메뉴 건너뛰기




Volumn 24, Issue 1, 2008, Pages 46-54

Anti-lipopolysaccharide factors from the black tiger shrimp, Penaeus monodon, are encoded by two genomic loci

Author keywords

Anti lipopolysaccharide factor; cis regulatory element; Genomic sequence; Penaeus monodon; RNA splicing

Indexed keywords

BACTERIA (MICROORGANISMS); DECAPODA (CRUSTACEA); PENAEUS MONODON; VIBRIO HARVEYI;

EID: 38349193705     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2007.07.010     Document Type: Article
Times cited : (80)

References (38)
  • 1
    • 0033022730 scopus 로고    scopus 로고
    • Antimicrobial peptides in insects; structure and function
    • Bulet P., Hetru C., Dimarcq J.L., and Hoffmann D. Antimicrobial peptides in insects; structure and function. Dev Comp Immunol 23 (1999) 329-344
    • (1999) Dev Comp Immunol , vol.23 , pp. 329-344
    • Bulet, P.1    Hetru, C.2    Dimarcq, J.L.3    Hoffmann, D.4
  • 2
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock R.E., and Scott M.G. The role of antimicrobial peptides in animal defenses. Proc Natl Acad Sci U S A 97 (2000) 8856-8861
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 3
    • 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., Munoz M., Cosseau C., Rodriguez J., Bulet P., Comps M., et al. Penaeidins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge. J Cell Sci 113 Pt 3 (2000) 461-469
    • (2000) J Cell Sci , vol.113 , Issue.PART 3 , pp. 461-469
    • Destoumieux, D.1    Munoz, M.2    Cosseau, C.3    Rodriguez, J.4    Bulet, P.5    Comps, M.6
  • 4
    • 20644460364 scopus 로고    scopus 로고
    • Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon
    • Somboonwiwat K., Marcos M., Tassanakajon A., Klinbunga S., Aumelas A., Romestand B., et al. Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon. Dev Comp Immunol 29 (2005) 841-851
    • (2005) Dev Comp Immunol , vol.29 , pp. 841-851
    • Somboonwiwat, K.1    Marcos, M.2    Tassanakajon, A.3    Klinbunga, S.4    Aumelas, A.5    Romestand, B.6
  • 5
    • 33845600236 scopus 로고    scopus 로고
    • Lysozyme gene expression by hemocytes of Pacific white shrimp, Litopenaeus vannamei, after injection with Vibrio
    • Burge E.J., Madigan D.J., Burnett L.E., and Burnett K.G. Lysozyme gene expression by hemocytes of Pacific white shrimp, Litopenaeus vannamei, after injection with Vibrio. Fish Shellfish Immunol 22 (2007) 327-339
    • (2007) Fish Shellfish Immunol , vol.22 , pp. 327-339
    • Burge, E.J.1    Madigan, D.J.2    Burnett, L.E.3    Burnett, K.G.4
  • 6
    • 0020416253 scopus 로고
    • Limulus anti-LPS factor: an anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system
    • Tanaka S., Nakamura T., Morita T., and Iwanaga S. Limulus anti-LPS factor: an anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system. Biochem Biophys Res Commun 105 (1982) 717-723
    • (1982) Biochem Biophys Res Commun , vol.105 , pp. 717-723
    • Tanaka, S.1    Nakamura, T.2    Morita, T.3    Iwanaga, S.4
  • 8
    • 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, L. setiferus
    • Gross P.S., Bartlett T.C., Browdy C.L., Chapman R.W., and Warr G.W. 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 (2001) 565-577
    • (2001) 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
  • 9
    • 28244463332 scopus 로고    scopus 로고
    • Molecular cloning and expression profile of putative antilipopolysaccharide factor in Chinese shrimp (Fenneropenaeus chinensis)
    • Liu F., Liu Y., Li F., Dong B., and Xiang J. Molecular cloning and expression profile of putative antilipopolysaccharide factor in Chinese shrimp (Fenneropenaeus chinensis). Mar Biotechnol (NY) 7 (2005) 600-608
    • (2005) Mar Biotechnol (NY) , vol.7 , pp. 600-608
    • Liu, F.1    Liu, Y.2    Li, F.3    Dong, B.4    Xiang, J.5
