Characterization of the novel antifungal protein PgAFP and the encoding gene of Penicillium chrysogenum

Rodrı́guez-Martı́n, Andrea; Acosta, Raquel; Liddell, Susan; Núñez, Félix; Benito, María José; Asensio, Miguel A.

doi:10.1016/j.peptides.2009.11.002

Cited by 60 publications

(51 citation statements)

References 26 publications

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“…Some antifungal proteins produced by molds are small, highly basic, and cysteine-rich proteins, such as PAF from Penicillium chrysogenum Q176 (Marx et al 1995), PgAFP from P. chrysogenum RP42C (Rodríguez-Martín et al 2010), PcArctin from P. chrysogenum A096 (Chen et al 2013), AFP from Aspergillus giganteus (Nakaya et al 1990), or NAFP from Neosartorya fischeri . The expression of these proteins is induced in the presence of other fungi and contributes to an ecological advantage (Marx 2004).…”

Section: Introductionmentioning

confidence: 99%

“…This is achieved through modulation of the intracellular glutathione (GSH) and ROS levels in Aspergillus nidulans (Hegedus et al 2011). Here we used PgAFP, one of these small, basic, and cysteine-rich proteins that inhibits growth of some toxigenic molds (Rodríguez-Martín et al 2010), to study the effect on the growth of A. flavus. Among the possible effects derived from antifungal proteins on A. flavus, those related to aflatoxin biosynthesis would be of interest for practical applications.…”

Section: Introductionmentioning

confidence: 99%

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Impact of the antifungal protein PgAFP from Penicillium chrysogenum on the protein profile in Aspergillus flavus

Delgado

Owens

Doyle

et al. 2015

Appl Microbiol Biotechnol

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Antifungal proteins produced by molds are generally small, highly basic, and cysteine-rich. The best known effects of these proteins include morphological changes, metabolic inactivation, and membrane perturbation on sensitive fungi. Reactive oxygen species (ROS) generation leads to apoptosis, with G -protein playing a key role in transduction of cell death signals. The antifungal protein PgAFP from Penicillium chrysogenum inhibits growth of some toxigenic molds. Here we analyzed the effect of the antifungal protein PgAFP on the growth of Aspergillus flavus. For this, comparative proteomic analysis was used to identify the whole protein profile and protein change in abundance after PgAFP treatment. PgAFP provoked metabolic changes related to reduced energy metabolism, cell wall integrity alteration, and increased stress response due to higher levels of ROS. The observed changes in protein abundance, favoring a higher glutathione concentration as well as the increased abundance in heat shock proteins, do not seem to be enough to avoid necrosis. The decreased chitin deposition observed in PgAFP-treated A. flavus is attributed to a lower relative quantity of Rho1. The reduced relative abundance of a β subunit of G -protein seems to be the underlying reason for modulation of apoptosis in PgAFP-treated A. flavus hyphae. We propose Rho1 and G -protein subunit β CpcB to be the main factors in the mode of action of PgAFP in A. flavus. Additionally, enzymes essential for the biosynthesis of aflatoxin were no longer detectable in A. flavus hyphae at 24 h, following treatment with PgAFP. This presents a promising effect of PgAFP, which may prevent A. flavus from producing mycotoxins. However, the impact of PgAFP on actual aflatoxin production requires further study.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Impact of the antifungal protein PgAFP from Penicillium chrysogenum on the protein profile in Aspergillus flavus

Delgado

Owens

Doyle

et al. 2015

Appl Microbiol Biotechnol

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“…The antifungal protein PgAFP produced by the strain Penicillium chrysogenum CECT 20922 (formerly RP42C) is within a group of small, highly basic and low molecular mass proteins (Rodríguez-Martín et al 2010). PgAFP inhibits various pathogenic and spoilage ascomycetes of interest in foods, including strains of various Aspergillus spp., such as A. carbonarius, A. flavus, A. ochraceus, A. fumigatus, and A. tubingensis, as well as Penicillium spp., such as P. commune, P. restrictum, P. nalgiovense, and P. chrysogenum (Delgado et al 2015a).…”

Section: Introductionmentioning

confidence: 99%

Increased chitin biosynthesis contributes to the resistance of Penicillium polonicum against the antifungal protein PgAFP

