Identification of a type of human IgG-like protein in shrimp Penaeus vannamei by mass spectrometry

Journal of Experimental Marine Biology and Ecology

Volumn 301, Issue 1, 2004, Pages 39-54

  Zhang, Yueling ^a   Wang, Sanying ^a   Peng, Xuanxian ^a  

^a XIAMEN UNIVERSITY   (China)

Author keywords

Hemocyanin; IgG like protein; Penaeus vannamei; Proteomics

Indexed keywords

DISEASE RESISTANCE; MASS SPECTROMETRY; PROTEIN; SHRIMP CULTURE;

ARTHROPODA; CAPRA HIRCUS; CRUSTACEA; DECAPODA (CRUSTACEA); INVERTEBRATA; LITOPENAEUS VANNAMEI; PENAEUS;

EID: 1842816565     PISSN: 00220981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jembe.2003.09.011     Document Type: Article

References (45)

1. Adachi K., Hirata T., Nagai K., Sakaguchi M. Hemocyanin a most likely inducer of black spots in kuruma prawn Penaeus japonicus during storage. J. Food Sci. 66:2001;1130-1136.
2. Adachi K., Hirata T., Nishioka T., Sakaguchi M. Hemocyte components in crustaceans convert hemocyanin into phenoloxidase-like enzyme. Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. 134:2003;135-141.
3. Arala-Chaves M., Sequeira T. Is there any kind of adaptive immunity in invertebrates? Aquaculture. 191:2000;247-258.
4. Bachère E. Shrimp immunity and disease control. Aquaculture. 191:2000;3-11.
5. Bachère E., Destoumieux D., Bulet P. Penaeidins, antimicrobial peptides of shrimp: a comparison with other effectors of innate immunity. Aquaculture. 191:2000;71-88.
6. Benian G.M., Kiff J.E., Neckelmann N., Moerman D.G., Waterston R.H. Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans. Nature. 342:1989;45-50.
7. Bergman A.C., Benjamin T., Alaiya A., Waltham M., Sakaguchi K., Franzen B., Linder S., Bergman T., Auer G., Appella E., Wirth P.J., Jornvall H. Identification of gel-separated tumor marker proteins by mass spectrometry. Electrophoresis. 21:2000;679-686.
8. Bettencourt R., Assefaw-Redda Y., Faye I. The insect immune protein hemolin is expressed during oogenesis and embryogenesis. Mech. Dev. 95:2000;301-304.
9. H genes expressed by individual B cells of a patient with X-linked hyper-IgM syndrome. Int. Immunol. 12:2000;767-775.
10. Bridges S.L. Jr., Lee S.K., Johnson M.L., Lavelle J.C., Fowler P.G., Koopman W.J., Schroeder H.W. Jr. Somatic mutation and CDR3 lengths of immunoglobulin kappa light chains expressed in patients with rheumatoid arthritis and in normal individuals. J. Clin. Invest. 96:1995;831-841.
11. Brummendorf T., Lemmon V. Immnoglobulin superfamily receptors: cis-interactions, intracellular adapters and alternative splicing regulate adhesion. Curr. Opin. Cell Biol. 13:2001;611-618.
12. Burmester T. Molecular evolution of the arthropod hemocyanin superfamily. Mol. Biol. Evol. 18:2001;184-195.
13. Decker H., Rimke T. Tarantula hemocyanin shows phenoloxidase activity. J. Biol. Chem. 273:1998;25889-25892.
14. Decker H., Ryan M., Jaenicke E., Terwilliger N. SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister. J. Biol. Chem. 276:2001;17796-17799.
15. Destoumieux-Garzón D., Saulnier D., Garnier J., Jouffrey C., Bulet P., Bachère E. Crustacean immunity. Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge. J. Biol. Chem. 276:2001;47070-47077.
16. Dunn-Walters D.K., Hackett M., Boursier L., Ciclitira P.J., Morgan P., Challacombe S.J., Spencer J. Characteristics of human IgA and IgM genes used by plasma cells in the salivary gland resemble those used in duodenum but not those used in the spleen. J. Immunol. 164:2000;1595-1601.
17. Flegel T.W. Major viral diseases of the black tiger prawn (Penaeus monodon) in Thailand. World J. Microbiol. Biotechnol. 13:1997;433-442.
18. Garbe J.C., Yang E., Fristrom J.W. IMP-L2: an essential secreted immunoglobulin family member implicated in neural and ectodermal development in Drosophila. Development. 119:1993;1237-1250.
19. Hoek R.M., Smit A.B., Frings H., Vink J.M., de Jong-Brink M., Geraerts W.P. A new Ig-superfamily member, molluscan defence molecule (MDM) from Lymnaea stagnalis, is down-regulated during parasitosis. Eur. J. Immunol. 26:1996;939-944.
20. Iwanaga S., Kawabata S., Muta T. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J. Biochem. 123:1998;1-15.
