메뉴 건너뛰기




Volumn 64, Issue , 2013, Pages 70-80

Hyaluronidase from the venom of the social wasp Polybia paulista (Hymenoptera, Vespidae): Cloning, structural modeling, purification, and immunological analysis

Author keywords

CDNA cloning; Hyaluronidase; Polybia paulista venom; Pp Hyal specific antibody; Protein purification; Structural modeling

Indexed keywords

COMPLEMENTARY DNA; GLYCOSIDASE; HYALURONIDASE; POLYCLONAL ANTIBODY; WASP VENOM;

EID: 84873175551     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2012.12.019     Document Type: Article
Times cited : (34)

References (43)
  • 1
    • 84859131417 scopus 로고    scopus 로고
    • The glycosylation pattern of common allergens: the recognition and uptake of Der p 1 by epithelial and dendritic cells is carbohydrate dependent
    • Al-Ghouleh A., Johal R., Sharquie I.K., Emara M., Harrington H., Shakib F., Ghaemmaghami A.M. The glycosylation pattern of common allergens: the recognition and uptake of Der p 1 by epithelial and dendritic cells is carbohydrate dependent. PLoS ONE 2012, 7(3):e33929.
    • (2012) PLoS ONE , vol.7 , Issue.3
    • Al-Ghouleh, A.1    Johal, R.2    Sharquie, I.K.3    Emara, M.4    Harrington, H.5    Shakib, F.6    Ghaemmaghami, A.M.7
  • 2
    • 13944265640 scopus 로고    scopus 로고
    • Enzymatic characterization, antigenic cross-reactivity and neutralization of dermonecrotic activity of five loxosceles spider venoms of medical importance in the Americas
    • Barbaro K.C., Knysak I., Martins R., Hogan C., Winkel K. Enzymatic characterization, antigenic cross-reactivity and neutralization of dermonecrotic activity of five loxosceles spider venoms of medical importance in the Americas. Toxicon 2005, 45:489-499.
    • (2005) Toxicon , vol.45 , pp. 489-499
    • Barbaro, K.C.1    Knysak, I.2    Martins, R.3    Hogan, C.4    Winkel, K.5
  • 3
    • 0026663986 scopus 로고
    • Molecular mass determination and assay of venom hyaluronidases by sodium dodecyl sulfate-polyacrilamide gel electrophoresis
    • Cevallos M.A., Navarro-Duque C., Varela-Julia M., Alagon A.C. Molecular mass determination and assay of venom hyaluronidases by sodium dodecyl sulfate-polyacrilamide gel electrophoresis. Toxicon 1992, 30:925-930.
    • (1992) Toxicon , vol.30 , pp. 925-930
    • Cevallos, M.A.1    Navarro-Duque, C.2    Varela-Julia, M.3    Alagon, A.C.4
  • 4
    • 0029942745 scopus 로고    scopus 로고
    • The PH-20 protein in Cynomolgus macaque spermatozoa: identification of two different forms exhibiting hyaluronidase activity
    • Cherr G.N., Meyers S.A., Yudin A.I., Van de Voort C.A., Myles D.G., Primakoff P., Overstreet J.W. The PH-20 protein in Cynomolgus macaque spermatozoa: identification of two different forms exhibiting hyaluronidase activity. Dev. Biol. 1996, 175:142-153.
    • (1996) Dev. Biol. , vol.175 , pp. 142-153
    • Cherr, G.N.1    Meyers, S.A.2    Yudin, A.I.3    Van de Voort, C.A.4    Myles, D.G.5    Primakoff, P.6    Overstreet, J.W.7
  • 6
    • 0039853037 scopus 로고    scopus 로고
    • Expression analysis of six paralogous human hyaluronidase genes clustered on chromosomes 3p21 and 7q31
    • Csóka A.B., Scherer S.W., Stern R. Expression analysis of six paralogous human hyaluronidase genes clustered on chromosomes 3p21 and 7q31. Genomics 1999, 60:356-361.
    • (1999) Genomics , vol.60 , pp. 356-361
    • Csóka, A.B.1    Scherer, S.W.2    Stern, R.3
  • 8
    • 84862854948 scopus 로고    scopus 로고
    • Double positivity to bee and wasp venom: improved diagnostic procedure by recombinant allergen-based IgE testing and basophil activation test including data about cross-reactive carbohydrate determinants
