文献类型： 外文期刊
作者： Ahmad, Aqeel 1 ; Akram, Waheed 2 ; Wang, Rui 1 ; Shahzadi, Iqra 3 ; Umer, Muhammad 4 ; Yasin, Nasim Ahmad 6 ; Wu, Tingquan 1 ;
作者机构： 1.Guangdong Acad Agr Sci, Inst Facil Agr, Guangdong Acad Agr Sci IFA GDAAS, Vegetable Res Inst,Guangdong Key Lab New Technol, Guangzhou 510640, Peoples R China
2.Univ Punjab, Fac Agr Sci, Dept Plant Pathol, Lahore, Pakistan
3.Wuhan Univ, Hubei Engn Ctr Nat Polymers Based Med Mat, Sch Resource & Environm Sci,Hubei Int Sci & Techn, Hubei Key Lab Biomass Resource Chem & Environm Bi, Wuhan, Peoples R China
4.Guizhou Univ, Forestry Coll, Res Ctr Forest Ecol, Guiyang, Guizhou, Peoples R China
5.Guizhou Univ, Key Lab Karst Georesources & Environm, Minist Educ, Guiyang, Peoples R China
6.Univ Punjab, RO II Wing, Lahore, Pakistan
关键词： Irradiation; mutation; pathogenicity proteins; structural characterization; physicochemical properties
期刊名称：JOURNAL OF PLANT INTERACTIONS （ 影响因子：4.029； 五年影响因子：5.124 ）
ISSN： 1742-9145
年卷期： 2022 年 17 卷 1 期
页码：
收录情况： SCI
摘要： Deciphering the transcriptional activities of pathogenicity genes is critical to understand pathogenesis mechanisms of Phytophthora melonis, a devastating pathogen of cucurbits. In this study, we have performed comparative proteomics among P. melonis mutants to evaluate the interacting pathogenicity proteins. Structural characterization of all detected proteins discovered the physicochemical factors behind their pathogenic behavior. Results revealed that gamma radiations have an extreme potential to mutate P. melonis spores, and can be a safe alternative of chemical mutagens. P. melonis is accomplished with seventy-three differentially expressed proteins among which, seven proteins were ranked as strong pathogenicity factors, i.e. Q9AT01 (Elicitin), D0MX11 (Oligopeptidase A, putative), D0NB60 (Secreted RXLR effector peptide protein, putative), D0NIK4 (IpiB3-like protein), D0NIZ1 (Carboxypeptidase), H3GZF4 and H3GZF6. The Ramachandran plot determined the positions of secondary structures (alpha helix and beta sheets) in the 3D structures of pathogenicity proteins. Furthermore, the glycine residues analysis highlighted that six out of seven proteins were functionally and structurally more stable than D0NIK4 protein. The study concluded that the pathogenic proteins must have negative phi angles greater than 63 degrees, and psi angles >= 80 degrees for their proper functioning. This study establishes functional connections between pathogenicity genes and the process of disease establishment.
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