Conidial surface proteins of Metarhizium anisopliae: Source of activities related with toxic effects, host penetration and pathogenesis
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Updated: Jun 17, 2026

Development of Metarhizium anisopliae as a Mycoinsecticide: From Isolation to Field Performance
Published on: July 30, 2017
Lucélia Santi1, Walter O Beys da Silva, Markus Berger
1Centro de Biotecnologia Universidade Federal do Rio Grande do Sul, P. O. Box 15005, CEP 91501-970, Porto Alegre, RS, Brazil.
Abstract:
Conidial contact with an arthropod surface is the first step of the fungal penetration and infection process. However, conidia of Metarhizium anisopliae have associated components, like enzymes that could be involved in triggering the penetration process and toxic effects that have not yet been well characterized. Fungi produce many enzymes that also are toxic components found in bacteria and animal venoms and thus may be considered as potential virulence factors. In this work, we report several enzymatic activities from spore surface protein extracts. The major proteolytic activities observed in spore surface proteins (SSP) were Pr1 and Pr2 activities, in that order. According to the zymograms obtained, SSP contain different proteases. SSP contain trehalase, exo- and endo-chitinase activities, and seven different chitinase bands which have been observed in zymograms. Activities involved in protection against reactive oxygen species (ROS) were also detected. Two lipolytic enzymes were also detected in lipase zymograms. Phospholipase C activity, closely related to microbial pathogenesis, was detected for the first time in M. anisopliae conidia. These activities described could be an initial step towards understanding the mechanisms involved in the first stage of M. anisopliae infection process and its toxic effects against arthropod hosts.
Insights
Metarhizium anisopliae spore surface proteins (SSP) possess diverse enzymatic activities, including proteases, chitinases, lipases, and phospholipase C. These enzymes are crucial for understanding fungal infection mechanisms and toxic effects on arthropod hosts.
Area of Science:
- Mycology
- Biochemistry
- Entomology
Background:
- Fungal pathogens initiate infection through conidial contact with host surfaces.
- The enzymatic components of Metarhizium anisopliae conidia involved in host penetration and toxicity remain incompletely understood.
- Enzymes produced by fungi can act as virulence factors, similar to toxins in bacteria and animal venoms.
Purpose of the Study:
- To characterize the enzymatic activities present on the surface of Metarhizium anisopliae conidia.
- To identify potential virulence factors contributing to the early stages of arthropod infection.
Main Methods:
- Extraction of spore surface proteins (SSP) from Metarhizium anisopliae.
- Analysis of enzymatic activities using zymography, including proteases, chitinases, lipases, and phospholipase C.
- Detection of antioxidant activities against reactive oxygen species (ROS).
Main Results:
- SSP exhibited significant proteolytic activities (Pr1 and Pr2), trehalase, exo- and endo-chitinase activities with seven distinct chitinase bands.
- Enzymatic assays revealed the presence of two lipolytic enzymes and phospholipase C activity, a first for M. anisopliae conidia.
- ROS-protective activities were also detected in the SSP.
Conclusions:
- Metarhizium anisopliae conidia possess a complex array of surface enzymes with potential roles in host interaction.
- These identified enzymatic activities provide insights into the initial mechanisms of fungal pathogenesis and toxic effects against arthropods.
- Further research into these enzymes can elucidate virulence strategies and inform biocontrol applications.
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