  • 10
    • 33645883237 scopus 로고    scopus 로고
    • Cloning and characterization of a LPS-regulatory gene having an LPS binding domain in kuruma prawn Marsupenaeus japonicus
    • Nagoshi H., Inagawa H., Morii K., Harada H., Kohchi C., Nishizawa T., et al. Cloning and characterization of a LPS-regulatory gene having an LPS binding domain in kuruma prawn Marsupenaeus japonicus. Mol Immunol 43 (2006) 2061-2069
    • (2006) Mol Immunol , vol.43 , pp. 2061-2069
    • Nagoshi, H.1    Inagawa, H.2    Morii, K.3    Harada, H.4    Kohchi, C.5    Nishizawa, T.6
  • 11
    • 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., Jiravanichpaisal P., Soderhall I., Cerenius L., and Soderhall K. Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus. J Virol 80 (2006) 10365-10371
    • (2006) J Virol , vol.80 , pp. 10365-10371
    • Liu, H.1    Jiravanichpaisal, P.2    Soderhall, I.3    Cerenius, L.4    Soderhall, K.5
  • 12
    • 34247334692 scopus 로고    scopus 로고
    • Antilipopolysaccharide factor (ALF) of mud crab Scylla paramamosain: molecular cloning, genomic organization and the antimicrobial activity of its synthetic LPS binding domain
    • Imjongjirak C., Amparyup P., Tassanakajon A., and Sittipraneed S. Antilipopolysaccharide factor (ALF) of mud crab Scylla paramamosain: molecular cloning, genomic organization and the antimicrobial activity of its synthetic LPS binding domain. Mol Immunol 44 (2007) 3195-3203
    • (2007) Mol Immunol , vol.44 , pp. 3195-3203
    • Imjongjirak, C.1    Amparyup, P.2    Tassanakajon, A.3    Sittipraneed, S.4
  • 13
    • 0021799698 scopus 로고
    • Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS)
    • Morita T., Ohtsubo S., Nakamura T., Tanaka S., Iwanaga S., Ohashi K., et al. Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS). J Biochem (Tokyo) 97 (1985) 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
  • 15
    • 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., Watson S., Siber G.R., and Liddington R. Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 A resolution. EMBO J 12 (1993) 3351-3356
    • (1993) EMBO J , vol.12 , pp. 3351-3356
    • Hoess, A.1    Watson, S.2    Siber, G.R.3    Liddington, R.4
  • 16
    • 14944342494 scopus 로고    scopus 로고
    • Structure of a synthetic fragment of the LALF protein when bound to lipopolysaccharide
    • Pristovsek P., Feher K., Szilagyi L., and Kidric J. Structure of a synthetic fragment of the LALF protein when bound to lipopolysaccharide. J Med Chem 48 (2005) 1666-1670
    • (2005) J Med Chem , vol.48 , pp. 1666-1670
    • Pristovsek, P.1    Feher, K.2    Szilagyi, L.3    Kidric, J.4
  • 17
    • 0032994485 scopus 로고    scopus 로고
    • Induction and regulation of antimicrobial peptides in Drosophila
    • Engstrom Y. Induction and regulation of antimicrobial peptides in Drosophila. Dev Comp Immunol 23 (1999) 345-358
    • (1999) Dev Comp Immunol , vol.23 , pp. 345-358
    • Engstrom, Y.1
  • 18
    • 33645233336 scopus 로고    scopus 로고
    • Genomic structure and transcriptional regulation of the penaeidin gene family from Litopenaeus vannamei
    • O'Leary N.A., and Gross P.S. Genomic structure and transcriptional regulation of the penaeidin gene family from Litopenaeus vannamei. Gene 371 (2006) 75-83
    • (2006) Gene , vol.371 , pp. 75-83
    • O'Leary, N.A.1    Gross, P.S.2
  • 19
    • 9944233151 scopus 로고    scopus 로고
    • Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach
    • Supungul P., Klinbunga S., Pichyangkura R., Hirono I., Aoki T., and Tassanakajon A. Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach. Dis Aquat Org 61 (2004) 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
  • 20
    • 33750965196 scopus 로고    scopus 로고
