Anti-lipopolysaccharide factors in the American lobster Homarus americanus: Molecular characterization and transcriptional response to Vibrio fluvialis challenge

Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics

Volumn 3, Issue 4, 2008, Pages 263-269

  Beale, K M ^a   Towle, D W ^a   Jayasundara, N ^a   Smith, C M ^a   Shields, J D ^b   Small, H J ^b   Greenwood, S J ^c  

^a MOUNT DESERT ISLAND BIOLOGICAL LABORATORY   (United States)

^b VIRGINIA INSTITUTE OF MARINE SCIENCE   (United States)

^c UNIVERSITY OF PRINCE EDWARD ISLAND   (Canada)

Author keywords

Antimicrobial peptides; Crustacean; DNA sequencing; Gill tissue; Hematopoetic tissue; Hepatopancreas tissue; Real time quantitative PCR

Indexed keywords

ANTI LIPOPOLYSACCHARIDE FACTOR; BLOOD CLOTTING FACTOR; COMPLEMENTARY DNA; CYSTEINE; DISULFIDE; MESSENGER RNA; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTHROPOD; ARTICLE; BACTERIAL IMMUNITY; BACTERIAL INFECTION; DISULFIDE BOND; DNA SEQUENCE; EXPRESSED SEQUENCE TAG; GENE LIBRARY; GENETIC REGULATION; GENETIC TRANSCRIPTION; GILL; HEMATOPOIETIC SYSTEM; HEPATOPANCREAS; INFECTION RESISTANCE; LIMULUS; LOBSTER; MOLECULAR CLONING; MOLECULAR MECHANICS; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PREDICTION; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; RNA SEQUENCE; VIBRIO FLUVIALIS;

ARTHROPODA; BACTERIA (MICROORGANISMS); CRUSTACEA; HOMARUS AMERICANUS; LIMULUS POLYPHEMUS; LOBSTER; MEROSTOMATA; VIBRIO; VIBRIO FLUVIALIS;

EID: 54449084865     PISSN: 1744117X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbd.2008.07.001     Document Type: Article

References (33)

