大丽轮枝菌（Verticillium dahliae VdLs.17）分泌组预测及分析

Abstract

【Objective】 The aim of this study was to predict and analyze secretome of Verticillium dahliae, an important soil-born fungal pathogen that causes vascular wilt diseases. 【Method】 The softwares SignalP, TargetP, TMHMM, Big-pi and PROSITE were used to predict the sectetome of V. dahliae. Protein databases were used for secretome annotation to find putative pectinase, cellulose and pathogen-host interaction proteins. The proteins with common fungal effector character were investigated by a set of computer algorithms. By using BLASTP, the secretome of V. dahliae and V. albo-atrum was compared to find V. dahliae specifically secreted proteins. 【Result】 A total of 922 possible secreted proteins were identified in V. dahliae scretome. The most frequent amino acid in signal peptides is alanine, and the least is glutamic acid and aspartic acid. The amino acid in the position-3 and-1 are very conserved. The secretome is equipped with 158 carbohydrate-active enzymes which include 10 pectic hydrolases and 14 pectic lyases, 190 putative pathogen-host interaction proteins, 97 RxLx motif containing proteins and 52 small cysteine-rich secreted proteins, and 58 V. dahliae specifically secreted proteins compared with V. albo-atrum. 【Conclusion】 This study has provided secretome prediction algorithms for V. dahliae. Length of signal peptides vary greatly. Composition of signal peptides are mainly aliphatic amino acid and sequences of signal peptides near C-terminal are conservative. V. dahliae secretome are rich in potential pectinase, pathogen-host interaction protein, RxLx motif containing protein and small cysteine-rich protein which may play roles in V. dahliae pathogenetic mechanism.