S.C., Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:1993;283-291.
27. Cohen G.H. ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions. J. Appl. Crystallogr. 30:1997;1160-1161.
28. Beezhold D.H., Kostyal D.A., Sussman G.L. IgE epitope analysis of the hevein preprotein; a major latex allergen. Clin. Exp. Immunol. 108:1997;114-121.
29. Vestlin M.M., Kelly A.M., Fenselau C. Optimization by mass spectrometry of a tryptophan-specific protein cleavage reaction. Rapid Commun. Mass Spectrom. 8:1994;786-790.
30. Argali V., Gueguen J. Chemical cleavage of bovine β-lactoglobulin by BNPS-skatole for preparative purposes: comparative study of hydrolytic procedures and peptide characterization. J. Protein Chem. 18:1999;1-12.
31. Rodriguez-Romero A., Arreguin B., Hernandez-Arana A. Unusual far-ultraviolet circular dichroism of wheat germ agglutinin and hevein originated from cystine residues. Biochim. Biophys. Acta. 998:1989;21-24.
32. Thomas M.W., Walborg E.F., Jirgensons B. Circular dichroism and saccharide-induced conformational transitions of wheat germ agglutinin. Arch. Biochem. Biophys. 178:1977;625-630.
33. Casey J.P., Martin R.B. Disulfide stereochemistry. Conformations and chiroptical properties of L-cystine derivatives. J. Am. Chem. Soc. 94:1972;6141-6151.
34. Breinteneder H., Ebner C. Molecular and biochemical classification of plant-derived food allergens. J. Allergy Clin. Immunol. 106:2000;27-36.
35. Miller S., Janin J., Lesk A.M., Chothia C. Interior and surface of monomeric proteins. J. Mol. Biol. 196:1987;641-656.
36. Fedorov A.A., Ball T., Mahoney M.N., Valenta R., Almo C.S. Crystal structure and IgE-epitope mapping of birch pollen profilin: molecular basis for allergen cross-reactivity. Structure. 5:1997;33-45.
37. Karisola P., Alenius H., Mikkola J., Kalkkinen N., Helin J., Pentikäinen T.O., Repo S., Reunala T., Turjanmaa K., Johnson S.M., Palosuo T., Kulomaa S.M. The major conformational IgE-binding epitopes of hevein (Hev b 6.02) are identified by a novel chimera-based allergen epitope mapping strategy. J. Biol. Chem. 277:2002;22656-22661.
38. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
39. Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.