    • Penaeus monodon gene discovery project: the generation of an EST collection and establishment of a database
    • Tassanakajon A., Klinbunga S., Paunglarp N., Rimphanitchayakit V., Udomkit A., Jitrapakdee S., et al. Penaeus monodon gene discovery project: the generation of an EST collection and establishment of a database. Gene 384 (2006) 104-112
    • (2006) Gene , vol.384 , pp. 104-112
    • Tassanakajon, A.1    Klinbunga, S.2    Paunglarp, N.3    Rimphanitchayakit, V.4    Udomkit, A.5    Jitrapakdee, S.6
  • 21
    • 0034740227 scopus 로고    scopus 로고
    • Application of a time-delay neural network to promoter annotation in the Drosophila melanogaster genome
    • Reese M.G. Application of a time-delay neural network to promoter annotation in the Drosophila melanogaster genome. Comput Chem 26 (2001) 51-56
    • (2001) Comput Chem , vol.26 , pp. 51-56
    • Reese, M.G.1
  • 22
    • 0023651307 scopus 로고
    • RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression
    • Shapiro M.B., and Senapathy P. RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression. Nucleic Acids Res 15 (1987) 7155-7174
    • (1987) Nucleic Acids Res , vol.15 , pp. 7155-7174
    • Shapiro, M.B.1    Senapathy, P.2
  • 24
    • 0028876679 scopus 로고
    • Aberrant splicing and transcription termination caused by P element insertion into the intron of a Drosophila gene
    • Horowitz H., and Berg C.A. Aberrant splicing and transcription termination caused by P element insertion into the intron of a Drosophila gene. Genetics 139 (1995) 327
    • (1995) Genetics , vol.139 , pp. 327
    • Horowitz, H.1    Berg, C.A.2
  • 25
    • 7444220147 scopus 로고    scopus 로고
    • Aberrant and alternative splicing in cancer
    • Venables J.P. Aberrant and alternative splicing in cancer. Cancer Res 64 (2004) 7647-7654
    • (2004) Cancer Res , vol.64 , pp. 7647-7654
    • Venables, J.P.1
  • 26
    • 0036494674 scopus 로고    scopus 로고
    • Aberrant splicing in several human tumors in the tumor suppressor genes Neurofibromatosis Type 1, Neurofibromatosis Type 2, Tuberous Sclerosis 2
    • Kaufmann D., Leistner W., Kruse P., Kenner O., Hoffmeyer S., Hein C., et al. Aberrant splicing in several human tumors in the tumor suppressor genes Neurofibromatosis Type 1, Neurofibromatosis Type 2, Tuberous Sclerosis 2. Cancer Res 62 (2002) 1503-1509
    • (2002) Cancer Res , vol.62 , pp. 1503-1509
    • Kaufmann, D.1    Leistner, W.2    Kruse, P.3    Kenner, O.4    Hoffmeyer, S.5    Hein, C.6
  • 27
    • 4544228457 scopus 로고    scopus 로고
    • Functions of NF-kappaB1 and NF-kappaB2 in immune cell biology
    • Beinke S., and Ley S.C. Functions of NF-kappaB1 and NF-kappaB2 in immune cell biology. Biochem J 382 (2004) 393-409
    • (2004) Biochem J , vol.382 , pp. 393-409
    • Beinke, S.1    Ley, S.C.2
  • 28
    • 0036142740 scopus 로고    scopus 로고
    • NF-kappa B-mediated transcriptional regulation of human beta-defensin-2 gene following lipopolysaccharide stimulation
    • Tsutsumi-Ishii Y., and Nagaoka I. NF-kappa B-mediated transcriptional regulation of human beta-defensin-2 gene following lipopolysaccharide stimulation. J Leukoc Biol 71 (2002) 154-162
    • (2002) J Leukoc Biol , vol.71 , pp. 154-162
    • Tsutsumi-Ishii, Y.1    Nagaoka, I.2
  • 29
    • 20544438245 scopus 로고    scopus 로고
    • Transcriptional regulation of beta-defensin-2 by lipopolysaccharide in cultured human cervical carcinoma (HeLa) cells
    • Mineshiba J., Myokai F., Mineshiba F., Matsuura K., Nishimura F., and Takashiba S. Transcriptional regulation of beta-defensin-2 by lipopolysaccharide in cultured human cervical carcinoma (HeLa) cells. FEMS Immunol Med Microbiol 45 (2005) 37-44
    • (2005) FEMS Immunol Med Microbiol , vol.45 , pp. 37-44