    • Eberlein B., Krischan L., Darsow U., Ollert M., Ring J. Double positivity to bee and wasp venom: improved diagnostic procedure by recombinant allergen-based IgE testing and basophil activation test including data about cross-reactive carbohydrate determinants. J. Allergy Clin. Immunol. 2012, 130:155-161.
    • (2012) J. Allergy Clin. Immunol. , vol.130 , pp. 155-161
    • Eberlein, B.1    Krischan, L.2    Darsow, U.3    Ollert, M.4    Ring, J.5
  • 9
    • 0021669997 scopus 로고
    • Hyaluronidase polymorphism detected by polyacrylamide gel electrophoresis. Application to hyaluronidases from bacteria, slime molds, bee and snake venoms, bovine testes, rat liver lysosomes, and human serum
    • Fiszer-Szafarz B. Hyaluronidase polymorphism detected by polyacrylamide gel electrophoresis. Application to hyaluronidases from bacteria, slime molds, bee and snake venoms, bovine testes, rat liver lysosomes, and human serum. Anal. Biochem. 1984, 143:76-81.
    • (1984) Anal. Biochem. , vol.143 , pp. 76-81
    • Fiszer-Szafarz, B.1
  • 10
    • 0025307749 scopus 로고
    • Polymorphism of hyaluronidase in serum from man, various mouse strains and other vertebrate species revealed by electrophoresis
    • Fiszer-Szafarz B., Szafarz D., Vannier P. Polymorphism of hyaluronidase in serum from man, various mouse strains and other vertebrate species revealed by electrophoresis. Biol. Cell. 1990, 68:95-100.
    • (1990) Biol. Cell. , vol.68 , pp. 95-100
    • Fiszer-Szafarz, B.1    Szafarz, D.2    Vannier, P.3
  • 11
    • 0027520896 scopus 로고
    • Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm
    • Gmachl M., Kreil G. Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:3569-3573.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 3569-3573
    • Gmachl, M.1    Kreil, G.2
  • 12
    • 40549122963 scopus 로고    scopus 로고
    • Cross-reactivity to honeybee and wasp venom
    • Hemmer W. Cross-reactivity to honeybee and wasp venom. Hautarzt 2008, 59:194-199.
    • (2008) Hautarzt , vol.59 , pp. 194-199
    • Hemmer, W.1
  • 13
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hidrolases
    • Henrissat B., Bairoch A. Updating the sequence-based classification of glycosyl hidrolases. Biochem. J. 1996, 316:695-696.
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 14
    • 0028023389 scopus 로고
    • Hyaluronidases of the gastrointestinal invasive nematodes Ancylostoma conium and Anisakissimplex: possible functions in the pathogenesis of human zoonoses
    • Hotez P., Cappello M., Hawdon J., Beckers C., Sakanari J. Hyaluronidases of the gastrointestinal invasive nematodes Ancylostoma conium and Anisakissimplex: possible functions in the pathogenesis of human zoonoses. J. Infect. Dis. 1994, 170:918-926.
    • (1994) J. Infect. Dis. , vol.170 , pp. 918-926
    • Hotez, P.1    Cappello, M.2    Hawdon, J.3    Beckers, C.4    Sakanari, J.5
  • 15
    • 38149058818 scopus 로고    scopus 로고
    • Affinity of IgE and IgG against cross-reactive carbohydrate determinants on plant and insect glycoproteins
    • Jin C., Hantusch B., Hemmer W., Stadlmann J., Altmann F. Affinity of IgE and IgG against cross-reactive carbohydrate determinants on plant and insect glycoproteins. J. Allergy Clin. Immunol. 2008, 121:185-190.
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 185-190
    • Jin, C.1    Hantusch, B.2    Hemmer, W.3    Stadlmann, J.4    Altmann, F.5
  • 17
    • 0021343667 scopus 로고
    • The purification and characterization of hyaluronidase from the venom of the honey bee, Apis mellijera
    • Kemeny D.M., Dalton N., Lawrence A.J., Pearce F.L., Vernon C.A. The purification and characterization of hyaluronidase from the venom of the honey bee, Apis mellijera. Eur. J. Biochem. 1984, 139:217-233.
    • (1984) Eur. J. Biochem. , vol.139 , pp. 217-233
    • Kemeny, D.M.1    Dalton, N.2    Lawrence, A.J.3    Pearce, F.L.4    Vernon, C.A.5
  • 18
    • 31644442036 scopus 로고    scopus 로고
