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Pathogens
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Fungal Cell Adhesion Proteins: Structure, Function, and Roles in Disease
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Fungal Cell Adhesion Proteins: Structure, Function, and Roles in Disease

A special issue of Pathogens (ISSN 2076-0817). This special issue belongs to the section "Fungal Pathogens".

Deadline for manuscript submissions: closed (1 September 2021) | Viewed by 11769

Special Issue Editor

Prof. Dr. Peter N. Lipke

E-Mail Website
Guest Editor
Biology Department, City University of New York Brooklyn College, Brooklyn, NY 11210, USA
Interests: role of functional amyloids in cell adhesion; structure and function of cell adhesion proteins in eukaryotes; role of fungal cell adhesion proteins in pathogenesis; structure, evolution, and biosynthesis of fungal cell walls; discovery of wall-targeted antifungal drugs
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Fungal adhesion proteins are key players in pathogenesis through attachment, aggregation with other fungal cells and bacteria, biofilm formation, and modulation of immune responses. This Special Issue will follow up on a 2018 issue of J. of Fungi that discussed the role of cell adhesion in fungal lifestyle. This new Special Issue of Pathogens will explore the structure–function relationships among adhesins and also describe new approaches to studying these large and complex gycoproteins. We welcome submissions on all aspects of the structure and activities of adhesins, including Candida, Crytococcus, Aspergillus, and other fungal pathogens.

We hope you will participate by submitting a high-quality research paper or review article for inclusion in this Special Issue.

References：

Lipke, P.N.; Klotz, S.A.; Dufrene, Y.F.; Jackson, D.N.; Garcia-Sherman, M.C. Amyloid-like β-Aggregates as Force-sensitive Switches in Fungal Biofilms and Infections. Microbiol. Molec. Biol. Reviews 2018, 82:e00035-17. Available online: https://doi.org/10.1128/MMBR.00035-17. PMID:29187516 PMC5813885 [Cover illustration].

Lipke, P.N. What we do not know about fungal cell adhesion proteins. J. Fungi 2018, 4, 59, doi:10.3390/jof4020059. PMID: 29772751 PMC6023273

Willaert, R.G. Adhesins of Yeasts: Protein Structure and Interactions. J Fungi (Basel) 2018, 4, E119. doi: 10.3390/jof4040119. Review. PMID: 30373267

Prof. Dr. Peter N. Lipke
Guest Editor

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. Pathogens 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 2700 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

  • Cell wall
  • Fungal biofilm
  • Fungal adhesion
  • Glycoprotein
  • Ligand
  • Homotypic binding
  • Heterotypic binding
  • GPI
  • Lectin
  • Atomic Force Microscope (AFM)
  • Cryoelectron microscopy

Published Papers (4 papers)

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Research

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17 pages, 1246 KiB  
Article
High Biofilm Formation of Non-Smooth Candida parapsilosis Correlates with Increased Incorporation of GPI-Modified Wall Adhesins
by Ana Esther Moreno-Martínez, Emilia Gómez-Molero, Pablo Sánchez-Virosta, Henk L. Dekker, Albert de Boer, Elena Eraso, Oliver Bader and Piet W. J. de Groot
Pathogens 2021, 10(4), 493; https://doi.org/10.3390/pathogens10040493 - 19 Apr 2021
Cited by 7 | Viewed by 2076
Abstract
Candida parapsilosis is among the most frequent causes of candidiasis. Clinical isolates of this species show large variations in colony morphotype, ranging from round and smooth to a variety of non-smooth irregular colony shapes. A non-smooth appearance is related to increased formation of [...] Read more.
Candida parapsilosis is among the most frequent causes of candidiasis. Clinical isolates of this species show large variations in colony morphotype, ranging from round and smooth to a variety of non-smooth irregular colony shapes. A non-smooth appearance is related to increased formation of pseudohyphae, higher capacity to form biofilms on abiotic surfaces, and invading agar. Here, we present a comprehensive study of the cell wall proteome of C. parapsilosis reference strain CDC317 and seven clinical isolates under planktonic and sessile conditions. This analysis resulted in the identification of 40 wall proteins, most of them homologs of known Candida albicans cell wall proteins, such as Gas, Crh, Bgl2, Cht2, Ecm33, Sap, Sod, Plb, Pir, Pga30, Pga59, and adhesin family members. Comparative analysis of exponentially growing and stationary phase planktonic cultures of CDC317 at 30 °C and 37 °C revealed only minor variations. However, comparison of smooth isolates to non-smooth isolates with high biofilm formation capacity showed an increase in abundance and diversity of putative wall adhesins from Als, Iff/Hyr, and Hwp families in the latter. This difference depended more strongly on strain phenotype than on the growth conditions, as it was observed in planktonic as well as biofilm cells. Thus, in the set of isolates analyzed, the high biofilm formation capacity of non-smooth C. parapsilosis isolates with elongated cellular phenotypes correlates with the increased surface expression of putative wall adhesins in accordance with their proposed cellular function. Full article
(This article belongs to the Special Issue Fungal Cell Adhesion Proteins: Structure, Function, and Roles in Disease)
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Review

