메뉴 건너뛰기




Volumn 8, Issue 7, 2013, Pages

Functional Divergence in Shrimp Anti-Lipopolysaccharide Factors (ALFs): From Recognition of Cell Wall Components to Antimicrobial Activity

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; ANTILIPOPOLYSACCHARIDE FACTOR; LIPOPOLYSACCHARIDE; POLYPEPTIDE; UNCLASSIFIED DRUG;

EID: 84879834447     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0067937     Document Type: Article
Times cited : (76)

References (47)
  • 1
    • 34250861495 scopus 로고    scopus 로고
    • In vitro antiviral activity of antimicrobial peptides against herpes simplex virus 1, adenovirus, and rotavirus
    • Carriel-Gomes MC, Kratz JM, Barracco MA, Bachère E, Barardi CR, et al. (2007) In vitro antiviral activity of antimicrobial peptides against herpes simplex virus 1, adenovirus, and rotavirus. Mem Inst Oswaldo Cruz 102: 469-472.
    • (2007) Mem Inst Oswaldo Cruz , vol.102 , pp. 469-472
    • Carriel-Gomes, M.C.1    Kratz, J.M.2    Barracco, M.A.3    Bachère, E.4    Barardi, C.R.5
  • 2
    • 84862777384 scopus 로고    scopus 로고
    • A new anti-lipopolysaccharide factor isoform (PtALF4) from the swimming crab Portunus trituberculatus exhibited structural and functional diversity of ALFs
    • Liu Y, Cui Z, Li X, Song C, Li Q, et al. (2012) A new anti-lipopolysaccharide factor isoform (PtALF4) from the swimming crab Portunus trituberculatus exhibited structural and functional diversity of ALFs. Fish & shellfish immunology 32: 724-731.
    • (2012) Fish & Shellfish Immunology , vol.32 , pp. 724-731
    • Liu, Y.1    Cui, Z.2    Li, X.3    Song, C.4    Li, Q.5
  • 3
    • 0021799698 scopus 로고
    • Isolation and biological activities of Limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharides (LPS)
    • Morita T, Ohtsubo S, Nakamura T, Tanaka S, Iwanaga S, et al. (1985) Isolation and biological activities of Limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharides (LPS). J Biochem 97: 1611-1620.
    • (1985) J Biochem , vol.97 , pp. 1611-1620
    • Morita, T.1    Ohtsubo, S.2    Nakamura, T.3    Tanaka, S.4    Iwanaga, S.5
  • 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, et al. (2005) Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon. Developmental and comparative immunology 29: 841-851.
    • (2005) Developmental and Comparative Immunology , vol.29 , pp. 841-851
    • Somboonwiwat, K.1    Marcos, M.2    Tassanakajon, A.3    Klinbunga, S.4    Aumelas, A.5
  • 5
    • 67650376043 scopus 로고    scopus 로고
    • Identification, cloning, characterization and recombinant expression of an anti-lipopolysaccharide factor from the hemocytes of Indian mud crab, Scylla serrata
    • Yedery RD, Reddy KV, (2009) Identification, cloning, characterization and recombinant expression of an anti-lipopolysaccharide factor from the hemocytes of Indian mud crab, Scylla serrata. Fish & shellfish immunology 27: 275-284.
    • (2009) Fish & Shellfish Immunology , vol.27 , pp. 275-284
    • Yedery, R.D.1    Reddy, K.V.2
  • 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, Iwanaga S, (1982) Limulus anti-LPS factor: an anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system. Biochemical and biophysical research communications 105: 717-723.
    • (1982) Biochemical and Biophysical Research Communications , vol.105 , pp. 717-723
    • Tanaka, S.1    Nakamura, T.2    Morita, T.3    Iwanaga, S.4
  • 7
    • 44749090947 scopus 로고    scopus 로고
    • A relationship between antimicrobial peptide gene expression and capacity of a selected shrimp line to survive a Vibrio infection
    • de Lorgeril J, Gueguen Y, Goarant C, Goyard E, Mugnier C, et al. (2008) A relationship between antimicrobial peptide gene expression and capacity of a selected shrimp line to survive a Vibrio infection. Molecular immunology 45: 3438-3445.
