Proteomic analysis of differentially expressed proteins in lymphoid organ of Fenneropenaeus chinensis response to Vibrio anguillarum stimulation

Fish and Shellfish Immunology

Volumn 29, Issue 2, 2010, Pages 186-194

  Zhang, Jinkang ^a,b   Li, Fuhua ^a   Jiang, Hao ^a,b   Yu, Yang ^a,b   Liu, Chengzhang ^a,b   Li, Shihao ^a,b   Wang, Bing ^a   Xiang, Jianhai ^a  

^a INSTITUTE OF OCEANOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

2 DE; Fenneropenaeus chinensis; Lymphoid organ; Proteomics; Vibrio anguillarum

Indexed keywords

CEPHALOPODA; DECAPODA (CRUSTACEA); FENNEROPENAEUS CHINENSIS; LISTONELLA ANGUILLARUM;

ANIMAL; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; IMMUNOLOGY; LYMPHOID TISSUE; MICROBIOLOGY; PENAEIDAE; PROTEOMICS; TWO DIMENSIONAL GEL ELECTROPHORESIS; VIBRIO;

ANIMALS; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; LYMPHOID TISSUE; PENAEIDAE; PROTEOMICS; VIBRIO;

EID: 77954957948     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2010.03.011     Document Type: Article

References (46)

