Proteomic analysis of proteins secreted by Botrytis cinerea in response to heavy metal toxicity

Abstract

Although essential in many cellular processes, metals become toxic when they are present in excess and constitute a global environmental hazard. To overcome this stress, fungi have evolved several mechanisms at both intracellular and extracellular levels. In particular, fungi are well known for their ability to secrete a large panel of proteins. However, their role in the adaptation of fungi to metal toxicity has not yet been investigated. To address this question, here, the fungus Botrytis cinerea was challenged to copper, zinc, nickel or cadmium stress and secreted proteins were collected and separated by 2D-PAGE. One hundred and sixteen spots whose volume varied under at least one tested condition were observed on 2D gels. Densitometric analyses revealed that the secretome signature in response to cadmium was significantly different from those obtained with the other metals. Fifty-five of these 116 spots were associated with unique proteins and functional classification revealed that the production of oxidoreductases and cell-wall degrading enzymes was modified in response to metals. Promoter analysis disclosed that PacC/Rim101 sites were statistically over-represented in the upstream sequences of the 31 genes corresponding to the varying unique spots suggesting a possible link between pH regulation and metal response in B. cinerea.

Proteomic profiling of Botrytis cinerea conidial germination

“…Therefore, proteomic analysis has an increasing importance in the search of virulence factors in plant pathogenic fungi (Garrido et al 2010;Gonzalez-Fernandez and Jorrin-Novo 2012). Recently, an increasing number of B. cinerea proteomics approaches has been published, ranging from total proteome analyses to various subproteome studies based on gel or gel-free techniques (Fernández-Acero et al 2006Shah et al 2009a, b;Espino et al 2010;Cherrad et al 2012;Li et al 2012;Gonzalez-Fernandez et al 2013;Davanture et al 2014). These advances have been facilitated due to the recent publication of two different genome databases of B. cinerea (http://www.broadinstitute.org/ annotation/genome/botrytis_cinerea/MultiHome.html and https://urgi.versailles.inra.fr/Species/Botrytis).…”

A proteomic‐based investigation of potential copper‐responsive biomarkers: Proteins, conceptual networks, and metabolic pathways featuring Penicillium janthinellum from a heavy metal‐polluted ecological niche

“…Furthermore, regulation of Cu uptake and export is relevant to posttranslational modifications of proteins (van den Berghe & Klomp, ). To the best of our knowledge, only a few studies have focused on Cu‐responsive proteins in filamentous fungi such as Aspergillus nidulans s (Oddon, Diatloff, & Roberts, ) and Botrytis cinerea s (Cherrad et al., ). Nevertheless, most of these existing studies have only focused on the final result of ATP use during Cu resistance and have not considered the following during the resistance at the proteome level: of the steps in the ATP‐generating metabolic pathways; the mediator protein‐based networks in Cu signal transduction; and the changes in fungi proteomes and pathways in response to changes in Cu concentration.…”

Horizontal gene transfer in the sponge Amphimedon queenslandica

“…(Cherrad et al 2012) and host zinc scavenging by the pathogen C. albicans (Citiulo et al 2012). However, co-option of the zinc binding properties is just one possible evolutionary trajectory of the AqAspzs, since moonlighters can also have functions quite distant and unconnected to the normal function or structure of the original peptide (Copley 2003).…”

“…Some aspzincins do not have proteolytic activity, but their zinc-binding properties facilitate other roles. For instance, aspzincins have an excess metal binding function in the fungus Botrytis cinerea (Cherrad et al 2012), and aspzincins scavenge host zinc for the pathogenic fungus Candida albicans (Citiulo et al 2012). …”

“…All detected hemopexin domain-containing genes in bacteria were investigated and their domain architectures are shown; however all other taxa shown are representative only and do not show the complete taxonomic distribution and domain architecture diversity of the hemopexin domain, but note that no other aspzincin-hemopexin genes have been identified. (Nonaka et al 1998;Fushimi et al 1999;Doi et al 2004;Arnadottir et al 2009), though some have zinc-binding roles (Cherrad et al 2012;Citiulo et al 2012). Because of their taxonomic distribution, it was surprising to find bacterial-like aspzincins in 16 diverse sponge species that together are predicted to represent both of the two major sponge lineages (Gazave et al 2010;Gazave et al 2012).…”