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April 13, 2026Scientific Reports0 citationsOpen Access

The proteome study of germinated Puccinia triticina urediniospores reveals a novel effector protein required for virulence

AÖAhmet Çağlar ÖzketenNear East UniversityMCMerve CetinturkAhi Evran UniversityCRChristof RampitschAgriculture and Agri-Food Canada

Key Points

  • The aim is to identify proteins in the germinated urediniospores of Puccinia triticina that contribute to virulence.
  • Used proteomics to analyze germinated urediniospores of Puccinia triticina.
  • Applied two-dimensional gel electrophoresis to isolate proteins.
  • Identified 123 proteins by tandem mass spectrometry and characterized them in silico.
  • Performed host-induced gene silencing on candidate effector PTTG_06852 to study its function.
  • Identified 123 proteins predominantly involved in metabolic and cellular processes.
  • Annotated six proteins as candidate effectors related to virulence.
  • Reduced expression of PtVF1 by 78% led to a 70% decrease in infection severity.
  • Demonstrated significant impairment of virulence, validating PtVF1 as a virulence effector.

Abstract

The obligate biotrophic fungus, Puccinia triticina (Pt), is a notorious plant pathogen known for wheat leaf rust disease that devastates global crop production annually. Pathogen-host interactions need to be elucidated, especially the identification of pathogen effectors contributing to virulence. ‘Omics’ strategies are an efficient tool set to study these pathogen-host interactions. No proteome data are available on the germlings stage of Pt, which could highlight proteins involved in the first interaction point between Pt and its host. Here, we have used a proteomics approach on germinated urediniospores of Pt to define the germling proteome. Using two-dimensional gel electrophoresis, 167 spots in the pI range of 4–7 were observed, from which 123 proteins were identified by tandem mass spectrometry. Further in silico characterization revealed that they were predominantly involved in metabolic and cellular processes, with six proteins annotated as candidate effectors. The candidate effector PTTG₀6852, hereafter named as virulence factor 1 (PtVF1), was silenced by host-induced gene silencing (HIGS) to investigate its biological function. When the expression of PtVF1 was reduced by 78%, the infection severity was suppressed by 70%. The results demonstrate a significant impairment of virulence upon silencing, which validates PtVF1 as a virulence effector of Pt.

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Cite This Study

Özketen et al. (2026) studied this question.

synapsesocial.com/papers/69dc87983afacbeac03e9eb1https://doi.org/10.1038/s41598-026-44996-2
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