1. Aketagawa J., Miyata T., Ohtsubo S., Nakamura T., Morita T., Hayashida H., Miyata T., Iwanaga S., Takao T., and Shimonishi Y. Primary structure of limulus anticoagulant anti-lipopolysaccharide factor. J. Biol. Chem. 261 (1986) 7357-7365
2. Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
3. Bendtsen J.D., Nielsen H., von Heijne G., and Brunak S. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340 (2004) 783-795
4. Burnett L.E., Holman J.D., Jorgensen D.D., Ikerd J.L., and Burnett K.G. Immune defense reduces respiratory fitness in Callinectes sapidus, the Atlantic blue crab. Biol. Bull. 211 (2006) 50-57
5. Bustin S.A., Benes V., Nolan T., and Pfaffl M.W. Quantitative real-time RT-PCR - a perspective. J. Mol. Endocrinol. 34 (2005) 597-601
6. Chaby R. Lipopolysaccharide-binding molecules: transporters, blockers and sensors. Cell. Mol. Life Sci. 61 (2004) 1697-1713
7. Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
8. Christie A.E., Rus S., Goiney C.C., Smith C.M., Towle D.W., and Dickinson P.S. Identification and characterization of a cDNA encoding a crustin-like, putative antibacterial protein from the American lobster Homarus americanus. Mol. Immunol. 44 (2007) 3333-3337
9. de la Vega E., O'Leary N.A., Shockey J.E., Robalino J., Payne C., Browdy C.L., Warr G.W., and Gross P.S. Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF): a broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection. Mol. Immunol. 45 (2008) 1916-1925
10. 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
11. 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
12. Iwanaga S., Kawabata S., and 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
13. Johansson M.W., Keyser P., Sritunyalucksana K., and Söderhäll K. Crustacean haemocytes and haematopoiesis. Aquaculture 191 (2000) 45-52
14. Kloczewiak M., Black K.M., Loiselle P., Cavaillon J.M., Wainwright N., and Warren H.S. Synthetic peptides that mimic the binding site of horseshoe crab antilipopolysaccharide factor. J. Infect. Dis. 170 (1994) 1490-1497
15. Kyte J., and Doolittle R.F. A simple method for displaying hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
16. 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. 7 (2005) 600-608
17. McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
18. Muta T., and Iwanaga S. The role of hemolymph coagulation in innate immunity. Curr. Opin. Immunol. 8 (1996) 41-47
19. Muta T., Miyata T., Tokunaga F., Nakamura T., and Iwanaga S. Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus. J. Biochem. 101 (1987) 1321-1330
20. Nicholas K.B., and Nicholas Jr. H.B. GeneDoc: a tool for editing and annotating multiple sequence alignments (1997). http://www.psc.edu/biomed/genedoc www.psc.edu/biomed/genedoc
21. Pan C.Y., Chao T.T., Chen J.C., Chen J.Y., Liu W.C., Lin C.H., and Kuo C.M. Shrimp (Penaeus monodon) anti-lipopolysaccharide factor reduces the lethality of Pseudomonas aeruginosa sepsis in mice. Int. Immunopharmacol. 7 (2007) 687-700
22. Robalino J., Almeida J.S., McKillen D., Colglazier J., Trent III H.F., Chen Y.A., Peck M.E., Browdy C.L., Chapman R.W., Warr G.W., and Gross P.S. Insights into the immune transcriptome of the shrimp Litopenaeus vannamei: tissue-specific expression profiles and transcriptomic responses to immune challenge. Physiol. Genomics 29 (2007) 44-56
23. Smolowitz R., Christoserdov A., and Hsu A. A description of the pathology of epizootic shell disease in the American lobster, Homarus americanus, H. Milne Edwards 1837. J. Shellfish Res. 24 (2005) 749-756
24. Söderhäll K., and Cerenius L. Crustacean immunity. Ann. Rev. Fish Dis. 2 (1992) 3-23
25. Somboonwiwat K., Marcos M., Tassanakajon A., Klinbunga S., Aumelas A., Romestand B., Gueguen Y., Boze H., Moulin G., and Bachere E. 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
26. Somboonwiwat K., Supungul P., Rimphanitchayakit V., Aoki T., Hirono I., and Tassanakajon A. Differentially expressed genes in hemocytes of Vibrio harveyi-challenged shrimp Penaeus monodon. J. Biochem. Mol. Biol. 39 (2006) 26-36
27. 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
28. Supungul P., Klinbunga S., Pichyangkura R., Jitrapakdee S., Hirono I., Aoki T., and Tassanakajon A. Identification of immune-related genes in hemocytes of black tiger shrimp (Penaeus monodon). Mar. Biotechnol. 4 (2002) 487-494
29. Tall B.D., Fall S., Pereira M.R., Ramos-Valle M., Curtis S.K., Kothary M.H., Chu D.M., Monday S.R., Kornegay L., Donkar T., Prince D., Thunberg R.L., Shangraw K.A., Hanes D.E., Khambaty F.M., Lampel K.A., Bier J.W., and Bayer R.C. Characterization of Vibrio fluvialis-like strains implicated in limp lobster disease. Appl. Environ. Microbiol. 69 (2003) 7435-7446
30. Tamura K., Dudley J., Nei M., and Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24 (2007) 1596-1599
31. Tassanakajon A., Klinbunga S., Paunglarp N., Rimphanitchayakit V., Udomkit A., Jitrapakdee S., Sritunyalucksana K., Phongdara A., Pongsomboon S., Supungul P., Tang S., Kuphanumart K., Pichyangkura R., and Lursinsap C. Penaeus monodon gene discovery project: the generation of an EST collection and establishment of a database. Gene 384 (2006) 104-112
32. Tharntada S., Somboonwiwat K., Rimphanitchayakit V., and Tassanakajon A. Anti-lipopolysaccharide factors from the black tiger shrimp, Penaeus monodon, are encoded by two genomic loci. Fish Shellfish Immunol. 24 (2008) 46-54
33. Towle D.W., and Smith C.M. Gene discovery in Carcinus maenas and Homarus americanus via expressed sequence tags. Integr. Comp. Biol. 46 (2006) 912-918