1. Pongsomboon S., Wongpanya R., Tang S., Chalorsrikul A., Tassanakajon A. Abundantly expressed transcripts in the lymphoid organ of the black tiger shrimp, Penaeus monodon, and their implication in immune function. Fish & Shellfish Immunology 2008, 25:485-493.
2. Chongsatja P.O., Bourchookarn A., Lo C.F., Thongboonkerd V., Krittanai C. Proteomic analysis of differentially expressed proteins in Penaeus vannamei hemocytes upon Taura syndrome virus infection. Proteomics 2007, 7:3592-3601.
3. Dimarcq J.L., Imler J.L., Lanot R., Ezekowitz R.A., Hoffmann J.A., Janeway C.A., et al. Treatment of l(2)mbn Drosophila tumorous blood cells with the steroid hormone ecdysone amplifies the inducibility of antimicrobial peptide gene expression. Insect Biochemistry and Molecular Biology 1997, 27:877-886.
4. Soderhall K., Cerenius L. Role of the prophenoloxidase-activating system in invertebrate immunity. Current Opinion in Immunology 1998, 10:23-28.
5. Martin G.G., Poole D., Poole C., Hose J.E., Arias M., Reynolds L., et al. Clearance of bacteria injected into the hemolymph of the penaeid shrimp, Sicyonia-Ingentis. Journal of Invertebrate Pathology 1993, 62:308-315.
6. Vazquez L., Maldonado G., Agundis C., Perez A., Cooper E.L., Zenteno E. Participation of a sialic acid-specific lectin from freshwater prawn Macrobrachium rosenbergii hemocytes in the recognition of non-self cells. Journal of Experimental Zoology 1997, 279:265-272.
7. Munoz M., Cedeno R., Rodriguez J., van der Knaap W.P.W., Mialhe E., Bachere E. Measurement of reactive oxygen intermediate production in haemocytes of the penaeid shrimp, Penaeus vannamei. Aquaculture 2000, 191:89-107.
8. Oka M. Studies on Penaeus orientalis Kishinouye-VIII structure of the newly found lymphoid organ. Bulletin of the Japanese Society of Scientific Fisheries 1969, 35:245-250.
9. van de Braak C.B., Botterblom M.H.A., Taverne N., Van Muiswinkel W.B., Rombout J.H.W.M., van der Knaap W.P.W. The roles of haemocytes and the lymphoid organ in the clearance of injected Vibrio bacteria in Penaeus monodon shrimp. Fish & Shellfish Immunology 2002, 13:293-309.
10. Martin G.G., Hose J.E., Minka G., Rosenberg S. Clearance of bacteria injected into the hemolymph of the ridgeback prawn, Sicyonia ingentis (Crustacea: Decapoda): role of the hematopoietic tissue. Journal of Morphology 1996, 227:227-233.
11. Hasson K.W., Lightner D.V., Mohney L.L., Redman R.M., White B.M. Role of lymphoid organ spheroids in chronic Taura syndrome virus (TSV) infection in Penaeus vannamei. Diseases of Aquatic Organisms 1999, 38:93-105.
12. Burgents J.E., Burnett L.E., Stabb E.V., Burnett K.G. Localization and bacteriostasis of Vibrio introduced into the Pacific white shrimp, Litopenaeus vannamei. Developmental and Comparative Immunology 2005, 29:681-691.
13. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72:248-254.
14. Jiang H., Li F.H., Xie Y.S., Huang B.X., Zhang J.K., Zhang J.Q., et al. Comparative proteomic profiles of the hepatopancreas in Fenneropenaeus chinensis response to hypoxic stress. Proteomics 2009, 9:3353-3367.
15. Duangsuwan P., Tinikul Y., Chotwiwatthanakun C., Vanichviriyakit R., Sobhon P. Changes in the histological organization and spheroid formation in lymphoid organ of Penaeus monodon infected with yellow head virus. Fish & Shellfish Immunology 2008, 25:560-569.
16. May R.C., Machesky L.M. Phagocytosis and the actin cytoskeleton. Journal of Cell Science 2001, 6:1061-1077.
17. Liu W., Han F., Zhang X. Ran GTPase regulates hemocytic phagocytosis of shrimp by interaction with myosin. Journal of Proteome Research 2009, 8:1198-1206.
18. Sun P.S., Soderlund M., Venzon N.C., Ye D.L., Lu Y.N. Isolation and characterization of two actins of the Pacific white shrimp, Litopenaeus vannamei. Marine Biology 2007, 151:2145-2151.
19. Zhu X.J., Dai Z.M., Liu J., Yang W.J. Actin gene in prawn, Macrobrachium rosenbergii: characteristics and differential tissue expression during embryonic development. Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology 2005, 140:599-605.
20. Vandermoere F., El Yazidi-Belkoura I., Demont Y., Slomianny C., Antol J., Lemoine J., et al. Proteomics exploration reveals that actin is a signaling target of the kinase Akt. Molecular & Cellular Proteomics 2007, 6:114-124.
21. Papakonstanti E.A., Stournaras C. Association of PI-3 kinase with PAK1 leads to actin phosphorylation and cytoskeletal reorganization. Molecular Biology of the Cell 2002, 13:2946-2962.
22. Abe A., Saeki K., Yasunaga T., Wakabayashi T. Acetylation at the N-terminus of actin strengthens weak interaction between actin and myosin. Biochemical and Biophysical Research Communications 2000, 268:14-19.
