메뉴 건너뛰기




Volumn 26, Issue 4, 2007, Pages 1169-1175

Isoforms of Litopenaeus vannamei anti-lipopolysaccharide and its expression by bacterial challenge

Author keywords

ALF; Gene expression; Immune response; Immunity; Litopenaeus; Shrimp; Vibrio

Indexed keywords

ARTHROPODA; BACTERIA (MICROORGANISMS); DECAPODA (CRUSTACEA); LITOPENAEUS; LITOPENAEUS VANNAMEI; PENAEIDAE; VIBRIO; VIBRIO ALGINOLYTICUS;

EID: 38349033560     PISSN: 07308000     EISSN: None     Source Type: Journal    
DOI: 10.2983/0730-8000(2007)26[1169:IOLVAA]2.0.CO;2     Document Type: Article
Times cited : (13)

References (53)
  • 3
    • 0034694378 scopus 로고    scopus 로고
    • Shrimp immunity and disease control
    • Bachère, E. 2000. Shrimp immunity and disease control. Aquaculture 191:3-11.
    • (2000) Aquaculture , vol.191 , pp. 3-11
    • Bachère, E.1
  • 4
    • 1642422727 scopus 로고    scopus 로고
    • Insights into the anti-microbial defense of marine invertebrates: The penaeid shrimps and the oyster Crassostrea gigas
    • Bachère, E., Y. Gueguen, M. González, J. de Lorgeril, J. Garnier & B. Romestand. 2004. Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas. Immunol. Rev. 198:149-168.
    • (2004) Immunol. Rev , vol.198 , pp. 149-168
    • Bachère, E.1    Gueguen, Y.2    González, M.3    de Lorgeril, J.4    Garnier, J.5    Romestand, B.6
  • 5
    • 0036071479 scopus 로고    scopus 로고
    • Crustins, Homologues of an 11.5-kDa Antibacterial peptide, from Two Species of Penaeid Shrimp, Litopenaeus vannamei and Litopenaeus setiferus
    • Bartlett, T. C., B. J. Cuthbertson, E. F. Shepard, R. W. Chapman, P. S. Gross & G. W. Warr. 2002. Crustins, Homologues of an 11.5-kDa Antibacterial peptide, from Two Species of Penaeid Shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Mar. Biotechnol. 4:278-293.
    • (2002) Mar. Biotechnol , vol.4 , pp. 278-293
    • Bartlett, T.C.1    Cuthbertson, B.J.2    Shepard, E.F.3    Chapman, R.W.4    Gross, P.S.5    Warr, G.W.6
  • 7
    • 0032401651 scopus 로고    scopus 로고
    • Biophysical characterisation of lysozyme binding to LPS Re and lipid A
    • Brandenburg, K., M. H. Koch & U. Seydel. 1998. Biophysical characterisation of lysozyme binding to LPS Re and lipid A. Eur. J. Biochem. 258:686-695.
    • (1998) Eur. J. Biochem , vol.258 , pp. 686-695
    • Brandenburg, K.1    Koch, M.H.2    Seydel, U.3
  • 8
  • 10
    • 0030692830 scopus 로고    scopus 로고
    • Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (decapoda)
    • Destoumieux, D., P. Bulet, D. Loew, A. Vandorsselaer, J. Rodriguez & E. Bachère. 1997. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (decapoda). J. Biol. Chem. 272:28398-28406.
    • (1997) J. Biol. Chem , vol.272 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    Vandorsselaer, A.4    Rodriguez, J.5    Bachère, E.6
  • 11
    • 0034002081 scopus 로고    scopus 로고
    • Penaeidins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge
    • Destoumieux, D., M. Muñoz, C. Cosseau, J. Rodríguez, P. Bulet, M. Comps & E. Bachère. 2000. Penaeidins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge. J. Cell Sci. 113:461-469.
    • (2000) J. Cell Sci , vol.113 , pp. 461-469
    • Destoumieux, D.1    Muñoz, M.2    Cosseau, C.3    Rodríguez, J.4    Bulet, P.5    Comps, M.6    Bachère, E.7
  • 12
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A. D., E. Hofmann, J. W. Coulton, K. Diederichs & W. Welte. 1998. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282:2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 14
    • 0034927549 scopus 로고    scopus 로고
    • Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp
    • Gross, P. S., T. C. Bartlett, C. L. Browdy, R. W. Chapman & G. W. Warr. 2001. Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp, L. setiferus. Dev. Comp. Immunol. 25:565-577.