    • (2008) Molecular Immunology , vol.45 , pp. 3438-3445
    • de Lorgeril, J.1    Gueguen, Y.2    Goarant, C.3    Goyard, E.4    Mugnier, C.5
  • 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 PS, Bartlett TC, Browdy CL, Chapman RW, Warr GW, (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) 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
    • 0036755716 scopus 로고    scopus 로고
    • Identification of immune-related genes in hemocytes of black tiger shrimp (Penaeus monodon)
    • Supungul P, Klinbunga S, Pichyangkura R, Jitrapakdee S, Hirono I, et al. (2002) Identification of immune-related genes in hemocytes of black tiger shrimp (Penaeus monodon). Mar Biotechnol 4: 487-494.
    • (2002) Mar Biotechnol , vol.4 , pp. 487-494
    • Supungul, P.1    Klinbunga, S.2    Pichyangkura, R.3    Jitrapakdee, S.4    Hirono, I.5
  • 10
    • 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 GR, Liddington R, (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
  • 11
    • 65249136556 scopus 로고    scopus 로고
    • NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: model of the possible lipid A-binding site
    • Yang Y, Boze H, Chemardin P, Padilla A, Moulin G, et al. (2009) NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: model of the possible lipid A-binding site. Biopolymers 91: 207-220.
    • (2009) Biopolymers , vol.91 , pp. 207-220
    • Yang, Y.1    Boze, H.2    Chemardin, P.3    Padilla, A.4    Moulin, G.5
  • 12
    • 79960901109 scopus 로고    scopus 로고
    • Antimicrobial peptides in crustaceans
    • Rosa RD, Barracco MA, (2010) Antimicrobial peptides in crustaceans. Inv Surv J 7: 262-284.
    • (2010) Inv Surv J , vol.7 , pp. 262-284
    • Rosa, R.D.1    Barracco, M.A.2
  • 14
    • 84859232975 scopus 로고    scopus 로고
    • Gene silencing reveals a crucial role for anti-lipopolysaccharide factors from Penaeus monodon in the protection against microbial infections
    • Ponprateep S, Tharntada S, Somboonwiwat K, Tassanakajon A, (2012) Gene silencing reveals a crucial role for anti-lipopolysaccharide factors from Penaeus monodon in the protection against microbial infections. Fish & shellfish immunology 32: 26-34.
    • (2012) Fish & Shellfish Immunology , vol.32 , pp. 26-34
    • Ponprateep, S.1    Tharntada, S.2    Somboonwiwat, K.3    Tassanakajon, A.4
  • 15
    • 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, et al. (2004) Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach. Dis Aquat Organ 61: 123-135.
    • (2004) Dis Aquat Organ , vol.61 , pp. 123-135
    • Supungul, P.1    Klinbunga, S.2    Pichyangkura, R.3    Hirono, I.4    Aoki, T.5
  • 16
    • 38349193705 scopus 로고    scopus 로고
    • Anti-lipopolysaccharide factors from the black tiger shrimp, Penaeus monodon, are encoded by two genomic loci
    • Tharntada S, Somboonwiwat K, Rimphanitchayakit V, Tassanakajon A, (2008) Anti-lipopolysaccharide factors from the black tiger shrimp, Penaeus monodon, are encoded by two genomic loci. Fish Shellfish Immunol 24: 46-54.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 46-54
    • Tharntada, S.1    Somboonwiwat, K.2    Rimphanitchayakit, V.3    Tassanakajon, A.4
  • 17
    • 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, Xiang J, (2005) Molecular cloning and expression profile of putative antilipopolysaccharide factor in Chinese shrimp (Fenneropenaeus chinensis). Mar Biotechnol (NY) 7: 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
  • 18
    • 72149103004 scopus 로고    scopus 로고
    • Molecular cloning and transcriptional analysis of a newly identified anti-lipopolysaccharide factor gene in kuruma shrimp, Marsupenaeus japonicus
    • Mekata T, Sudhakaran R, Okugawa S, Kono T, Sakai M, et al. (2010) Molecular cloning and transcriptional analysis of a newly identified anti-lipopolysaccharide factor gene in kuruma shrimp, Marsupenaeus japonicus. Letters in applied microbiology 50: 112-119.
