title: Comparative transcriptional analysis reveals distinct expression patterns of channel catfish genes after the first infection and re-infection with Aeromonas hydrophila.
abstract: To determine whether transcriptional levels of channel catfish (Ictalurus punctatus) genes are differentially regulated between a first infection with Aeromonas hydrophila and a re-infection, suppression subtractive hybridization (SSH) was performed in this study using anterior kidney cDNA after the re-infection as tester. Of the 96 clones isolated from the SSH library, 28 unique expressed sequence tags (ESTs) were obtained, of which eight were confirmed to be slightly but significantly (P < 0.05) more up-regulated by the re-infection at 6 h post infection (hpi). Expression kinetics studies at 3, 6, 12, 24, and 48 hpi revealed that the eight ESTs were significantly (P = 0.016) more up-regulated by the first infection, with a major peak at 3 hpi. A total of 96 genes reported in literature to be up-regulated by bacterial infections were selected and subjected to expression analysis at 3 hpi. Of the 96 selected genes, 19 were found to be significantly (P < 0.05) induced by A. hydrophila after the first infection and the re-infection. The 19 genes belonged to the following five main categories: 1) toll-like receptor (TLR2, TLR3, TLR5, TLR21); 2) antimicrobial peptide (NK-lysin type 1, NK-lysin type 2, NK-lysin type 3, cathepsin D, transferrin, hepcidin); 3) cytokine or chemokine (interleukin-1β, interleukin-10, tumor necrosis factor α, chemokine CXCL-10); 4) signaling proteins (cadherin EGF LAG seven-pass G-type receptor 1, very large inducible GTPase 1, arginine deiminase type 2, lymphokine-activated killer T-cell originated protein kinase); 5) lysozyme (lysozyme c). Overall, the total 27 genes (8 ESTs plus the 19 selected genes) were significantly (P < 0.001) more induced by the first infection. Peaked expression of lysozyme c and serum lysozyme activity after the first infection were seen at 24 hpi, whereas that after the re-infection were seen at 12 hpi, suggesting that both innate and adaptive immunity were involved in the defense against the re-infection of A. hydrophila.
authors.affiliation: Aquatic Animal Health Research Unit, USDA-ARS, 990 Wire Road, Auburn, AL 36832, USA.
authors.forename: Xingjiang
authors.initials: X
authors.lastname: Mu
authors.forename: Julia W
authors.initials: JW
authors.lastname: Pridgeon
authors.forename: Phillip H
authors.initials: PH
authors.lastname: Klesius
mesh_terms: D016980:Aeromonas hydrophila; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000378:metabolism; D001483:Base Sequence; D016207:Cytokines / Q000378:metabolism; D017931:DNA Primers / Q000235:genetics; D020224:Expressed Sequence Tags / Q000378:metabolism; D005393:Fish Diseases / Q000378:metabolism* / Q000382:microbiology*; D020869:Gene Expression Profiling / Q000662:veterinary; D005786:Gene Expression Regulation / Q000276:immunology*; D015723:Gene Library; D016905:Gram-Negative Bacterial Infections / Q000378:metabolism / Q000662:veterinary*; D007059:Ictaluridae / Q000235:genetics* / Q000276:immunology* / Q000378:metabolism; D008969:Molecular Sequence Data; D009113:Muramidase / Q000378:metabolism; D017422:Sequence Analysis, DNA; D018709:Statistics, Nonparametric; D051193:Toll-Like Receptors / Q000378:metabolism
chemical_list: D023181:Antimicrobial Cationic Peptides; D016207:Cytokines; D017931:DNA Primers; D051193:Toll-Like Receptors; D009113:Muramidase
keywords: Adaptive immunity; Aeromonas hydrophila; Ictalurus punctatus; Innate immunity; Transcription
