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Secretome of the biocontrol agent Metarhizium anisopliae induced by the cuticle of the cotton pest Dysdercus peruvianus reveals new insights into infection

Academic Article
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Overview

authors

  • Beys-da-Silva, W. O.
  • Santi, L.
  • Berger, M.
  • Calzolari, D.
  • Passos, D. O.
  • Guimaraes, J. A.
  • Moresco, J. J.
  • Yates III, John

publication date

  • May 2014

journal

  • Journal of Proteome Research  Journal

abstract

  • Metarhizium anisopliae is an entomopathogenic fungus that has evolved specialized strategies to infect insect hosts. Here we analyzed secreted proteins related to Dysdercus peruvianus infection. Using shotgun proteomics, abundance changes in 71 proteins were identified after exposure to host cuticle. Among these proteins were classical fungal effectors secreted by pathogens to degrade physical barriers and alter host physiology. These include lipolytic enzymes, Pr1A, B, C, I, and J proteases, ROS-related proteins, oxidorreductases, and signaling proteins. Protein interaction networks were generated postulating interesting candidates for further studies, including Pr1C, based on possible functional interactions. On the basis of these results, we propose that M. anisopliae is degrading host components and actively secreting proteins to manage the physiology of the host. Interestingly, the secretion of these factors occurs in the absence of a host response. The findings presented here are an important step in understanding the host-pathogen interaction and developing more efficient biocontrol of D. peruvianus by M. anisopliae.

subject areas

  • Animals
  • Cell Surface Extensions
  • Fungal Proteins
  • Gossypium
  • Heteroptera
  • Host-Pathogen Interactions
  • Metarhizium
  • Proteome
  • Proteomics
  • Tandem Mass Spectrometry
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Research

keywords

  • Dysdercus peruvianus
  • Metarhizium anisopliae
  • biocontrol
  • host infection
  • shotgun proteomics
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Identity

PubMed Central ID

  • PMC4012838

International Standard Serial Number (ISSN)

  • 1535-3893

Digital Object Identifier (DOI)

  • 10.1021/pr401204y

PubMed ID

  • 24702058
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Additional Document Info

start page

  • 2282

end page

  • 2296

volume

  • 13

issue

  • 5

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