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16 pages, 891 KiB  
Review
FLO11, a Developmental Gene Conferring Impressive Adaptive Plasticity to the Yeast Saccharomyces cerevisiae
by Clara Bouyx, Marion Schiavone and Jean Marie François
Pathogens 2021, 10(11), 1509; https://doi.org/10.3390/pathogens10111509 - 19 Nov 2021
Cited by 8 | Viewed by 3303
Abstract
The yeast Saccharomyces cerevisiae has a remarkable ability to adapt its lifestyle to fluctuating or hostile environmental conditions. This adaptation most often involves morphological changes such as pseudofilaments, biofilm formation, or cell aggregation in the form of flocs. A prerequisite for these phenotypic [...] Read more.
The yeast Saccharomyces cerevisiae has a remarkable ability to adapt its lifestyle to fluctuating or hostile environmental conditions. This adaptation most often involves morphological changes such as pseudofilaments, biofilm formation, or cell aggregation in the form of flocs. A prerequisite for these phenotypic changes is the ability to self-adhere and to adhere to abiotic surfaces. This ability is conferred by specialized surface proteins called flocculins, which are encoded by the FLO genes family in this yeast species. This mini-review focuses on the flocculin encoded by FLO11, which differs significantly from other flocculins in domain sequence and mode of genetic and epigenetic regulation, giving it an impressive plasticity that enables yeast cells to swiftly adapt to hostile environments or into new ecological niches. Furthermore, the common features of Flo11p with those of adhesins from pathogenic yeasts make FLO11 a good model to study the molecular mechanism underlying cell adhesion and biofilm formation, which are part of the initial step leading to fungal infections. Full article
(This article belongs to the Special Issue Fungal Cell Adhesion Proteins: Structure, Function, and Roles in Disease)
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39 pages, 10552 KiB  
Review
The Flo Adhesin Family
by Ronnie G. Willaert, Yeseren Kayacan and Bart Devreese
Pathogens 2021, 10(11), 1397; https://doi.org/10.3390/pathogens10111397 - 28 Oct 2021
Cited by 12 | Viewed by 2701
Abstract
The first step in the infection of fungal pathogens in humans is the adhesion of the pathogen to host tissue cells or abiotic surfaces such as catheters and implants. One of the main players involved in this are the expressed cell wall adhesins. [...] Read more.
The first step in the infection of fungal pathogens in humans is the adhesion of the pathogen to host tissue cells or abiotic surfaces such as catheters and implants. One of the main players involved in this are the expressed cell wall adhesins. Here, we review the Flo adhesin family and their involvement in the adhesion of these yeasts during human infections. Firstly, we redefined the Flo adhesin family based on the domain architectures that are present in the Flo adhesins and their functions, and set up a new classification of Flo adhesins. Next, the structure, function, and adhesion mechanisms of the Flo adhesins whose structure has been solved are discussed in detail. Finally, we identified from Pfam database datamining yeasts that could express Flo adhesins and are encountered in human infections and their adhesin architectures. These yeasts are discussed in relation to their adhesion characteristics and involvement in infections. Full article
(This article belongs to the Special Issue Fungal Cell Adhesion Proteins: Structure, Function, and Roles in Disease)
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11 pages, 4600 KiB  
Review
A New Function for Amyloid-Like Interactions: Cross-Beta Aggregates of Adhesins form Cell-to-Cell Bonds
by Peter N. Lipke, Marion Mathelié-Guinlet, Albertus Viljoen and Yves F. Dufrêne
Pathogens 2021, 10(8), 1013; https://doi.org/10.3390/pathogens10081013 - 11 Aug 2021
Cited by 11 | Viewed by 2858
Abstract
Amyloid structures assemble through a repeating type of bonding called “cross-β”, in which identical sequences in many protein molecules form β-sheets that interdigitate through side chain interactions. We review the structural characteristics of such bonds. Single cell force microscopy (SCFM) shows that yeast [...] Read more.
Amyloid structures assemble through a repeating type of bonding called “cross-β”, in which identical sequences in many protein molecules form β-sheets that interdigitate through side chain interactions. We review the structural characteristics of such bonds. Single cell force microscopy (SCFM) shows that yeast expressing Als5 adhesin from Candida albicans demonstrate the empirical characteristics of cross-β interactions. These properties include affinity for amyloid-binding dyes, birefringence, critical concentration dependence, repeating structure, and inhibition by anti-amyloid agents. We present a model for how cross-β bonds form in trans between two adhering cells. These characteristics also apply to other fungal adhesins, so the mechanism appears to be an example of a new type of cell–cell adhesion. Full article
(This article belongs to the Special Issue Fungal Cell Adhesion Proteins: Structure, Function, and Roles in Disease)
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