Antimicrobial Activities of Novel Peptides Derived from Defensin Genes of Brassica hybrid cv Pule

Kaewklom, Siriporn; Euanorasetr, Jirayut; Intra, Bungonsiri; Panbangred, Watanalai; Aunpad, Ratchaneewan

doi:10.1007/s10989-015-9488-2

Cited by 9 publications

(11 citation statements)

References 22 publications

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“…On the contrary, the γ-core motif of PAF has antifungal activity by itself [44]. In plant defensins, which are other cysteine-rich antifungal proteins structurally related to fungal AFPs, some γ-core motifs have been reported to have antifungal activity, as it is the case of MtDef4 from Medicago truncatula [45] and BhDef2 from Brassica hybrid [46], while in other cases a structural role for this γ-core is proposed [45].…”

Section: Discussionmentioning

confidence: 99%

Rational Design and Biotechnological Production of Novel AfpB-PAF26 Chimeric Antifungal Proteins

et al. 2018

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Antimicrobial peptides (AMPs) have been proposed as candidates to develop new antimicrobial compounds for medicine, agriculture, and food preservation. PAF26 is a synthetic antifungal hexapeptide obtained from combinatorial approaches with potent fungicidal activity against filamentous fungi. Other interesting AMPs are the antifungal proteins (AFPs) of fungal origin, which are basic cysteine-rich and small proteins that can be biotechnologically produced in high amounts. A promising AFP is the AfpB identified in the phytopathogen Penicillium digitatum. In this work, we aimed to rationally design, biotechnologically produce and test AfpB::PAF26 chimeric proteins to obtain designed AFPs (dAfpBs) with improved properties. The dAfpB6 and dAfpB9 chimeras could be produced using P. digitatum as biofactory and a previously described Penicillium chrysogenum-based expression cassette, but only dAfpB9 could be purified and characterized. Protein dAfpB9 showed subtle and fungus-dependent differences of fungistatic activity against filamentous fungi compared to native AfpB. Significantly, dAfpB9 lost the fungicidal activity of PAF26 and AfpB, thus disconnecting this activity from the fungistatic activity and mapping fungicidal determinants to the exposed loop L3 of AfpB, wherein modifications are located. This study provides information on the design and development of novel chimeric AFPs.

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Section: Discussionmentioning

confidence: 99%

Rational Design and Biotechnological Production of Novel AfpB-PAF26 Chimeric Antifungal Proteins

et al. 2018

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“…Most of the studies based on peptides derived from antifungal CRPs have focused on defensins and the highly conserved γ-motif (Sagaram et al, 2011; Avitabile et al, 2013; van der Weerden and Anderson, 2013; Muñoz et al, 2014; Kaewklom et al, 2016), but not on fungal AFPs. Our data identify for the first time synthetic peptides derived from fungal AFPs with antifungal activity.…”

Section: Discussionmentioning

confidence: 99%

“…Plant defensins are related to AFPs in that they are small and cationic CRPs that have antifungal activity and contain the γ-core motif; however, their αβ fold is structurally distinct from that of AFPs (van der Weerden and Anderson, 2013; Silva et al, 2014). Analogous γ-core peptides from the plant defensins MtDef4 from Medicago , SolyC07g007760 from tomato, or BhDef2 from Brassica were antimicrobial (Sagaram et al, 2011; Avitabile et al, 2013; Kaewklom et al, 2016). However, other γ-core peptides such as the two motifs derived from the Medicago defensin MsDef1 did not show antifungal activity against Fusarium graminearum (Sagaram et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

“…In previous studies, a correlation between the cationic net charge of the γ-core-derivative peptides and their antimicrobial activity was demonstrated. The peptide derivative BhDEF12M from BhDef1 protein contains asparagine to arginine substitutions that promoted antibacterial and antifungal activity (Kaewklom et al, 2016). Yet, there are exemptions to this rule as other non-cationic γ-core peptides derived from plant defensins (i.e., BhDef23) were antimicrobial (Kaewklom et al, 2016).…”

Section: Discussionmentioning

confidence: 99%

“…The peptide derivative BhDEF12M from BhDef1 protein contains asparagine to arginine substitutions that promoted antibacterial and antifungal activity (Kaewklom et al, 2016). Yet, there are exemptions to this rule as other non-cationic γ-core peptides derived from plant defensins (i.e., BhDef23) were antimicrobial (Kaewklom et al, 2016). In this context, PAF109 is a peptide that has low positive charge (ca.…”

Section: Discussionmentioning

confidence: 99%

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Mapping and Identification of Antifungal Peptides in the Putative Antifungal Protein AfpB from the Filamentous Fungus Penicillium digitatum

et al. 2017

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Antifungal proteins (AFPs) from Ascomycetes are small cysteine-rich proteins that are abundantly secreted and show antifungal activity against non-producer fungi. A gene coding for a class B AFP (AfpB) was previously identified in the genome of the plant pathogen Penicillium digitatum. However, previous attempts to detect the AfpB protein were not successful despite the high expression of the corresponding afpB gene. In this work, the structure of the putative AfpB was modeled. Based on this model, four synthetic cysteine-containing peptides, PAF109, PAF112, PAF118, and PAF119, were designed and their antimicrobial activity was tested and characterized. PAF109 that corresponds to the γ-core motif present in defensin-like antimicrobial proteins did not show antimicrobial activity. On the contrary, PAF112 and PAF118, which are cationic peptides derived from two surface-exposed loops in AfpB, showed moderate antifungal activity against P. digitatum and other filamentous fungi. It was also confirmed that cyclization through a disulfide bridge prevented peptide degradation. PAF116, which is a peptide analogous to PAF112 but derived from the Penicillium chrysogenum antifungal protein PAF, showed activity against P. digitatum similar to PAF112, but was less active than the native PAF protein. The two AfpB-derived antifungal peptides PAF112 and PAF118 showed positive synergistic interaction when combined against P. digitatum. Furthermore, the synthetic hexapeptide PAF26 previously described in our laboratory also exhibited synergistic interaction with the peptides PAF112, PAF118, and PAF116, as well as with the PAF protein. This study is an important contribution to the mapping of antifungal motifs within the AfpB and other AFPs, and opens up new strategies for the rational design and application of antifungal peptides and proteins.

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Analysis of the Structural Stability Among Cyclotide Members Through Cystine Knot Fold that Underpins Its Potential Use as a Drug Scaffold

Senthilkumar

Rajasekaran

2016

Int J Pept Res Ther

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Antimicrobial Activities of Novel Peptides Derived from Defensin Genes of Brassica hybrid cv Pule

Cited by 9 publications

References 22 publications

Rational Design and Biotechnological Production of Novel AfpB-PAF26 Chimeric Antifungal Proteins

Rational Design and Biotechnological Production of Novel AfpB-PAF26 Chimeric Antifungal Proteins

Mapping and Identification of Antifungal Peptides in the Putative Antifungal Protein AfpB from the Filamentous Fungus Penicillium digitatum

Analysis of the Structural Stability Among Cyclotide Members Through Cystine Knot Fold that Underpins Its Potential Use as a Drug Scaffold

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