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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.

Beys-da-Silva WO, Santi L, Berger M, Calzolari D, Passos DO, Guimarães JA, Moresco JJ, Yates JR - J. Proteome Res. (2014)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemical Physiology and ‡Department of Cell and Molecular Biology, The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.

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.

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Related in: MedlinePlus

Network analysis of differentially expressedproteins identifiedin 96h M. anisopliae supernatant when grown D. peruvianus cuticle medium. Spheres and triangles representproteins; lines connecting spheres indicate interactions between proteins.Red spheres, proteins up-regulated in response to DP cuticle; bluespheres, proteins down-regulated; green triangles, exclusive proteinsidentified in DP cuticle.
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fig4: Network analysis of differentially expressedproteins identifiedin 96h M. anisopliae supernatant when grown D. peruvianus cuticle medium. Spheres and triangles representproteins; lines connecting spheres indicate interactions between proteins.Red spheres, proteins up-regulated in response to DP cuticle; bluespheres, proteins down-regulated; green triangles, exclusive proteinsidentified in DP cuticle.

Mentions: When the 96h networkwas analyzed, 40% of the proteins had predictedinteractions (Figure 4). When compared withthe 48 h time point, it was not possible to identify any clustersof proteins with multiple connections. All 12 proteins interact withone or two other proteins. However, the highest score was observedfor the same group that already appears in the 48 h time point, functionsrelated to sugar degradation, suggesting the importance of these proteinsin glucose uptake for fungal growth.


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

Beys-da-Silva WO, Santi L, Berger M, Calzolari D, Passos DO, Guimarães JA, Moresco JJ, Yates JR - J. Proteome Res. (2014)

Network analysis of differentially expressedproteins identifiedin 96h M. anisopliae supernatant when grown D. peruvianus cuticle medium. Spheres and triangles representproteins; lines connecting spheres indicate interactions between proteins.Red spheres, proteins up-regulated in response to DP cuticle; bluespheres, proteins down-regulated; green triangles, exclusive proteinsidentified in DP cuticle.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4012838&req=5

fig4: Network analysis of differentially expressedproteins identifiedin 96h M. anisopliae supernatant when grown D. peruvianus cuticle medium. Spheres and triangles representproteins; lines connecting spheres indicate interactions between proteins.Red spheres, proteins up-regulated in response to DP cuticle; bluespheres, proteins down-regulated; green triangles, exclusive proteinsidentified in DP cuticle.
Mentions: When the 96h networkwas analyzed, 40% of the proteins had predictedinteractions (Figure 4). When compared withthe 48 h time point, it was not possible to identify any clustersof proteins with multiple connections. All 12 proteins interact withone or two other proteins. However, the highest score was observedfor the same group that already appears in the 48 h time point, functionsrelated to sugar degradation, suggesting the importance of these proteinsin glucose uptake for fungal growth.

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemical Physiology and ‡Department of Cell and Molecular Biology, The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.

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.

Show MeSH
Related in: MedlinePlus