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Multifunctional Fungal Proteins
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Multifunctional Fungal Proteins

A special issue of Journal of Fungi (ISSN 2309-608X). This special issue belongs to the section "Fungal Genomics, Genetics and Molecular Biology".

Deadline for manuscript submissions: closed (30 September 2023) | Viewed by 6912

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
Dr. Sunil K Shaw

E-Mail Website
Guest Editor
1. Women & Infants Hospital, Providence, RI, USA
2. Alpert Medical School of Medicine, Brown University, Providence, RI, USA
Interests: Candida; cell wall; adhesion; phagocytosis; cytoskeleton; endothelium; epithelium

Special Issue Information

Dear Colleagues,

Fungi produce and secrete a variety of proteins at different stages of their life cycle, and this process may also be influenced by changing external conditions, reflecting the great adaptability of these microorganisms. An interesting phenomenon is the performance of several substantially different functions by one particular protein depending on its location, availability of ligands, ions or regulatory molecules, as well as oligomerization state or the ability to form complexes with other proteins.

Multifunctional proteins are often involved in regulatory processes, response to environmental conditions, interactions with other microorganisms that coexist in the same ecological niche, and in the pathogenesis of fungal infections. One interesting group of such proteins are the so-called moonlighting proteins, represented by the evolutionarily conserved intracellular enzymes from the basic metabolic cycles, which are also often secreted or displayed at the cell surface, where they play a completely different role, including being involved in the interactions with host tissues or proteins during infection. In addition, typical fungal cell wall proteins, which perform specific functions on the cell surface and take part in fungal adhesion, may also exhibit other functions, for instance by playing the role of invasins, sensors, and regulators.

This special issue will include studies on various aspects of fungal protein multifunctionality and is intended to cover the state of research on the different roles of intracellular and extracellular proteins produced by various fungal species, as well as mechanisms for acquiring new functions by protein or identifying a protein as a moonlighting protein. Original research articles or reviews exploring the variety of fungal protein activities or the characteristics of one particular protein involved in different pathways and activities are welcome.

Dr. Justyna Karkowska-Kuleta
Dr. Sunil K Shaw
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

  • multifunctionality
  • moonlighting proteins
  • adhesins
  • invasins
  • regulators
  • sensors
  • secretome
  • cell wall

Published Papers (4 papers)