    • (2001) L. setiferus. Dev. Comp. Immunol , vol.25 , pp. 565-577
    • Gross, P.S.1    Bartlett, T.C.2    Browdy, C.L.3    Chapman, R.W.4    Warr, G.W.5
  • 15
    • 0141922176 scopus 로고    scopus 로고
    • Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species
    • Hikima, S., J.-i. Hikima, J. Rojtinnakorn, I. Hirono & T. Aoki. 2003. Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species. Gene 316:187-195.
    • (2003) Gene , vol.316 , pp. 187-195
    • Hikima, S.1    Hikima, J.-I.2    Rojtinnakorn, J.3    Hirono, I.4    Aoki, T.5
  • 16
    • 0027171383 scopus 로고
    • Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 A resolution
    • Hoess, A., S. Watson, G. R. Siber & R. Liddington. 1993. Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 A resolution. EMBO J. 12:3351-3356.
    • (1993) EMBO J , vol.12 , pp. 3351-3356
    • Hoess, A.1    Watson, S.2    Siber, G.R.3    Liddington, R.4
  • 17
    • 0345863449 scopus 로고    scopus 로고
    • Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase
    • Huang, C. C., K. Sritunyalucksana, K. Söderhäll & Y. L. Song. 2004. Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase. Dev. Comp. Immunol. 28:279-294.
    • (2004) Dev. Comp. Immunol , vol.28 , pp. 279-294
    • Huang, C.C.1    Sritunyalucksana, K.2    Söderhäll, K.3    Song, Y.L.4
  • 18
    • 0027394999 scopus 로고
    • The limulus clotting reaction
    • Iwanaga, S. 1993. The limulus clotting reaction. Curr. Opin. Immunol. 5:74-82.
    • (1993) Curr. Opin. Immunol , vol.5 , pp. 74-82
    • Iwanaga, S.1
  • 19
    • 0032159526 scopus 로고    scopus 로고
    • Evolution and phylogeny of defense molecules associated with innate immunity in horseshoe crab
    • Iwanaga, S. & S. I. Kawabata. 1998. Evolution and phylogeny of defense molecules associated with innate immunity in horseshoe crab. Front. Biosci. 3:973-984.
    • (1998) Front. Biosci , vol.3 , pp. 973-984
    • Iwanaga, S.1    Kawabata, S.I.2
  • 20
    • 13544251554 scopus 로고    scopus 로고
    • A four-Kazal domain protein in Litopenaeus vannamei hemocytes
    • Jiménez-Vega, F. & F. Vargas-Albores. 2005. A four-Kazal domain protein in Litopenaeus vannamei hemocytes. Dev. Comp. Immunol. 29:385-391.
    • (2005) Dev. Comp. Immunol , vol.29 , pp. 385-391
    • Jiménez-Vega, F.1    Vargas-Albores, F.2
  • 21
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
    • Kumar, S., K. Tamura & M. Nei. 2004. MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief. Bioinform. 5:150-163.
    • (2004) Brief. Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 22
    • 28244463332 scopus 로고    scopus 로고
    • Molecular cloning and expression profile of putative antilipopolysaccharide factor in Chinese shrimp (Fenneropenaeus chinensis)
    • Liu, F., Y. Liu, F. Li, B. Dong & J. Xiang. 2005. Molecular cloning and expression profile of putative antilipopolysaccharide factor in Chinese shrimp (Fenneropenaeus chinensis). Mar. Biotechnol. 7:600-608.
    • (2005) Mar. Biotechnol , vol.7 , pp. 600-608
    • Liu, F.1    Liu, Y.2    Li, F.3    Dong, B.4    Xiang, J.5
  • 23
    • 33750306792 scopus 로고    scopus 로고
    • Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus
    • Liu, H., P. Jiravanichpaisal, I. Söderhäll, L. Cerenius & K. Söderhäll. 2006. Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus. J. Virol. 80:10365-10371.
    • (2006) J. Virol , vol.80 , pp. 10365-10371
    • Liu, H.1    Jiravanichpaisal, P.2    Söderhäll, I.3    Cerenius, L.4    Söderhäll, K.5
  • 25
    • 0021799698 scopus 로고
    • Isolation and biological activities of Limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharides (LPS)