    • (2010) Letters in Applied Microbiology , vol.50 , pp. 112-119
    • Mekata, T.1    Sudhakaran, R.2    Okugawa, S.3    Kono, T.4    Sakai, M.5
  • 19
    • 46549083956 scopus 로고    scopus 로고
    • Localization of anti-lipopolysaccharide factor (ALFPm3) in tissues of the black tiger shrimp, Penaeus monodon, and characterization of its binding properties
    • Somboonwiwat K, Bachère E, Rimphanitchayakit V, Tassanakajon A, (2008) Localization of anti-lipopolysaccharide factor (ALFPm3) in tissues of the black tiger shrimp, Penaeus monodon, and characterization of its binding properties. Developmental and comparative immunology 32: 1170-1176.
    • (2008) Developmental and Comparative Immunology , vol.32 , pp. 1170-1176
    • Somboonwiwat, K.1    Bachère, E.2    Rimphanitchayakit, V.3    Tassanakajon, A.4
  • 20
    • 77950515754 scopus 로고    scopus 로고
    • NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization
    • Bhunia A, Domadia PN, Torres J, Hallock KJ, Ramamoorthy A, et al. (2010) NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization. J Biol Chem 285: 3883-3895.
    • (2010) J Biol Chem , vol.285 , pp. 3883-3895
    • Bhunia, A.1    Domadia, P.N.2    Torres, J.3    Hallock, K.J.4    Ramamoorthy, A.5
  • 21
    • 79959903251 scopus 로고    scopus 로고
    • NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity
    • Bhunia A, Saravanan R, Mohanram H, Mangoni ML, Bhattacharjya S, (2011) NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity. J Biol Chem 286: 24394-24406.
    • (2011) J Biol Chem , vol.286 , pp. 24394-24406
    • Bhunia, A.1    Saravanan, R.2    Mohanram, H.3    Mangoni, M.L.4    Bhattacharjya, S.5
  • 22
    • 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, et al. (2006) Cloning and characterization of a LPS-regulatory gene having an LPS binding domain in kuruma prawn Marsupenaeus japonicus. Molecular immunology 43: 2061-2069.
    • (2006) Molecular Immunology , vol.43 , pp. 2061-2069
    • Nagoshi, H.1    Inagawa, H.2    Morii, K.3    Harada, H.4    Kohchi, C.5
  • 23
    • 50449111197 scopus 로고    scopus 로고
    • Bioactive peptides derived from the Limulus anti-lipopolysaccharide factor: structure-activity relationships and formation of mixed peptide/lipid complexes
    • Mora P, De La Paz ML, Pérez-Payá E, (2008) Bioactive peptides derived from the Limulus anti-lipopolysaccharide factor: structure-activity relationships and formation of mixed peptide/lipid complexes. J Pept Sci 14: 963-971.
    • (2008) J Pept Sci , vol.14 , pp. 963-971
    • Mora, P.1    De La Paz, M.L.2    Pérez-Payá, E.3
  • 24
    • 34548178989 scopus 로고    scopus 로고
    • Mechanism of interaction of optimized Limulus-derived cyclic peptides with endotoxins: thermodynamic, biophysical and microbiological analysis
    • Andrä J, Howe J, Garidel P, Rössle M, Richter W, et al. (2007) Mechanism of interaction of optimized Limulus-derived cyclic peptides with endotoxins: thermodynamic, biophysical and microbiological analysis. Biochem J 406: 297-307.
    • (2007) Biochem J , vol.406 , pp. 297-307
    • Andrä, J.1    Howe, J.2    Garidel, P.3    Rössle, M.4    Richter, W.5
  • 25
    • 39149087407 scopus 로고    scopus 로고
    • Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF): a broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection
    • de la Vega E, O'Leary NA, Shockey JE, Robalino J, Payne C, et al. (2008) Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF): a broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection. Molecular immunology 45: 1916-1925.