23. de Diego J.L., Katz J.M., Marshall P., Gutierrez B., Manning J.E., Nussenzweig V., et al. The ubiquitin-proteasome pathway plays an essential role in proteolysis during Trypanosoma cruzi remodeling. Biochemistry 2001, 40:1053-1062.
24. He N.H., Liu H.P., Xu X. Identification of genes involved in the response of haemocytes of Penaeus japonicus by suppression subtractive hybridization (SSH) following microbial challenge. Fish & Shellfish Immunology 2004, 17:121-128.
25. Tu B.P., Weissman J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. Journal of Cell Biology 2004, 164:341-346.
26. Freedman R.B., Hirst T.R., Tuite M.F. Protein disulphide isomerase: building bridges in protein folding. Trends in Biochemical Sciences 1994, 19:331-336.
27. Luana W., Li F.H., Wang B., Zhang X.J., Liu Y.C., Xiang J.H. Molecular characteristics and expression analysis of calreticulin in Chinese shrimp Fenneropenaeus chinensis. Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology 2007, 147:482-491.
28. Asgari S., Schmidt O. Is cell surface calreticulin involved in phagocytosis by insect hemocytes?. Journal of Insect Physiology 2003, 49:545-550.
29. Kuraishi T., Manaka J., Kono M., Ishii H., Yamamoto N., Koizumi K., et al. Identification of calreticulin as a marker for phagocytosis of apoptotic cells in Drosophila. Experimental Cell Research 2007, 313:500-510.
30. Wang B., Li F., Dong B., Zhang X., Zhang C., Xiang J. Discovery of the genes in response to white spot syndrome virus (WSSV) infection in Fenneropenaeus chinensis through cDNA microarray. Marine Biotechnology (NY) 2006, 8:491-500.
31. Hsing L.C.R.A. The lysosomal cysteine proteases in MHC class II antigen presentation. Immunological Reviews 2005, 207:229-241.
32. Chwieralski C.E., Welte T., Buhling F. Cathepsin-regulated apoptosis. Apoptosis 2006, 11:143-149.
33. Liu J.P., Guo Q., Chen B.X., Yu Y., Lu H., Li Y.Y. Cathepsin B and its interacting proteins, bikunin and TSRC1, correlate with TNF-induced apoptosis of ovarian cancer cells OV-90. FEBS Letters 2006, 580:245-250.
34. Pacheco F.J., Servin J., Dang D., Kim J., Molinaro C., Daniels T., et al. Involvement of lysosomal cathepsins in the cleavage of DNA topoisomerase I during necrotic cell death. Arthritis and Rheumatism 2005, 52:2133-2145.
35. Anggraeni M.S., Owens L. The haemocytic origin of lymphoid organ spheroid cells in the penaeid prawn Penaeus monodon. Diseases of Aquatic Organisms 2000, 40:85-92.
36. Robalino J., Almeida J.S., McKillen D., Colglazier J., Trent H.F., Chen Y.A., et al. Insights into the immune transcriptome of the shrimp Litopenaeus vannamei: tissue-specific expression profiles and transcriptomic responses to immune challenge. Physiological Genomics 2007, 29:44-56.
37. Assavalapsakul W., Smith D.R., Panyim S. Identification and characterization of a Penaeus monodon lymphoid cell-expressed receptor for the yellow head virus. Journal of Virology 2006, 80:262-269.
38. Gunning P., Weinberger R., Jeffrey P. Actin and tropomyosin isoforms in morphogenesis. Anatomy and Embryology (Berlin) 1997, 195:311-315.
39. Mounier N., Arrigo A.-P. Actin cytoskeleton and small heat shock proteins: how do they interact. Cell Stress Chaperones 2002, 7:167-176.
40. Bourchookarn A., Havanapan P.O., Thongboonkerd V., Krittanai C. Proteomic analysis of altered proteins in lymphoid organ of yellow head virus infected Penaeus monodon. Biochimica Et Biophysica Acta-Proteins and Proteomics 2008, 1784:504-511.
41. Harrison R.E., Grinstein S. Phagocytosis and the microtubule cytoskeleton. Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire 2002, 80:509-515.
42. +-Atpase in animal virus entry. Journal of General Virology 1994, 75:2595-2606.
43. Nurten R., Bermek E. Interactions of elongation factor 2(EF-2) with guanine nucleotides and ribosomes: binding of periodate-oxidized guanine nucleotides to EF-2. European Journal of Biochemistry 1980, 3:551-555.
44. Gomis-Ruth F.X. Structure and mechanism of metallocarboxypeptidases. Critical Reviews in Biochemistry and Molecular Biology 2008, 43:319-345.
45. Stevens R.L., Adachi R. Protease-proteoglycan complexes of mouse and human mast cells and importance of their beta-tryptase-heparin complexes in inflammation and innate immunity. Immunological Reviews 2007, 217:155-167.
46. Wang H.C., Wang H.C., Leu J.H., Kou G.H., Wang A.H.J., Lo C.F. Protein expression profiling of the shrimp cellular response to white spot syndrome virus infection. Developmental and Comparative Immunology 2007, 31:672-686.