Delgado

Owens

Doyle

et al. 2015

Appl Microbiol Biotechnol

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Antifungal proteins from molds have been proposed as a valuable tool against unwanted molds, but the resistance of some fungi limits their use. Resistance to antimicrobial peptides has been suggested to be due to lack of interaction with the mold or to a successful response. The antifungal protein PgAFP produced by Penicillium chrysogenum inhibits the growth of various ascomycetes, but not Penicillium polonicum. To study the basis for resistance to this antifungal protein, localization of PgAFP and metabolic, structural, and morphological changes were investigated in P. polonicum. PgAFP bound the outer layer of P. polonicum but not regenerated chitin, suggesting an interaction with specific molecules. Comparative two-dimensional gel electrophoresis (2D-PAGE) and comparative quantitative proteomics revealed changes in the relative abundance of several proteins from ribosome, spliceosome, metabolic, and biosynthesis of secondary metabolite pathways. The proteome changes and an altered permeability reveal an active reaction of P. polonicum to PgAFP. The successful response of the resistant mold seems to be based on the higher abundance of protein Rho GTPase Rho1 that would lead to the increased chitin deposition via cell wall integrity (CWI) signaling pathway. Thus, combined treatment with chitinases could provide a complementary means to combat resistance to antifungal proteins.

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“…This property could explain the high thermostability of the AcAMP peptide. Similar three-dimensional (3D) structures were obtained with antifungal peptides from ascomycetes such as AcAFP [28], PcAFP [26], and AFP [25]. The common feature shared among the cationic antimicrobial peptides is their ability to fold into amphipathic conformations in the presence of hydrophobic amino acid residues.…”

Section: Discussionmentioning

confidence: 75%

“…The mature protein would adopt its active conformation after the pro-sequence is cleaved. Antimicrobial peptides produced as pre-pro-proteins from ascomycetes include AFP, AcAFP, and PgAFP from A. giganteus, A. clavatus VR1, and P. chrysogenum, respectively [25,26,28].…”

Section: Discussionmentioning

confidence: 99%

A highly thermostable antimicrobial peptide from Aspergillus clavatus ES1: biochemical and molecular characterization

Hajji¹,

Jellouli²,

Hmidet³

et al. 2010

J Ind Microbiol Biotechnol

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Antimicrobial peptides (AMPs) are extremely attractive candidates as therapeutic agents due to their wide spectrum of antimicrobial activity and mechanism of action, which differs from that of small-molecule antibiotics. In this study, a 6.0-kDa antimicrobial peptide from Aspergillus clavatus ES1, designated as AcAMP, was isolated by a one-step heat treatment. AcAMP was sensitive to proteolytic enzymes, stable between pH 5.0 and 10.0, and heat resistant (15 min at 100 degrees C). The acamp gene encoding AcAMP peptide was isolated by reverse-transcriptase polymerase chain reaction (RT-PCR) and cloned in pCRII-TOPO vector. Sequence analysis of the complementary DNA (cDNA) acamp gene revealed an open reading frame of 282 bp encoding a peptide of 94 amino acid residues consisting of a 21-aa signal peptide, a 22-aa pro-peptide, and a 51-aa mature peptide. The deduced amino acid sequence showed high identity with other ascomycete antifungal peptides. AcAMP belongs to the group of small, cysteine-rich, basic proteins with antimicrobial activity. In addition to its antifungal activity, AcAMP is the first fungal peptide exhibiting antibacterial activity against several Gram-positive and Gram-negative bacteria. Based on all these features, AcAMP can be considered as a promising new member of the restraint family of ascomycete antimicrobial peptides that might be used in biological control of plant diseases and also for potential applications in food preservation.

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Characterization of the novel antifungal protein PgAFP and the encoding gene of Penicillium chrysogenum

Cited by 60 publications

References 26 publications

Impact of the antifungal protein PgAFP from Penicillium chrysogenum on the protein profile in Aspergillus flavus

Impact of the antifungal protein PgAFP from Penicillium chrysogenum on the protein profile in Aspergillus flavus

Increased chitin biosynthesis contributes to the resistance of Penicillium polonicum against the antifungal protein PgAFP

A highly thermostable antimicrobial peptide from Aspergillus clavatus ES1: biochemical and molecular characterization

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