    • (2008) Molecular Immunology , vol.45 , pp. 1916-1925
    • de la Vega, E.1    O'Leary, N.A.2    Shockey, J.E.3    Robalino, J.4    Payne, C.5
  • 26
    • 67649197704 scopus 로고    scopus 로고
    • Role of anti-lipopolysaccharide factor from the black tiger shrimp, Penaeus monodon, in protection from white spot syndrome virus infection
    • Tharntada S, Ponprateep S, Somboonwiwat K, Liu H, Soderhall I, et al. (2009) Role of anti-lipopolysaccharide factor from the black tiger shrimp, Penaeus monodon, in protection from white spot syndrome virus infection. J Gen Virol 90: 1491-1498.
    • (2009) J Gen Virol , vol.90 , pp. 1491-1498
    • Tharntada, S.1    Ponprateep, S.2    Somboonwiwat, K.3    Liu, H.4    Soderhall, I.5
  • 27
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S, (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 24: 1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 28
    • 33644852494 scopus 로고    scopus 로고
    • Characterization of a defensin from the oyster Crassostrea gigas. Recombinant production, folding, solution structure, antimicrobial activities, and gene expression
    • Gueguen Y, Herpin A, Aumelas A, Garnier J, Fievet J, et al. (2006) Characterization of a defensin from the oyster Crassostrea gigas. Recombinant production, folding, solution structure, antimicrobial activities, and gene expression. J Biol Chem 281: 313-323.
    • (2006) J Biol Chem , vol.281 , pp. 313-323
    • Gueguen, Y.1    Herpin, A.2    Aumelas, A.3    Garnier, J.4    Fievet, J.5
  • 29
    • 77956547991 scopus 로고    scopus 로고
    • Insight into invertebrate defensin mechanism of action: oyster defensins inhibit peptidoglycan biosynthesis by binding to lipid II
    • Schmitt P, Wilmes M, Pugnière M, Aumelas A, Bachère E, et al. (2010) Insight into invertebrate defensin mechanism of action: oyster defensins inhibit peptidoglycan biosynthesis by binding to lipid II. J Biol Chem 285: 29208-29216.
    • (2010) J Biol Chem , vol.285 , pp. 29208-29216
    • Schmitt, P.1    Wilmes, M.2    Pugnière, M.3    Aumelas, A.4    Bachère, E.5
  • 30
    • 0030632142 scopus 로고    scopus 로고
    • Strategies for the isolation and characterization of antimicrobial peptides of invertebrates
    • Hetru C, Bulet P, (1997) Strategies for the isolation and characterization of antimicrobial peptides of invertebrates. Methods Mol Biol 78: 35-49.
    • (1997) Methods Mol Biol , vol.78 , pp. 35-49
    • Hetru, C.1    Bulet, P.2
  • 31
    • 84861223473 scopus 로고    scopus 로고
    • Evidence for a novel biological role for the multifunctional beta-1,3-glucan binding protein in shrimp
    • Goncalves P, Vernal J, Rosa RD, Yepiz-Plascencia G, de Souza CR, et al. (2012) Evidence for a novel biological role for the multifunctional beta-1,3-glucan binding protein in shrimp. Molecular immunology 51: 363-367.
    • (2012) Molecular Immunology , vol.51 , pp. 363-367
    • Goncalves, P.1    Vernal, J.2    Rosa, R.D.3    Yepiz-Plascencia, G.4    de Souza, C.R.5
  • 32
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT Method
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT Method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 33
    • 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, et al. (2004) Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach. Dis Aquat Organ 61: 123-135.
    • (2004) Dis Aquat Organ , vol.61 , pp. 123-135
    • Supungul, P.1    Klinbunga, S.2    Pichyangkura, R.3    Hirono, I.4    Aoki, T.5
  • 34
    • 34247325507 scopus 로고    scopus 로고
    • A male-specific expression gene, encodes a novel anionic antimicrobial peptide, scygonadin, in Scylla serrata
    • Wang KJ, Huang WS, Yang M, Chen HY, Bo J, et al. (2007) A male-specific expression gene, encodes a novel anionic antimicrobial peptide, scygonadin, in Scylla serrata. Molecular immunology 44: 1961-1968.