    • Morita, T., S. Ohtsubo, T. Nakamura, S. Tanaka, S. Iwanaga, K. Ohashi & M. Niwa. 1985. Isolation and biological activities of Limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharides (LPS). J. Biochem. (Tokyo) 97:1611-1620.
    • (1985) J. Biochem. (Tokyo) , vol.97 , pp. 1611-1620
    • Morita, T.1    Ohtsubo, S.2    Nakamura, T.3    Tanaka, S.4    Iwanaga, S.5    Ohashi, K.6    Niwa, M.7
  • 26
    • 0036274247 scopus 로고    scopus 로고
    • Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp
    • Muñoz, M., F. Vandenbulcke, D. Saulnier & E. Bachère. 2002. Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp. Eur. J. Biochem. 269:2678-2689.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2678-2689
    • Muñoz, M.1    Vandenbulcke, F.2    Saulnier, D.3    Bachère, E.4
  • 27
    • 0036568279 scopus 로고    scopus 로고
    • Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles
    • Pollastri, G., D. Przybylski, B. Rost & P. Baldi. 2002. Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles. Proteins 47:228-235.
    • (2002) Proteins , vol.47 , pp. 228-235
    • Pollastri, G.1    Przybylski, D.2    Rost, B.3    Baldi, P.4
  • 28
    • 0035524463 scopus 로고    scopus 로고
    • Peptides neutralizing lipopolysaccharide - structure and function
    • Pristovsek, P. & J. Kidric. 2001. Peptides neutralizing lipopolysaccharide - structure and function. Mini Rev. Med. Chem. 1:409-416.
    • (2001) Mini Rev. Med. Chem , vol.1 , pp. 409-416
    • Pristovsek, P.1    Kidric, J.2
  • 30
    • 0033198883 scopus 로고    scopus 로고
    • Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab
    • Relf, J. M., J. R. Chisholm, G. D. Kemp & V. J. Smith. 1999. Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas. Eur. J. Biochem. 264:350-357.
    • (1999) Carcinus maenas. Eur. J. Biochem , vol.264 , pp. 350-357
    • Relf, J.M.1    Chisholm, J.R.2    Kemp, G.D.3    Smith, V.J.4
  • 31
    • 0036634213 scopus 로고    scopus 로고
    • The Lipopolysaccharide and β-1,3-Glucan binding protein gene is upregulated in white spot virus-infected Shrimp (Penaeus stylirostris)
    • Roux, M. M., A. Pain, K. R. Klimpel & A. K. Dhar. 2002. The Lipopolysaccharide and β-1,3-Glucan binding protein gene is upregulated in white spot virus-infected Shrimp (Penaeus stylirostris). J. Virol. 76:7140-7149.
    • (2002) J. Virol , vol.76 , pp. 7140-7149
    • Roux, M.M.1    Pain, A.2    Klimpel, K.R.3    Dhar, A.K.4
  • 33
    • 0028964136 scopus 로고
    • Defensins in granules of phagocytic and nonphagocytic cells
    • Selsted, M. E. & A. J. Ouellette. 1995. Defensins in granules of phagocytic and nonphagocytic cells. Trends Cell Biol. 5:114-119.
    • (1995) Trends Cell Biol , vol.5 , pp. 114-119
    • Selsted, M.E.1    Ouellette, A.J.2
  • 34
    • 0031870993 scopus 로고    scopus 로고
    • The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids
    • Shi, J. & T. Ganz. 1998. The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids. Infect. Immun. 66:3611-3617.
    • (1998) Infect. Immun , vol.66 , pp. 3611-3617
    • Shi, J.1    Ganz, T.2
  • 36
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase-activating system in invertebrate immunity
    • Söderhäll, K. & L. Cerenius. 1998. Role of the prophenoloxidase-activating system in invertebrate immunity. Curr. Opin. Immunol. 10:23-28.
    • (1998) Curr. Opin. Immunol , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2
  • 37
    • 0002749939 scopus 로고    scopus 로고
    • The prophenoloxidase activating system in invertebrates
    • K. Söderhäll, S. Iwanaga & G. R. Vasta, editors, Fair Haven, NJ: SOS Publications, pp
    • Söderhäll, K., L. Cerenius & M. W. Johansson. 1996. The prophenoloxidase activating system in invertebrates. In: K. Söderhäll, S. Iwanaga & G. R. Vasta, editors. New directions in invertebrate immunology, Fair Haven, NJ: SOS Publications, pp. 229-253.
