Computational identification of putative copper-binding proteins in pomegranate bacterial blight pathogen Xanthomonas citri pv. punicae

Dineshkumar, Krishnamoorthy; Antony, Ginny

doi:10.1007/s00203-022-02982-y

Cited by 3 publications

(2 citation statements)

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“…In this study, we employed a systematic computational pipeline of open‐access tools with documented better prediction accuracy, broad recognition, and trustworthiness. Furthermore, similar pipeline adoption by other researchers in published work, particularly in extracting metal‐binding proteins from microorganisms, further validated its suitability for our study 7,29 …”

Section: Introductionsupporting

confidence: 69%

“…Furthermore, similar pipeline adoption by other researchers in published work, particularly in extracting metal-binding proteins from microorganisms, further validated its suitability for our study. 7,29 We have also identified iron-and copper-binding effector candidates which may be involved in the virulence of Fol. In this in-depth in silico investigation, we present a comprehensive catalog of putative candidate metalloproteins that may serve as valuable starting points for subsequent experimental analysis and may be targeted to mitigate the virulence of phytopathogenic fungi.…”

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confidence: 99%

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The study of iron‐ and copper‐binding proteome of Fusarium oxysporum and its effector candidates

Kushwah,

Dixit,

Upadhyay

et al. 2024

Proteins

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Fusarium oxysporum f.sp. lycopersici is a phytopathogen which causes vascular wilt disease in tomato plants. The survival tactics of both pathogens and hosts depend on intricate interactions between host plants and pathogenic microbes. Iron‐binding proteins (IBPs) and copper‐binding proteins (CBPs) play a crucial role in these interactions by participating in enzyme reactions, virulence, metabolism, and transport processes. We employed high‐throughput computational tools at the sequence and structural levels to investigate the IBPs and CBPs of F. oxysporum. A total of 124 IBPs and 37 CBPs were identified in the proteome of Fusarium. The ranking of amino acids based on their affinity for binding with iron is Glu > His> Asp > Asn > Cys, and for copper is His > Asp > Cys respectively. The functional annotation, determination of subcellular localization, and Gene Ontology analysis of these putative IBPs and CBPs have unveiled their potential involvement in a diverse array of cellular and biological processes. Three iron‐binding glycosyl hydrolase family proteins, along with four CBPs with carbohydrate‐binding domains, have been identified as potential effector candidates. These proteins are distinct from the host Solanum lycopersicum proteome. Moreover, they are known to be located extracellularly and function as enzymes that degrade the host cell wall during pathogen–host interactions. The insights gained from this report on the role of metal ions in plant–pathogen interactions can help develop a better understanding of their fundamental biology and control vascular wilt disease in tomato plants.

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confidence: 69%

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confidence: 99%