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Proteomic and secretomic response of an African Armillaria species to iron.

ABSTRACT: Armillaria species have attracted considerable research interest because they are widely distributed, mostly plant-pathogenic, and exhibit unique characteristics. Abiotic factors influence intra- and inter-species variations in pathogenicity and/or virulence of these fungi. However, the mechanisms involved in causing these variations are not well understood. Iron is an indispensable element in several molecular and biological processes. Yet, excessive abundance of iron can be toxic to organisms due to Fenton-like reactions. This study aimed to gain insights into the type and extent of iron-responsive proteomic and secretomic changes in Armillaria sp. strain CMW4456 cultured in liquid media supplemented with iron using a multi-omics approach. Significant iron-dependent alterations of proteins involved in metabolism and growth were observed in the proteomes and secretomes. Iron supplementation at 100µM did not elicit an oxidative stress response by the fungus. Our analyses revealed three putative siderophore biosynthetic gene clusters (BGCs) in the genome and expression of proteins encoded by some BGC genes in the proteome. This knowledge contributes to a better understanding of the mechanisms employed by an Armillaria sp. in response to iron, gives insights into possible modes for inhibiting or attenuating pathogenicity and/or virulence of Armillaria spp., and can be valorised for more biotechnological applications.

INSTRUMENT(S):

ORGANISM(S): Fungi Armillaria Sp. Cmw 4456 Basidiomycota

TISSUE(S): Culture Fluid, Vegetative Cell (sensu Fungi), Mycelium

SUBMITTER: Deborah L. Narh

LAB HEAD: Brenda D.

PROVIDER: PXD068883 | Pride | 2026-03-02

REPOSITORIES: Pride

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Source:

			Action	DRS
	1253_all_filtered.fasta	Fasta
	20220419_UP_4456_Mde_1-.mzML	Mzml
	20220419_UP_4456_Mde_1.raw	Raw
	20220419_UP_4456_Mde_2-.mzML	Mzml
	20220419_UP_4456_Mde_2.raw	Raw

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Project description:As integral parts of gene regulatory networks, small regulatory RNAs (sRNAs) play important roles in the adaptation of bacteria to environmental conditions. To adapt to iron limitation, many bacteria exploit an "iron-sparing" response mediated by Fur-regulated sRNAs such as RyhB of E. coli, allowing them to reduce the synthesis of iron-utilizing proteins not essential for growth. In this study, we aimed to confirm the regulatory role of the sRNA IsrR (Iron-sparing response Regulator) of S. aureus and to characterize the IsrR targetome in order to better understand the pathogens adaptation to iron-limited conditions often encountered in the host. To identify potential IsrR targets, two different experimental approaches were used. In the first, proteome profiles of S. aureus HG001 were compared to those of an isogenic ΔisrR mutant under iron-limited conditions. In the second approach, the effects of IsrR on the proteome under iron-rich conditions were analyzed using a strain in which IsrR was constitutively expressed from a plasmid. In silico target prediction was performed using the CopraRNA2 tool. Presence of IsrR caused a large number of consistent changes in protein levels both under iron-limited or iron-rich conditions. Among the proteins exhibiting significantly different abundance, 63 were in common between both experiments. Since sRNAs can have direct and indirect effects on global gene expression, the experimental approach was combined with in silico target prediction. In this way, very likely direct IsrR targets were identified, which include catalase (KatA) and three tricarboxylic acid (TCA) cycle enzymes (CitB, SdhA, SucA). Follow-up analyses confirmed that IsrR negatively affects KatA and CitB enzymatic activities. In contrast to most identified IsrR targets, the predicted interaction region of IsrR with the katA mRNA does not overlap the ribosome binding site, suggesting that IsrR cannot only inhibit translation, but also directly affect mRNA stability. A putative IsrR targetome was identified. In agreement with Fur-regulated sRNAs of other organisms, IsrR negatively affects the expression of TCA cycle and heme biosynthesis enzymes.

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Proteomic and secretomic response of an African Armillaria species to iron.

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