Characterization of lectin aggregates in the hemolymph of freshwater prawn Macrobrachium rosenbergii

Biochimica et Biophysica Acta - General Subjects

Volumn 1673, Issue 3, 2004, Pages 122-130

  Pereyra, Ali ^a   Zenteno, Roberto ^b   Vázquez, Lorena ^c   Martínez Cairo, Salvador ^d   Rodríguez, Adela ^e   Mendoza Hernández, Guillermo ^f   Zenteno, Edgar ^f   Agundis, Concepción ^f  

^a INSTITUTO NACIONAL DE ENFERMEDADES RESPIRATORIAS   (Mexico)

^b UNIVERSIDAD VERACRUZANA   (Mexico)

^c CENTRO DE INVESTIGACIONES QUÍMICAS   (Mexico)

^d INSTITUTO MEXICANO DEL SEGURO SOCIAL   (Mexico)

^e UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^f UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

Author keywords

Hemolymph; Lectin; Macrobrachium rosenbergii

Indexed keywords

ALANINE; AMIDE; AMINO ACID; ASPARTYLVALYLPROLYLLEUCYLLEUCINE; CARBOHYDRATE; DODECYL SULFATE SODIUM; LECTIN; MONOCLONAL ANTIBODY; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; FEMALE; GEL FILTRATION; HEMAGGLUTINATION; HEMOLYMPH; HUMAN; HUMAN CELL; MACROBRACHIUM ROSENBERGII; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; MOUSE; NONHUMAN; NORMAL HUMAN; NUCLEOTIDE SEQUENCE; PHYSICAL CHEMISTRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN STRUCTURE; RAT; SHRIMP;

AMINO ACID SEQUENCE; ANIMALS; CHROMATOGRAPHY, AFFINITY; CIRCULAR DICHROISM; CRUSTACEA; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HEMOLYMPH; LECTINS; PROTEIN ISOFORMS;

INVERTEBRATA; MACROBRACHIUM; MACROBRACHIUM ROSENBERGII;

EID: 3242806669     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2004.04.004     Document Type: Article

References (49)