    • (1996) New directions in invertebrate immunology , pp. 229-253
    • Söderhäll, K.1    Cerenius, L.2    Johansson, M.W.3
  • 43
    • 0015396521 scopus 로고
    • Natural and induced bactericidal activities in the hemolymph of the lobster, Homarus americanus: Products of hemocyte-plasma interaction
    • Stewart, J. E. & B. M. Zwicker. 1972. Natural and induced bactericidal activities in the hemolymph of the lobster, Homarus americanus: products of hemocyte-plasma interaction. Can. J. Microbiol. 18:1499-1509.
    • (1972) Can. J. Microbiol , vol.18 , pp. 1499-1509
    • Stewart, J.E.1    Zwicker, B.M.2
  • 44
    • 9944233151 scopus 로고    scopus 로고
    • Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach
    • Supungul, P., S. Klinbunga, R. Pichyangkura, I. Hirono, T. Aoki & A. Tassanakajon. 2004. Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach. Dis. Aquat. Org. 61:123-135.
    • (2004) Dis. Aquat. Org , vol.61 , pp. 123-135
    • Supungul, P.1    Klinbunga, S.2    Pichyangkura, R.3    Hirono, I.4    Aoki, T.5    Tassanakajon, A.6
  • 46
    • 0025989172 scopus 로고
    • Morphology of the granular hemocytes of the Japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances
    • Toh, Y., A. Mizutani, F. Tokunaga, T. Muta & S. Iwanaga. 1991. Morphology of the granular hemocytes of the Japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances. Cell Tissue Res. 266:137-147.
    • (1991) Cell Tissue Res , vol.266 , pp. 137-147
    • Toh, Y.1    Mizutani, A.2    Tokunaga, F.3    Muta, T.4    Iwanaga, S.5
  • 47
    • 0038447123 scopus 로고    scopus 로고
    • Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock
    • Van Amersfoort, E. S., T. J. Van Berkel & J. Kuiper. 2003. Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock. Clin. Microbiol. Rev. 16:379-414.
    • (2003) Clin. Microbiol. Rev , vol.16 , pp. 379-414
    • Van Amersfoort, E.S.1    Van Berkel, T.J.2    Kuiper, J.3
  • 48
    • 0027467258 scopus 로고
    • A Lipopolysaccharide-binding agglutinin isolated from brown shrimp (Penaeus californiensis HOLMES) haemolymph
    • Vargas-Albores, F., A. Guzmán-Murillo & J. L. Ochoa. 1993a. A Lipopolysaccharide-binding agglutinin isolated from brown shrimp (Penaeus californiensis HOLMES) haemolymph. Comp. Biochem. Physiol. 104A:407-413.
    • (1993) Comp. Biochem. Physiol , vol.104 A , pp. 407-413
    • Vargas-Albores, F.1    Guzmán-Murillo, A.2    Ochoa, J.L.3
  • 49
    • 0027376379 scopus 로고
    • An anticoagulant solution for haemolymph collection and prophenoloxidase studies of Penaeid shrimp (Penaeus californiensis)
    • Vargas-Albores, F., M. A. Guzmán-Murillo & J.-L. Ochoa. 1993b. An anticoagulant solution for haemolymph collection and prophenoloxidase studies of Penaeid shrimp (Penaeus californiensis). Comp. Biochem. Physiol. 106A:299-303.
    • (1993) Comp. Biochem. Physiol , vol.106 A , pp. 299-303
    • Vargas-Albores, F.1    Guzmán-Murillo, M.A.2    Ochoa, J.-L.3
  • 51
    • 0034694373 scopus 로고    scopus 로고
    • Beta glucan binding protein and its role in shrimp immune response
    • Vargas-Albores, F. & G. Yepiz-Plascencia. 2000. Beta glucan binding protein and its role in shrimp immune response. Aquaculture 191:13-21.
    • (2000) Aquaculture , vol.191 , pp. 13-21
    • Vargas-Albores, F.1    Yepiz-Plascencia, G.2
  • 53
    • 1842455284 scopus 로고    scopus 로고
    • Disulfide connectivity prediction using recursive neural networks and evolutionary information
    • Vullo, A. & P. Frasconi. 2004. Disulfide connectivity prediction using recursive neural networks and evolutionary information. Bioinformatics 20:653-659.
    • (2004) Bioinformatics , vol.20 , pp. 653-659
    • Vullo, A.1    Frasconi, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.