    • Mineshiba, J.1    Myokai, F.2    Mineshiba, F.3    Matsuura, K.4    Nishimura, F.5    Takashiba, S.6
  • 30
    • 0034830455 scopus 로고    scopus 로고
    • Involvement of Rel factors in the expression of antimicrobial peptide genes in amphibia
    • Miele R., Bjorklund G., Barra D., Simmaco M., and Engstrom Y. Involvement of Rel factors in the expression of antimicrobial peptide genes in amphibia. Eur J Biochem 268 (2001) 443-449
    • (2001) Eur J Biochem , vol.268 , pp. 443-449
    • Miele, R.1    Bjorklund, G.2    Barra, D.3    Simmaco, M.4    Engstrom, Y.5
  • 32
    • 0027402290 scopus 로고
    • Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila
    • Kappler C., Meister M., Lagueux M., Gateff E., Hoffmann J.A., and Reichhart J.M. Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila. EMBO J 12 (1993) 1561-1568
    • (1993) EMBO J , vol.12 , pp. 1561-1568
    • Kappler, C.1    Meister, M.2    Lagueux, M.3    Gateff, E.4    Hoffmann, J.A.5    Reichhart, J.M.6
  • 33
    • 0026557911 scopus 로고
    • Insect immunity: developmental and inducible activity of the Drosophila diptericin promoter
    • Reichhart J.M., Meister M., Dimarcq J.L., Zachary D., Hoffmann D., Ruiz C., et al. Insect immunity: developmental and inducible activity of the Drosophila diptericin promoter. EMBO J 11 (1992) 1469-1477
    • (1992) EMBO J , vol.11 , pp. 1469-1477
    • Reichhart, J.M.1    Meister, M.2    Dimarcq, J.L.3    Zachary, D.4    Hoffmann, D.5    Ruiz, C.6
  • 34
    • 0028559509 scopus 로고
    • Insect immunity. A transgenic analysis in Drosophila defines several functional domains in the diptericin promoter
    • Meister M., Braun A., Kappler C., Reichhart J.M., and Hoffmann J.A. Insect immunity. A transgenic analysis in Drosophila defines several functional domains in the diptericin promoter. EMBO J 13 (1994) 5958-5966
    • (1994) EMBO J , vol.13 , pp. 5958-5966
    • Meister, M.1    Braun, A.2    Kappler, C.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 36
    • 0141447390 scopus 로고    scopus 로고
    • Identification, structure and differential expression of novel pleurocidins clustered on the genome of the winter flounder, Pseudopleuronectes americanus (Walbaum)
    • Douglas S.E., Patrzykat A., Pytyck J., and Gallant J.W. Identification, structure and differential expression of novel pleurocidins clustered on the genome of the winter flounder, Pseudopleuronectes americanus (Walbaum). Eur J Biochem 270 (2003) 3720-3730
    • (2003) Eur J Biochem , vol.270 , pp. 3720-3730
    • Douglas, S.E.1    Patrzykat, A.2    Pytyck, J.3    Gallant, J.W.4
  • 37
    • 0027360443 scopus 로고
    • Virus-mediated induction of interferon A gene requires cooperation between multiple binding factors in the interferon alpha promoter region
    • Au W.C., Su Y., Raj N.B., and Pitha P.M. Virus-mediated induction of interferon A gene requires cooperation between multiple binding factors in the interferon alpha promoter region. J Biol Chem 268 (1993) 24032-24040
    • (1993) J Biol Chem , vol.268 , pp. 24032-24040
    • Au, W.C.1    Su, Y.2    Raj, N.B.3    Pitha, P.M.4
  • 38
    • 0028917210 scopus 로고
    • Drosophila immunity. A sequence homologous to mammalian interferon consensus response element enhances the activity of the diptericin promoter
    • Georgel P., Kappler C., Langley E., Gross I., Nicolas E., Reichhart J.M., et al. Drosophila immunity. A sequence homologous to mammalian interferon consensus response element enhances the activity of the diptericin promoter. Nucleic Acids Res 23 (1995) 1140-1145
    • (1995) Nucleic Acids Res , vol.23 , pp. 1140-1145
    • Georgel, P.1    Kappler, C.2    Langley, E.3    Gross, I.4    Nicolas, E.5    Reichhart, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.