3-D Model of the bee venom acid phosphatase: Insights into allergenicity

Biochemical and Biophysical Research Communications

Volumn 378, Issue 4, 2009, Pages 711-715

  Georgieva, Dessislava ^a   Greunke, Kerstin ^b   Genov, Nicolay ^c   Betzel, Christian ^a  

^a DESY   (Germany)

^b Protein Ligand Structural PLS Design GmbH   (Germany)

^c INSTITUTE OF ORGANIC CHEMISTRY   (Bulgaria)

Author keywords

Acid phosphatase; Allergen; Honeybee venom; Protein modeling

Indexed keywords

ACID PHOSPHATASE PROSTATE ISOENZYME; BEE VENOM; EPITOPE; HISTIDINE; IMMUNOGLOBULIN E;

ALLERGENICITY; ARTICLE; BINDING SITE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; HUMAN; MALE; MOLECULAR MECHANICS; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; RAT; THREE DIMENSIONAL IMAGING;

ACID PHOSPHATASE; ALLERGENS; AMINO ACID SEQUENCE; ANIMALS; BEE VENOMS; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; HUMANS; IMMUNODOMINANT EPITOPES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHATES; PROTEIN STRUCTURE, TERTIARY; RATS;

APIS MELLIFERA; APOIDEA;

EID: 57849128822     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.11.101     Document Type: Article

References (34)

1. Forestier F., and Palmer M. Bee venom in rheumatology-an experiment performed with 1600 cases. Apiacta 19 (1984) 19-22
2. Kim C.M. Bee venom therapy for arthritis. Z. Rheumatol. 41 (1989) 67-72
3. Klinghardt D.K. Bee venom therapy for chronic pain. J. Neurol. Orthopedic MedSurg. 11 (1990) 195-197
4. Thaller M.C., Schippa S., and Rossolini G.M. Conserved sequence motifs among bacterial, eukaryotic, and archaeal phosphatises that define a new phosphohydrolase superfamily. Protein Sci. 7 (1998) 1647-1652
5. Schneider G., Lindqvist Y., and Vihko P. Three-dimensional structure of rat acid phosphatase. EMBO J. 12 (1993) 2609-2615
6. Jakob C.G., Lewinski K., Kuciel R., Ostrowski W., and Lebioda L. Crystal structure of human prostatic acid phosphatise. The Prostate 42 (2000) 211-218
7. Hayman A.R. Tartrate-resistant acid phosphatase (TRAP) and the osteoclast/immune cell dichotomy. Autoimmunity 41 (2008) 218-223
8. Calderone V., Forleo C., Benvenuti M., Thaller M.C., Rossolini G.M., and Mangani S. A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases. J. Mol. Biol. 355 (2006) 708-721
9. V. S. Reddy, A. K. Singh, R. Rajasekharan, The Saccharomyces cerevisiae PHM8 gene encodes a soluble magnesium dependent lysophosphatidic acid phosphatase, J. Biol. Chem. PMID (2008) 18234677.
10. Schenk G., Elliot T.W., Leung E., Carrington L.E., Mitic N., Gahan L.R., and Guddat L.W. Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycle. BMC Struct. Biol. 8 (2008) 6
11. Hoffman D.R. Hymenoptera venom allergens. Clin. Rev. Allergy Immunol. 30 (2006) 109-128
12. Hoffman D.R., Weimer E.T., Sakell R.H., and Schmidt M. Sequence and characterization of honeybee venom acid phosphatase. J. Allergy Clin. Immunol. 115 (2005) S107
13. Barboni E., Kemeny D.M., Campos S., and Vernon C.A. The purification of acid phosphatase from honey bee venom (Apis mellifica). Toxicon 10 (1987) 1097-1103
14. März L., Kühne C., and Michl H. The glycoprotein nature of phospholipase A2, hyaluronidase and acid phosphatase from honey-bee venom. Toxicon 21 (1983) 893-896
15. Grunwald T., Bockisch B., Spillner E., Ring J., Bredehorst R., and Ollert M.W. Molecular cloning and expression in insect cells of honeybee venom allergen acid phosphatase (Api m 3). J. Allergy Clin. Immunol. 117 (2006) 848-854
16. Venclovas C., and Margelevicius M. Comparative modeling in CASP6 using consensus approach to template selection, sequence-structure alignment, and structure assessment. Proteins 61 S7 (2005) 99-105
17. Altschul S.F., Gish W., Miller W W., Myers E.W., and Lipman D.J. Basic alignment search tool. J. Mol. Biol. 215 (1990) 403-410
18. Petisch M.C. Computer modelling of biological molecules. Biochem. Soc. Trans. 24 (1996) 274-279
19. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291
20. Lee B., and Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55 (1971) 379-400
21. Collaborative Computational Project, Number 4. The CCP4 Suite: program for protein crystallography. Acta Crystall. D50 (1994) 760-763
22. Kabsh W. A solution for the best rotation to relate two sets of vectors. Acta Crystall. A32 (1976) 922-923
23. Saha S., and Raghava G.P.S. AlgPred: prediction of allergenic proteins and mapping of IgE epitopes. Nucleic Acids Res. 34 (2006) W202-W209
24. Kolaskar A.S., and Tongaonkar P.C. A semi-empirical method for prediction of antigenic determinants on protein antigens. FEBS Lett. 276 (1990) 172-174
25. Marti-Renom M.A., Stuart A.C., Fiser A., Sanchez R., Melo F., and Sali A. Comparative protein structure modelling of genes and genomes. Annu. Rev. Biophys. Biomol. Struct. 29 (2000) 291-325
26. Ostanin K., Harms E.H., Stevis P.E., Kuciel R., Zhou M.-M., and Van Etten R.L. Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase. J. Biol. Chem. 267 (1992) 22830-22836
27. Gehlhar K., Rajashankar K.R., Hofmann E., Betzel Ch., Weber W., Werner S., and Bufe A. Lysine as a critical amino acid for IgE binding in Phl p 5b C terminus. Int. Arch. Allergy Immunol. 140 (2006) 285-294
28. Beezhold D.H., Hickey V.L., and Sussman G.L. Mutational analysis of the IgE epitopes in the latex allergen Hev b 5. J. Allergy Clin. Immunol. 107 (2001) 1069-1076
29. Mullaney E.J., and Ullah A.H.J. Identification of a histidine acid phosphatase (phy A)-like gene in Arabidopsis thaliana. Biochem. Biophys. Res. Commun. 251 (1998) 252-255
30. Van Etten R.L. Human prostatic acid phosphatise: a histidine phosphatase. Ann. N. Y. Acad. Sci. 390 (1982) 27-51
31. Van Etten R.L., Davidson R., Stevis P.E., MacArthur H., and Moore D.L. Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. J. Biol. Chem. 266 (1991) 2313-2319
32. Povari K.S., Herrala A.M., Kurkela R.M., Taavitsainen P.A., Lindqvist Y., Schneider G., and Vihko P.T. Site-directed mutagenesis of prostatic acid phosphatase. Catalytically important aspartic acid 258, substrate specificity and oligomerization. J. Biol. Chem. 269 (1994) 22642-22646
33. Beezhold D.H., Hickey V.L., Slater J.E., and Sussman G.L. Human IgE-binding epitopes of the latex allergen Hev b 5. J. Allergy Clin. Immunol. 103 (1999) 1166-1172
34. Rabjohn P., West C.M., Connaughton C., Sampson H.A., Helm R.M., Burks A.W., and Bannon G.A. Modification of peanut allergen Ara h 3: effects on IgE binding and T cell stimulation. Int. Arch. Allergy Immunol. 128 (2001) 15-23