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Protein Research in Pathogenic Fungi
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Protein Research in Pathogenic Fungi

A special issue of Journal of Fungi (ISSN 2309-608X).

Deadline for manuscript submissions: 31 July 2025 | Viewed by 1741

Special Issue Editors

Dr. Justyna Karkowska-Kuleta

E-Mail Website
Guest Editor
Department of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland
Interests: biochemistry; protein purification; proteins; fungi
Special Issues, Collections and Topics in MDPI journals
Dr. Dorota Satala

E-Mail Website
Guest Editor
Department of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland
Interests: biochemistry; protein purification; proteins; fungi

Special Issue Information

Dear Colleagues,

The thorough characterization and identification of fungal proteins must be prioritized in investigations into the pathogenesis of fungal infections. The structural attributes of these molecules, their localization, their enzymatic functions, and their interaction capabilities are essential in fungal cell biology and communication between pathogenic fungi and other microorganisms inhabiting the same niche, as well as between pathogenic fungi and the host. Intracellular proteins, those presenting on the fungal cell surface, and those secreted outside the cell, including proteins transported by fungal extracellular vesicles, can be involved, through multifaceted cooperation, in a range of biological processes. Investigating the differential expression of these proteins under specific environmental conditions and the variability in their interactions is necessary in elucidating infection mechanisms and developing effective strategies for the prevention and treatment of fungal diseases.

For this Special Issue, we will accept both original research articles and review papers focused on the study of fungal proteins produced by pathogenic fungi affecting plants, animals, and humans. 

Dr. Justyna Karkowska-Kuleta
Dr. Dorota Satala
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Journal of Fungi is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • protein characterization
  • fungal proteomics
  • enzymatic activity
  • protein–protein interactions
  • host–pathogen interactions
  • environmental stress response
  • differential protein expression
  • virulence factors
  • antifungal resistance
  • signaling
  • protein structure

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Further information on MDPI's Special Issue policies can be found here.

Published Papers (2 papers)

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28 pages, 4650 KiB  
Article
Silencing of MNT1 and PMT2 Shows the Importance of O-Linked Glycosylation During the Sporothrix schenckii–Host Interaction
by Manuela Gómez-Gaviria, José A. Martínez-Álvarez, Iván Martínez-Duncker, Andrea Regina de Souza Baptista and Héctor M. Mora-Montes
J. Fungi 2025, 11(5), 352; https://doi.org/10.3390/jof11050352 - 2 May 2025
Viewed by 1119
Abstract
Sporothrix schenckii is a pathogenic fungus of worldwide distribution and one of the etiological agents of sporotrichosis. The cell wall is the first point of contact with host cells; therefore, its composition has been widely studied. It has a cell wall composed of [...] Read more.
Sporothrix schenckii is a pathogenic fungus of worldwide distribution and one of the etiological agents of sporotrichosis. The cell wall is the first point of contact with host cells; therefore, its composition has been widely studied. It has a cell wall composed of chitin, β-glucans, and glycoproteins modified with N-linked and O-linked glycans. Protein O-linked glycosylation is mediated by two gene families, PMT and MNT. Therefore, we evaluated the relevance of protein O-linked glycosylation during the interaction of S. schenckii with the host. Independent silencing of the MNT1 and PMT2 was accomplished by interference RNA. Morphological analyses revealed defects in cell morphology in both yeast and mycelial cells; however, these defects differed between MNT1 and PMT2 silencing. Subsequently, the cell wall was characterized, and the silencing of these genes markedly changed cell wall organization. When the silenced strains interacted with human peripheral blood mononuclear cells, a reduced ability to stimulate the proinflammatory cytokines IL-6 and TNFα was found. However, the PMT2-silenced mutants also stimulated higher levels of IL-10 and IL-1β. Interaction with macrophages and neutrophils was also altered, with increased phagocytosis and decreased extracellular trap formation in both sets of silenced strains. Survival assays in Galleria mellonella larvae showed that silencing of any of these genes reduced the ability of S. schenckii to kill the host. In addition, the mutant strains showed defects in the adhesion to extracellular matrix proteins. These data indicate that MNT1 and PMT2 are relevant for cell wall synthesis and interaction with the host. Full article
(This article belongs to the Special Issue Protein Research in Pathogenic Fungi)
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46 pages, 13286 KiB  
Article
Three-Dimensional Structural Heteromorphs of Mating-Type Proteins in Hirsutella sinensis and the Natural Cordyceps sinensis Insect–Fungal Complex
by Xiu-Zhang Li, Yu-Ling Li and Jia-Shi Zhu
J. Fungi 2025, 11(4), 244; https://doi.org/10.3390/jof11040244 - 23 Mar 2025
Viewed by 336
Abstract
The MAT1-1-1 and MAT1-2-1 proteins are essential for the sexual reproduction of Ophiocordyceps sinensis. Although Hirsutella sinensis has been postulated to be the sole anamorph of O. sinensis and to undergo self-fertilization under homothallism or pseudohomothallism, little is known about the three-dimensional [...] Read more.
The MAT1-1-1 and MAT1-2-1 proteins are essential for the sexual reproduction of Ophiocordyceps sinensis. Although Hirsutella sinensis has been postulated to be the sole anamorph of O. sinensis and to undergo self-fertilization under homothallism or pseudohomothallism, little is known about the three-dimensional (3D) structures of the mating proteins in the natural Cordyceps sinensis insect–fungal complex, which is a valuable therapeutic agent in traditional Chinese medicine. However, the alternative splicing and differential occurrence and translation of the MAT1-1-1 and MAT1-2-1 genes have been revealed in H. sinensis, negating the self-fertilization hypothesis but rather suggesting the occurrence of self-sterility under heterothallic or hybrid outcrossing. In this study, the MAT1-1-1 and MAT1-2-1 proteins in 173 H. sinensis strains and wild-type C. sinensis isolates were clustered into six and five clades in the Bayesian clustering trees and belonged to 24 and 21 diverse AlphaFold-predicted 3D structural morphs, respectively. Over three-quarters of the strains/isolates contained either MAT1-1-1 or MAT1-2-1 proteins but not both. The diversity of the heteromorphic 3D structures of the mating proteins suggested functional alterations of the proteins and provided additional evidence supporting the self-sterility hypothesis under heterothallism and hybridization for H. sinensis, Genotype #1 of the 17 genome-independent O. sinensis genotypes. The heteromorphic stereostructures and mutations of the MAT1-1-1 and MAT1-2-1 proteins in the wild-type C. sinensis isolates and natural C. sinensis insect–fungi complex suggest that there are various sources of the mating proteins produced by two or more cooccurring heterospecific fungal species in natural C. sinensis that have been discovered in mycobiotic, molecular, metagenomic, and metatranscriptomic studies, which may inspire future studies on the biochemistry of mating and pheromone receptor proteins and the reproductive physiology of O. sinensis. Full article
(This article belongs to the Special Issue Protein Research in Pathogenic Fungi)
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