references.citation: Fish Physiol Biochem. 2009 Nov;35(4):677-82
references.pmid: 19449165
references.citation: Cytokine Growth Factor Rev. 2002 Dec;13(6):483-502
references.pmid: 12401481
references.citation: Dev Comp Immunol. 2002 Jun;26(5):445-59
references.pmid: 11906724
references.citation: Vet Immunol Immunopathol. 2012 Jun 30;147(3-4):170-9
references.pmid: 22578983
references.citation: Vet Immunol Immunopathol. 2010 Apr 15;134(3-4):184-98
references.pmid: 19800135
references.citation: Fish Shellfish Immunol. 2011 Dec;31(6):1162-72
references.pmid: 22019831
references.citation: Mol Mar Biol Biotechnol. 1998 Sep;7(3):232-9
references.pmid: 9701618
references.citation: Adv Immunol. 1996;63:377-454
references.pmid: 8787635
references.citation: J Fish Dis. 2003 Feb;26(2):117-20
references.pmid: 12962220
references.citation: Fish Shellfish Immunol. 2011 Oct;31(4):564-70
references.pmid: 21767651
references.citation: J Biol Chem. 2003 Nov 21;278(47):46307-20
references.pmid: 12923194
references.citation: Immunity. 2012 Jan 27;36(1):23-31
references.pmid: 22244845
references.citation: Fish Shellfish Immunol. 2007 Dec;23(6):1218-30
references.pmid: 17981052
references.citation: Vet Immunol Immunopathol. 2010 Nov 15;138(1-2):25-33
references.pmid: 20630605
references.citation: Semin Immunol. 2007 Feb;19(1):24-32
references.pmid: 17275323
references.citation: mBio. 2010 Oct 26;1(5):
references.pmid: 20978541
references.citation: Innate Immun. 2013 Dec;19(6):644-54
references.pmid: 23548829
references.citation: Science. 2012 Dec 14;338(6113):1435-9
references.pmid: 23239728
references.citation: Dis Aquat Organ. 2011 May 9;94(3):249-53
references.pmid: 21790073
references.citation: Peptides. 2009 Apr;30(4):638-46
references.pmid: 19150638
references.citation: J Interferon Cytokine Res. 2002 Apr;22(4):413-9
references.pmid: 12034023
references.citation: Indian J Biochem Biophys. 2007 Oct;44(5):401-6
references.pmid: 18341217
references.citation: Dis Aquat Organ. 2001 Aug 22;46(1):23-9
references.pmid: 11592699
references.citation: Dev Comp Immunol. 2008;32(11):1301-12
references.pmid: 18538841
references.citation: Fish Shellfish Immunol. 2004 May;16(5):645-58
references.pmid: 15110338
references.citation: Indian J Biochem Biophys. 1972 Jun;9(2):162-5
references.pmid: 4661756
references.citation: Fish Shellfish Immunol. 2010 Feb;28(2):401-5
references.pmid: 19944172
references.citation: Dis Aquat Organ. 2009 Dec 22;88(1):45-54
references.pmid: 20183964
references.citation: J Fish Dis. 2012 Mar;35(3):227-37
references.pmid: 22324346
references.citation: Dis Aquat Organ. 2011 Jul 12;95(3):209-15
references.pmid: 21932532
references.citation: Nucleic Acids Res. 2001 May 1;29(9):e45
references.pmid: 11328886
references.citation: Fish Shellfish Immunol. 2009 Jan;26(1):140-5
references.pmid: 18817878
references.citation: Dev Comp Immunol. 2013 May;40(1):11-9
references.pmid: 23396098
references.citation: Trends Microbiol. 2000 Oct;8(10):452-6
references.pmid: 11044679
references.citation: J Exp Med. 1993 Sep 1;178(3):1041-8
references.pmid: 8102388
references.citation: Am J Physiol Lung Cell Mol Physiol. 2003 Oct;285(4):L862-8
references.pmid: 12909584
references.citation: J Fish Dis. 2010 Jun 1;33(6):497-505
references.pmid: 20384909
references.citation: FEMS Microbiol Lett. 1994 Mar 15;117(1):85-90
references.pmid: 7514147
references.citation: Dev Comp Immunol. 2009;33(1):35-45
references.pmid: 18760303
references.citation: Fish Shellfish Immunol. 2009 Sep;27(3):454-9
references.pmid: 19563896