1. Renwrantz L. Lectins in molluscs and arthropods: their occurrence, origin and roles in immunity. Symp. Zool. Soc. Lond. 56:1986;81-93
2. Cooper E.L., Rinkevich B., Uhlenbruck G., Valembois P. Invertebrate immunity: another viewpoint. Scand. J. Immunol. 35:1992;247-266
3. Goldstein I.J., Hughes R.C., Monsigny M., Osawa T., Sharon N. What should be called a lectin? Nature. 66:1980;285-286
4. Nesser R., Koellreautter B., Wuersch P. Oligomanoside type glycopeptides inhibiting adhesion of Escherichia coli strains mediated by type 1 pili, preparation of potent inhibitors from plant glycopeptides. Infect. Immun. 58:1986;428-436
5. Sharon N. Surface carbohydrates and surface lectins are recognition determinants in phagocytosis. Immunol. Today. 5:1984;1-5
6. Bayne C.J. Phagocytosis and non-self recognition in invertebrates. Bioscience. 40:1990;723-731
7. Vasta G.R. Invertebrate lectins: distribution, synthesis, molecular biology, and function. Allen H.J., Kisalius E.C. Glycoconjugates, Composition, Structure and Function. 1992;593-634 Marcel Dekker, New York
8. Fragdiakis G.A., Stratakis E.K. The lectin from the crustacean Liocarcinus depurator recognizes Oacetylsialic acids. Comp. Biochem. Physiol., B. 117:1997;545-552
9. Vazquez L., Masso F., Rosas P., Montaño L.F., Zenteno E. Purification and characterization of a lectin from Macrobrachium rosenbergii (Crustacea: Decapoda) hemolymph. Comp. Biochem. Physiol., B. 105:1993;617-623
10. Vazquez L., Lanz H., Montaño L.F., Zenteno E. Biological activity of the lectin from Macrobrachium rosenbergii. Van Driessche E., Bog-Hansen T.C. Lectins, Biology Biochemistry, Clinical Chemistry. vol. 10:1994;261-265 Textop, Hellerup, Denmark
11. Vazquez L., Jaramillo L., Lascurain R., Cooper E.L., Rosas P., Zenteno E. Bacterial agglutination by the sialic acid specific serum lectin from Macrobrachium rosenbergii. Comp. Biochem. Physiol., B. 113:1996;355-359
12. Olafsen J.A. Lectins: models of natural and induced molecules in invertebrates. Adv. Comp. Environ. Physiol. 24:1996;49-76
13. Vazquez L., Maldonado G., Agundis C., Perez A., Cooper E.L., Zenteno E. Participation of a sialic acid specific lectin from the freshwater prawn Macrobrachium rosenbergii hemocytes, in the recognition of non-self cells. J. Exp. Zool. 279:1997;265-272
14. Vazquez L., Perez A., Millan D., Agundis C., Martin G., Cooper E.L., Lascurain R., Zenteno E. Morphological analysis of hemocytes from the freshwater prawn Macrobrachium rosenbergii. J. Morphol. 234:1997;147-153
15. Sierra C., Pérez A., Agundis C., Zenteno E., Vázquez L. Subcellular organization of the seric lectin in haemocytes from the freshwater prawn Macrobrachium rosenbergii (Decapoda, Nanantia). Schram F.R., von Vaupel Klein J.C. Crustaceans and the Biodiversity Crisis. vol. I:1999;961-970 Brill, Leiden
16. Peebles J.B. A rapid technique for molt staging in live Macrobrachium rosenbergii. Aquaculture. 12:1977;173-180
17. Spiro R.G., Bhoyroo V.D. Structure of the O-glycosidically linked carbohydrate unit of fetuin. J. Biol. Chem. 249:1974;5704-5717
18. Bradford M. A rapid and sensitive method for the quantitation of protein utilizing the principles of protein-dye binding. Anal. Biochem. 72:1976;248-254
19. Bidlingmeyer B.A., Cohen S.A., Tarvin T.L. Rapid analysis of amino acid using pre-column derivatization. J. Chromatogr. 33:1984;93-104
20. Zanetta J.P., Timmerman T., Leroy Y. Determination of constituents of sulfated proteoglycans using a methanolysis procedure and gas chromatography/mass spectrometry of heptafluorobutyrate derivatives. Glycobiology. 9:1999;255-266
21. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-683
22. Hellman U., Wernstedt C., Gonez J., Heldin C. Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal. Biochem. 224:1995;451-455
23. Kohler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 256:1975;495-497
24. Gefter M.L., Marulies D.H., Scharff M.D. A simple method for polyethylene glycol-promoted hybridisation of mouse myeloma cells. Somatic Cell Genet. 3:1977;213-236
25. Avrameas S., Ternynck T. Peroxidase labeled antibody and Fab conjugates with enhanced intracellular penetration. Immunochemistry. 8:1971;1175-1179