    • (2007) Molecular Immunology , vol.44 , pp. 1961-1968
    • Wang, K.J.1    Huang, W.S.2    Yang, M.3    Chen, H.Y.4    Bo, J.5
  • 35
    • 27644520345 scopus 로고    scopus 로고
    • PenBase, the shrimp antimicrobial peptide penaeidin database: sequence-based classification and recommended nomenclature
    • Gueguen Y, Garnier J, Robert L, Lefranc MP, Mougenot I, et al. (2006) PenBase, the shrimp antimicrobial peptide penaeidin database: sequence-based classification and recommended nomenclature. Developmental and comparative immunology 30: 283-288.
    • (2006) Developmental and Comparative Immunology , vol.30 , pp. 283-288
    • Gueguen, Y.1    Garnier, J.2    Robert, L.3    Lefranc, M.P.4    Mougenot, I.5
  • 36
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY, (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55: 27-55.
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 37
    • 33645233336 scopus 로고    scopus 로고
    • Genomic structure and transcriptional regulation of the penaeidin gene family from Litopenaeus vannamei
    • O'Leary NA, Gross PS, (2006) Genomic structure and transcriptional regulation of the penaeidin gene family from Litopenaeus vannamei. Gene 371: 75-83.
    • (2006) Gene , vol.371 , pp. 75-83
    • O'Leary, N.A.1    Gross, P.S.2
  • 39
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense
    • Lai Y, Gallo RL, (2009) AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol 30: 131-141.
    • (2009) Trends Immunol , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 40
    • 0032734313 scopus 로고    scopus 로고
    • Expression and regulation of the human beta-defensins hBD-1 and hBD-2 in intestinal epithelium
    • O'Neil DA, Porter EM, Elewaut D, Anderson GM, Eckmann L, et al. (1999) Expression and regulation of the human beta-defensins hBD-1 and hBD-2 in intestinal epithelium. J Immunol 163: 6718-6724.
    • (1999) J Immunol , vol.163 , pp. 6718-6724
    • O'Neil, D.A.1    Porter, E.M.2    Elewaut, D.3    Anderson, G.M.4    Eckmann, L.5
  • 41
    • 80053261618 scopus 로고    scopus 로고
    • Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas
    • Rosa RD, Santini A, Fievet J, Bulet P, Destoumieux-Garzón D, et al. (2011) Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas. PLoS ONE 6: e25594.
    • (2011) PLoS ONE , vol.6
    • Rosa, R.D.1    Santini, A.2    Fievet, J.3    Bulet, P.4    Destoumieux-Garzón, D.5
  • 44
    • 84864285600 scopus 로고    scopus 로고
    • A mini review on the antimicrobial peptides isolated from the genus Hylarana (Amphibia: Anura) with a proposed nomenclature for amphibian skin peptides
    • Thomas P, Kumar TV, Reshmy V, Kumar KS, George S, (2012) A mini review on the antimicrobial peptides isolated from the genus Hylarana (Amphibia: Anura) with a proposed nomenclature for amphibian skin peptides. Mol Biol Rep 39: 6943-6947.
    • (2012) Mol Biol Rep , vol.39 , pp. 6943-6947
    • Thomas, P.1    Kumar, T.V.2    Reshmy, V.3    Kumar, K.S.4    George, S.5
  • 45
    • 38349033560 scopus 로고    scopus 로고
    • Isoforms of Litopenaeus vannamei anti-lipopolysaccharide and its expression by bacterial challenge
    • Jiménez-Vega F, Vargas-Albores F, (2007) Isoforms of Litopenaeus vannamei anti-lipopolysaccharide and its expression by bacterial challenge. J Shell Res 26: 1169-1175.
    • (2007) J Shell Res , vol.26 , pp. 1169-1175
    • Jiménez-Vega, F.1    Vargas-Albores, F.2
  • 46
    • 84925034478 scopus 로고    scopus 로고
    • Cloning and characterisation of cDNA sequences encoding for anti-lipopolysaccharide factors (ALFs) in Brazilian palaemonid and penaeid shrimps
    • Rosa RD, Stoco PH, Barracco MA, (2008) Cloning and characterisation of cDNA sequences encoding for anti-lipopolysaccharide factors (ALFs) in Brazilian palaemonid and penaeid shrimps. Fish & shellfish immunology 25: 693-696.
    • (2008) Fish & Shellfish Immunology , vol.25 , pp. 693-696
    • Rosa, R.D.1    Stoco, P.H.2    Barracco, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.