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Review

14 pages, 873 KiB  
Review
Moonlighting Proteins: Diverse Functions Found in Fungi
by Nicole J. Curtis, Krupa J. Patel, Amina Rizwan and Constance J. Jeffery
J. Fungi 2023, 9(11), 1107; https://doi.org/10.3390/jof9111107 - 15 Nov 2023
Viewed by 1257
Abstract
Moonlighting proteins combine multiple functions in one polypeptide chain. An increasing number of moonlighting proteins are being found in diverse fungal taxa that vary in morphology, life cycle, and ecological niche. In this mini-review we discuss examples of moonlighting proteins in fungi that [...] Read more.
Moonlighting proteins combine multiple functions in one polypeptide chain. An increasing number of moonlighting proteins are being found in diverse fungal taxa that vary in morphology, life cycle, and ecological niche. In this mini-review we discuss examples of moonlighting proteins in fungi that illustrate their roles in transcription and DNA metabolism, translation and RNA metabolism, protein folding, and regulation of protein function, and their interaction with other cell types and host proteins. Full article
(This article belongs to the Special Issue Multifunctional Fungal Proteins)
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19 pages, 3567 KiB  
Review
Sticking to the Subject: Multifunctionality in Microbial Adhesins
by Peter N. Lipke and Peleg Ragonis-Bachar
J. Fungi 2023, 9(4), 419; https://doi.org/10.3390/jof9040419 - 29 Mar 2023
Cited by 2 | Viewed by 1607
Abstract
Bacterial and fungal adhesins mediate microbial aggregation, biofilm formation, and adhesion to host. We divide these proteins into two major classes: professional adhesins and moonlighting adhesins that have a non-adhesive activity that is evolutionarily conserved. A fundamental difference between the two classes is [...] Read more.
Bacterial and fungal adhesins mediate microbial aggregation, biofilm formation, and adhesion to host. We divide these proteins into two major classes: professional adhesins and moonlighting adhesins that have a non-adhesive activity that is evolutionarily conserved. A fundamental difference between the two classes is the dissociation rate. Whereas moonlighters, including cytoplasmic enzymes and chaperones, can bind with high affinity, they usually dissociate quickly. Professional adhesins often have unusually long dissociation rates: minutes or hours. Each adhesin has at least three activities: cell surface association, binding to a ligand or adhesive partner protein, and as a microbial surface pattern for host recognition. We briefly discuss Bacillus subtilis TasA, pilin adhesins, gram positive MSCRAMMs, and yeast mating adhesins, lectins and flocculins, and Candida Awp and Als families. For these professional adhesins, multiple activities include binding to diverse ligands and binding partners, assembly into molecular complexes, maintenance of cell wall integrity, signaling for cellular differentiation in biofilms and in mating, surface amyloid formation, and anchorage of moonlighting adhesins. We summarize the structural features that lead to these diverse activities. We conclude that adhesins resemble other proteins with multiple activities, but they have unique structural features to facilitate multifunctionality. Full article
(This article belongs to the Special Issue Multifunctional Fungal Proteins)
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20 pages, 1468 KiB  
Review
More than Just Protein Degradation: The Regulatory Roles and Moonlighting Functions of Extracellular Proteases Produced by Fungi Pathogenic for Humans
by Dorota Satala, Grazyna Bras, Andrzej Kozik, Maria Rapala-Kozik and Justyna Karkowska-Kuleta
J. Fungi 2023, 9(1), 121; https://doi.org/10.3390/jof9010121 - 15 Jan 2023
Cited by 6 | Viewed by 2131
Abstract
Extracellular proteases belong to the main virulence factors of pathogenic fungi. Their proteolytic activities plays a crucial role in the acquisition of nutrients from the external environment, destroying host barriers and defenses, and disrupting homeostasis in the human body, e.g., by affecting the [...] Read more.
Extracellular proteases belong to the main virulence factors of pathogenic fungi. Their proteolytic activities plays a crucial role in the acquisition of nutrients from the external environment, destroying host barriers and defenses, and disrupting homeostasis in the human body, e.g., by affecting the functions of plasma proteolytic cascades, and playing sophisticated regulatory roles in various processes. Interestingly, some proteases belong to the group of moonlighting proteins, i.e., they have additional functions that contribute to successful host colonization and infection development, but they are not directly related to proteolysis. In this review, we describe examples of such multitasking of extracellular proteases that have been reported for medically important pathogenic fungi of the Candida, Aspergillus, Penicillium, Cryptococcus, Rhizopus, and Pneumocystis genera, as well as dermatophytes and selected endemic species. Additional functions of proteinases include supporting binding to host proteins, and adhesion to host cells. They also mediate self-aggregation and biofilm formation. In addition, fungal proteases affect the host immune cells and allergenicity, understood as the ability to stimulate a non-standard immune response. Finally, they play a role in the proper maintenance of cellular homeostasis. Knowledge about the multifunctionality of proteases, in addition to their canonical roles, greatly contributes to an understanding of the mechanisms of fungal pathogenicity. Full article
(This article belongs to the Special Issue Multifunctional Fungal Proteins)
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13 pages, 2020 KiB  
Review
Fungal Hal3 (and Its Close Relative Cab3) as Moonlighting Proteins
by Antonio Casamayor and Joaquín Ariño
J. Fungi 2022, 8(10), 1066; https://doi.org/10.3390/jof8101066 - 11 Oct 2022
Cited by 1 | Viewed by 1221
Abstract
Hal3 (Sis2) is a yeast protein that was initially identified as a regulatory subunit of the Saccharomyces cerevisiae Ser/Thr protein phosphatase Ppz1. A few years later, it was shown to participate in the formation of an atypical heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme, thus [...] Read more.
Hal3 (Sis2) is a yeast protein that was initially identified as a regulatory subunit of the Saccharomyces cerevisiae Ser/Thr protein phosphatase Ppz1. A few years later, it was shown to participate in the formation of an atypical heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme, thus catalyzing a key reaction in the pathway leading to Coenzyme A biosynthesis. Therefore, Hal3 was defined as a moonlighting protein. The structure of Hal3 in some fungi is made of a conserved core, similar to bacterial or mammalian PPCDCs; meanwhile, in others, the gene encodes a larger protein with N- and C-terminal extensions. In this work, we describe how Hal3 (and its close relative Cab3) participates in these disparate functions and we review recent findings that could make it possible to predict which of these two proteins will show moonlighting properties in fungi. Full article
(This article belongs to the Special Issue Multifunctional Fungal Proteins)
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