26. Agundis C., Pereyra A., Zenteno R., Brassart C., Sierra C., Vazquez L., Zenteno E. Quantification of lectin in freshwater prawn (Macrobrachium rosenbergii) hemolymph by ELISA. Comp. Biochem. Physiol., B. 127:2000;165-172
27. Engvall E., Perlman P. Enzyme-linked immunoabsorbent assay (ELISA). Quantitative assay of immunoglobulin G. Immunochemistry. 8:1971;871-873
28. Massó F., Sandoval S., Rosas P., Páez E., Díaz L., Zenteno E., Montaño L.F. Eficacia de un ELISA con extracto proteico completo y delipidizado de Mycobacterium tuberculosis Cepa H37Rv como prueba serológica para descartar tuberculosis pulmonar. Rev. Latinoam. Microbiol. 35:1993;177-184
29. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76:1979;4350-4354
30. Iwanaga S. The molecular basis of innate immunity in the horseshoe crab. Curr. Opin. Immunol. 14:2002;87-95
31. Schauer R., Casals-Stenzel J., Corfield A.P., Veh R.W. Subcellular site of the biosynthesis of O-acetylated sialic acids in bovine submandibular gland. Glycocon. J. 5:1988;257-270
32. Egge H., Peter-Katalinic J., Paz-Parente J., Strecker G., Montreuil J., Fournet B. Carbohydrate structures of hen ovomucoid. A mass spectrometric analysis. FEBS Lett. 156:1983;357-362
33. Schmid K., Binette J.P., Dorland L., Vliegenthart J.F., Fournet B., Montreuil J. The primary structure of the asialo-carbohydrate units of the first glycosylation site of human plasma alpha1-acid glycoprotein. Biochim. Biophys. Acta. 581:1979;356-359
34. Stambach N.S., Taylor M.E. Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells. Glycobiology. 13:2003;401-410
35. Kondo M., Itami T., Takahashi Y. Preliminary characterization of lectins in the hemolymph of kuruma prawn. Fish Pathol. 33:1998;429-435
36. Inamori K., Saito T., Iwaki D., Nagira T., Iwanaga S., Arisaka F., Kawabata S. A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides. J. Biol. Chem. 274:1999;3272-3278
37. Hall J.L., Rowlands D.T. Heterogeneity of lobster agglutinins: II. Specificity of agglutinin-erythrocyte binding. Biochemistry. 13:1974;828-832
38. Takahashi T., Itoh M., Shimabayashi Y. Aggregation and fragmentation of Phaseolus vulgaris lectin. Agric. Biol. Chem. 44:1980;1655-1657
39. Subbalakshmi C., Nagaraj R., Sitaram N. Biological activities of C-terminal 15-residue synthetic fragment of melittin: design of an analog with improved antibacterial activity. FEBS Lett. 448:1999;62-66
40. Mor A., Hani K., Nicolas P. The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms. J. Biol. Chem. 269:1994;31635-31641
41. Feder R., Dagan A., Mor A. Structure-activity relationship study of antimicrobial dermaseptin S4 showing the consequences of peptide oligomerization on selective cytotoxicity. J. Biol. Chem. 275:2000;4230-4238
42. Martinez-Cruz M., Perez-Campos E., Zenteno E., Cordoba F. Analysis of the lectins from teosinte (Zea diploperensis) and maize (Zea mays) coleoptites. J. Agric. Food Chem. 51:2003;3783-3789
43. Sankaranarayanan R., Sekar K., Banerjee R., Sharma V., Surolia A., Vijayan M. A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold. Nat. Struct. Biol. 3:1996;596-603
44. Pratap J.V., Jeyaprakash A.A., Rani P.G., Sekar K., Surolia A., Vijayan M. Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-alpha-D-mannose: implications to the generation of carbohydrate specificity. J. Mol. Biol. 317:2002;237-247
45. Hernández P., Debray H., Jaekel H., Garfias Y., Jiménez M.C., Martínez-Cairo S., Zenteno E. Chemical characterization of the lectin from Amaranthus leucocarpus syn. hypocondriacus by 2-D proteome analysis. Glycoconj. J. 18:2001;321-329
46. Zenteno R., Vazquez L., Sierra C., Pereyra A., Slomianny M.C., Bouquelet S., Zenteno E. Chemical characterization of the lectin from the freshwater prawn Macrobrachium rosenbergii (De Man) by MALDI-TOF. Comp. Biochem. Physiol., B. 127:2000;243-250
47. Drickamer K. C-type lectin-like domains. Curr. Opin. Struct. Biol. 9:1999;585-590
48. de Wildt R.M., Hoet R.M.A., van Venrooij W.J., Tomlinson I.M., Winter G. Analysis of heavy and light chain pairings indicates that receptor editing shapes the human antibody repertoire. J. Mol. Biol. 285:1999;895-901
49. Gold D.P., Offner H., Sun D., Wiley S., Vandenbark A.A., Wilson D.B. Analysis of T cell receptor beta chains in Lewis rats with experimental allergic encephalomyelitis: conserved complementarity determining region 3. J. Exp. Med. 174:1991;1467-1476