    • Snake venom hyaluronidase: a therapeutic target
    • Kemparaju K., Girish K.S. Snake venom hyaluronidase: a therapeutic target. Cell Biochem. Funct. 2006, 24:7-12.
    • (2006) Cell Biochem. Funct. , vol.24 , pp. 7-12
    • Kemparaju, K.1    Girish, K.S.2
  • 19
    • 0034307511 scopus 로고    scopus 로고
    • N-glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1
    • Kolarich D., Altmann F. N-glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. Anal. Biochem. 2000, 285:64-75.
    • (2000) Anal. Biochem. , vol.285 , pp. 64-75
    • Kolarich, D.1    Altmann, F.2
  • 20
    • 27144480341 scopus 로고    scopus 로고
    • The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris
    • Kolarich D., Léonard R., Hemmer W., Altman F. The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris. FEBS J. 2005, 272:5182-5190.
    • (2005) FEBS J. , vol.272 , pp. 5182-5190
    • Kolarich, D.1    Léonard, R.2    Hemmer, W.3    Altman, F.4
  • 21
    • 0029079957 scopus 로고
    • Hyaluronidases - a group of neglected enzymes
    • Kreil G. Hyaluronidases - a group of neglected enzymes. Protein Sci. 1995, 4:1666-1669.
    • (1995) Protein Sci. , vol.4 , pp. 1666-1669
    • Kreil, G.1
  • 22
    • 0028915061 scopus 로고
    • The asparagine-linked carbohydrate of honeybee venom hyaluronidase
    • Kubelka V., Altmann F., März L. The asparagine-linked carbohydrate of honeybee venom hyaluronidase. Glycoconj. J. 1995, 12:77-83.
    • (1995) Glycoconj. J. , vol.12 , pp. 77-83
    • Kubelka, V.1    Altmann, F.2    März, L.3
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 1993, 26:238-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 238-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 0024367373 scopus 로고
    • The Biology of Hyaluronan
    • John Wiley & Sons, New York,
    • Laurent T.C. The Biology of Hyaluronan. Ciba Foundation Symp. 143 1989, John Wiley & Sons, New York, pp. 1-298.
    • (1989) Ciba Foundation Symp. 143 , pp. 1-298
    • Laurent, T.C.1
  • 26
    • 0027972221 scopus 로고
    • Characteristics of hyaluronidase and hemolytic activity in fishing tentacle nematocyst venom of Chrysaora quinquecirrha
    • Long-Rowe K.O., Burnett J.W. Characteristics of hyaluronidase and hemolytic activity in fishing tentacle nematocyst venom of Chrysaora quinquecirrha. Toxicon 1994, 32:165-174.
    • (1994) Toxicon , vol.32 , pp. 165-174
    • Long-Rowe, K.O.1    Burnett, J.W.2
  • 27
    • 0028956730 scopus 로고
    • Sequence identity and antigenic crossreactivity of hite face hornet venom allergen, also a hyaluronidase, with other proteins
    • Lu G., Kochoumian L., King T.P. Sequence identity and antigenic crossreactivity of hite face hornet venom allergen, also a hyaluronidase, with other proteins. J. Biol. Chem. 1995, 270:4457-4465.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4457-4465
    • Lu, G.1    Kochoumian, L.2    King, T.P.3
  • 29
    • 0036773411 scopus 로고    scopus 로고
    • Quantification of protein surfaces, volumes and atom-atom contacts using a constrained Voronoi procedure
    • McConkey B.J., Sobolev V., Edelman M. Quantification of protein surfaces, volumes and atom-atom contacts using a constrained Voronoi procedure. Bioinformatics 2002, 18:1365-1373.
    • (2002) Bioinformatics , vol.18 , pp. 1365-1373
    • McConkey, B.J.1    Sobolev, V.2    Edelman, M.3
  • 30
    • 77956924584 scopus 로고
    • Hyaluronidases
    • Academic Press, New York
    • Meyer K. Hyaluronidases. The Enzymes 1971, vol. V:307-320. Academic Press, New York. third ed.
    • (1971) The Enzymes , vol.5 , pp. 307-320
    • Meyer, K.1
  • 31
    • 84882860308 scopus 로고    scopus 로고
    • Insect venom peptides
    • Academic Press, Burlington, A.J. Kastin (Ed.)