21. Johansson M.W. Cell adhesion molecules in invertebrate immunity. Dev. Comp. Immunol. 23:1999;303-315.
22. Krol R.M., Hawkins W.E., Overstreet R.M. Rickettsial and mollicute infections in hepatopancreatic cells of cultured pacific white shrimp Penaeus vannamei. J. Invertebr. Pathol. 57:1991;362-370.
23. Kurth J., Spieker T., Wustrow J., Strickler G.J., Hansmann L.M., Rajewsky K., Kuppers R. EBV-infected B cells in infectious mononucleosis: viral strategies for spreading in the B cell compartment and establishing latency. Immunity. 13:2000;485-495.
24. Ladendorff N.E., Kanost M.R. Bacteria-induced protein P4 (hemolin) from Manduca sexta: a member of the immunoglobulin superfamily which can inhibit hemocyte aggregation. Arch. Insect Biochem. Physiol. 18:1991;285-300.
25. Lanz-Mendoza H., Bettencourt R., Fabbri M., Faye I. Regulation of the insect immune response: the effect of hemolin on cellular immune mechanisms. Cell. Immunol. 169:1996;47-54.
26. Lee S.Y., Lee B.L., Söderhäll K. Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculs. J. Biol. Chem. 278:2003;7927-7933.
27. Lightner D.V., Redman R.M., Bell T.A. Infectious hypodermal and hematopoietic necrosis, a newly recognized virus disease of penaeid shrimp. J. Invertebr. Pathol. 42:1983;62-70.
28. Marques M.R.F., Barracco M.A. Lectins, as non-self-recognition factors, in crustaceans. Aquaculture. 191:2000;23-44.
29. Mendoza H.L., Faye I. Physiology aspects of the immunoglobulin superfamily in invertebrates. Dev. Comp. Immunol. 23:1999;359-374.
30. Nagai T., Kawabata S.-I. A link between blood coagulation and prophenol oxidase activation in arthropod host defense. J. Biol. Chem. 275:2000;29264-29267.
31. Nagai T., Osaki T., Kawabata S-i. Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides. J. Biol. Chem. 276:2001;27166-27170.
32. Neiland A.E., Soley N., Varley J.B., Whitmarsh D.J. Shrimp aquaculture: economic perspectives for policy development. Mar. Policy. 25:2001;265-279.
33. Nelson R.E., Fessler L.I., Takagi Y., Blumberg B., Keene D.R., Olson P.F., Parker C.G., Fessler J.H. Peroxidasin: a novel enzyme-matrix protein of Drosophila development. EMBO J. 13:1994;3438-3447.
34. O'Farrell P.H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:1975;4007-4021.
35. Pancer Z., Skorokhod A., Blumbach B., MuÈller W.E. Multiple Ig-like featuring genes divergent within and among individuals of the marine sponge Geodia cydonium. Gene. 207:1998;227-233.
36. Paul R.J., Pirow R. The physiological significance of respiratory proteins in invertebrates. Zool.-Anal. Complex Syst. 100:1997;298-306.
37. Peng X.X., Luo W., Zhang J.Y., Wang S.Y., Lin S.C. Rapid detection of Shigella species in environmental sewage by an immunocapture PCR with universal primers. Appl. Environ. Microbiol. 68:2002;2580-2583.
38. Roch P. Defense mechanisms and disease prevention in farmed marine invertebrates. Aquaculture. 172:1999;125-145.
39. Rodríguez J., Le Moullac G. State of the art of immunological tools and health control of penaeid shrimp. Aquaculture. 191:2000;109-119.
40. Salvato B., Santamaria M., Beltramini M., Alzuet G., Casella L. The enzymatic properties of octopus vulgaris hemocyanin: o-diphenol oxidase activity. Biochemistry. 37:1998;14065-14077.
41. Schachner M. Neural recognition molecules and synaptic plasticity. Curr. Opin. Cell Biol. 9:1997;627-634.
42. Vasta G.R., Ahmed H., Fink N.E., Elola M.T., Marsh A.G., Snowden A., Odom E.W. Animal lectins as self/non-self recognition molecules. Biochemical and genetic approaches to understanding their biological roles and evolution. Ann. N.Y. Acad. Sci. 712:1994;55-73.
43. Wang W.Q., Li A.J., Lan C.X., Guo J. Measuring immune factors in the serum of Penaeus chinensis with the method of nephelometry. J. Fish. China. 22:1998;170-175.
44. Zhang Y.L., Peng X.X., Wang S.Y. Study on three classes of immunogolobulin-like components in Penaeus japonicus. Mar. Sci. 25:2001;37-41.
45. Zlateva T., Muro P.D., Salvato B., Beltramini M. The o-diphenol oxidase activity of arthropod hemocyanin. FEBS Lett. 384:1996;251-254.