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| Prediction of Functional Domain of Effector Protein of Type ⅢSecretion System in Pathogen Edwardsiella tarda |
| WANG Bin,LI Jun-wei,ZHAO Feng-mei,WANG Hui,HU Liang,JIANG Zhi-qiang |
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Abstract The PCR was performed to detect the T TSS genes eseB ,eseC ,and eseD in pathogen Edw ard-siella tarda L-49231 strain isolated from turbot Scophthalmus maximus infected with septicaemia hemor-rhage .The PCR products were cloned into vector PMD19-T and the positive clones were sequenced .The results showed that the fragments were composed of 594 bp in eseB ,934 bp in eseC ,and 445 bp in eseD , showing 100% ,100% ,and 99% homology separately compared to E . tarda PPD FL6-60 in GenBank . Thereby ,the E . tarda L-49231 strain contained the T TSS effector genes eseB ,eseC ,and ese D .The molecular weight , amino acid composition , hydrophobicity , transmembrane structure and the signal peptide of eseB ,eseC and eseD were predicted by bioinformatics .The eseB was found to be 21 732 .26 u , with the maximal level of aspartic acid , representing 10 .61% of the total amino acids . The eseC had molecular weight of 53 606 .08 u ,with maximal level of alanine ,accounting for 14 .43% of the total amino acids .The eseD showed the molecular weight of 21 112 .43 u ,glutamine being the maximum ,representing 11 .04% of the total amino acids .In addition ,all of the three proteins contained much glycin ,alanine and leucine but a little cysteine and tryptophan . The eseB ,eseC and eseD were all found to be hydrophilic proteins ,without transmembrane structure in the eseB . There was three transmembrane structures at 192 ~ 210 aa ,213 ~ 233 aa and 63 ~ 284 aa domain in eseC .The eseD contained a transmembrane structure at 90 ~ 106 aa domain .There was no signal peptide in all of the three proteins .
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Received: 25 July 2013
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