    • Palma M.S. Insect venom peptides. Handbook of Biologically Active Peptides 2006, 389-396. Academic Press, Burlington. A.J. Kastin (Ed.).
    • (2006) Handbook of Biologically Active Peptides , pp. 389-396
    • Palma, M.S.1
  • 32
    • 84861956280 scopus 로고    scopus 로고
    • Proteomic characterization of the hyaluronidase (E.C. 3.2.1.35) from the venom of the social wasp Polybia paulista
    • Pinto J.R., Santos L.D., Arcuri H.A., Dias N.B., Palma M.S. Proteomic characterization of the hyaluronidase (E.C. 3.2.1.35) from the venom of the social wasp Polybia paulista. Protein Pep. Lett. 2012, 19:624-634.
    • (2012) Protein Pep. Lett. , vol.19 , pp. 624-634
    • Pinto, J.R.1    Santos, L.D.2    Arcuri, H.A.3    Dias, N.B.4    Palma, M.S.5
  • 34
    • 0030908273 scopus 로고    scopus 로고
    • Advances in comparative protein-structure modeling
    • Sanchez R., Sali A. Advances in comparative protein-structure modeling. Curr. Opin. Struct. Biol. 1997, 7:206-214.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 206-214
    • Sanchez, R.1    Sali, A.2
  • 36
    • 0017390556 scopus 로고
    • A rapid, sensitive and versatile assay for protein using Coomassie brilliant blue G250
    • Sedmak J.J., Grossberg S.E. A rapid, sensitive and versatile assay for protein using Coomassie brilliant blue G250. Anal. Biochem. 1977, 79:544-552.
    • (1977) Anal. Biochem. , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 37
    • 1642528831 scopus 로고    scopus 로고
    • Post-translational modifications and their biological functions: proteomic analysis and systematic approaches
    • Seo J., Lee K.J. Post-translational modifications and their biological functions: proteomic analysis and systematic approaches. J. Biochem. Mol. Biol. 2004, 37:35-44.
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 35-44
    • Seo, J.1    Lee, K.J.2
  • 38
    • 4644360277 scopus 로고    scopus 로고
    • A comparative study of protein and enzymatic activity in venoms of some common wasps (hymenoptera: vespidae) from São Paulo State
    • Silva G.P., Brochetto-Braga M.R., Ruberti M., Ternero M.L., Gobbi N. A comparative study of protein and enzymatic activity in venoms of some common wasps (hymenoptera: vespidae) from São Paulo State. Sociobiology 2004, 44:271-282.
    • (2004) Sociobiology , vol.44 , pp. 271-282
    • Silva, G.P.1    Brochetto-Braga, M.R.2    Ruberti, M.3    Ternero, M.L.4    Gobbi, N.5
  • 41
    • 33645372800 scopus 로고    scopus 로고
    • Hyaluronidases: their genomics, structures, and mechanisms of action
    • Stern R., Jedrzejas M.J. Hyaluronidases: their genomics, structures, and mechanisms of action. Chem. Rev. 2006, 106:818-839.
    • (2006) Chem. Rev. , vol.106 , pp. 818-839
    • Stern, R.1    Jedrzejas, M.J.2
  • 42
    • 0028244342 scopus 로고
    • Characterization of hydrolysis and transglycosylation by testicular hyaluronidase using ion-spray mass spectroscopy
    • Takagaki K., Nakamura T., Izumi J., Saitoh H., Endo M., Kojima K., Kato I., Majima M. Characterization of hydrolysis and transglycosylation by testicular hyaluronidase using ion-spray mass spectroscopy. Biochemistry 1994, 33:6503-6507.
    • (1994) Biochemistry , vol.33 , pp. 6503-6507
    • Takagaki, K.1    Nakamura, T.2    Izumi, J.3    Saitoh, H.4    Endo, M.5    Kojima, K.6    Kato, I.7    Majima, M.8
  • 43
    • 0015805632 scopus 로고
    • Hyaluronidase and esterase activities of the venom of the poisonous brown recluse spider
    • Wright R.P., Elgert K.D., Campbell B.J., Barret J.T. Hyaluronidase and esterase activities of the venom of the poisonous brown recluse spider. Arch. Biochem. Biophys. 1973, 159:415-426.
    • (1973) Arch. Biochem. Biophys. , vol.159 , pp. 415-426
    • Wright, R.P.1    Elgert, K.D.2    Campbell, B.J.3    Barret, J.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.