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Abstract Detail


Lovett, Brian [1], Gandier, Julie-Anne [2], Kasson, Matt [1].

Cataloging the diversity of hydrophobins and hydrophobin-like proteins.

Hydrophobin proteins are reliably found at the surface of fungal spores assembled into remarkably stable structured coatings that mediate interactions between air-water and, in certain cases, confer non-immunogenic properties. However, the careful characterization of a number of hydrophobins in model organisms (e.g., Aspergillus sp., Neurospora crassa, Trichoderma reesei) reveals a spectrum of properties which allow the fungi to modulate not only their own hydrophobicity and wettability (e.g., coating aerial hyphae), but that of their environment (e.g., interacting with plant surfaces, modulating surface tension of liquids and adhesion to surfaces). The hydrophobin family's functional plasticity is reflected in the limited conservation of their protein sequences. Defined in the literature as exclusively secreted and typically short (~150 AA long), members are identified by a pattern of eight cysteines (C-CC-C-C-CC-C) whose relative spacing can vary significantly. This presents a challenge for identifying and comparing hydrophobins across an entire genome. Considering the watery origins of fungi, hydrophobins may represent a fundamental evolutionary innovation for fungi, and are generally thought to have an ancient origin. Yet, the timing of the emergence of this protein family has not been established. The diversity of hydrophobins across fungi and the gains and losses within specific fungi will provide fundamental insights into fungal ecology and evolution. Accordingly, here we report on our work to catalog what is known and expand the known universe of hydrophobins. Fungal genomes are increasingly available, and we have assembled a database of over 50 genomes, including early divergent fungi, fungi with diverse lifestyles and informative outgroups (e.g., slime molds and Streptomyces coelicolor). Using typical alignment-based methods and by searching for structural amino acid motifs-that take into consideration the particular challenges associated with searching for hydrophobin-like sequences-we have identified hundreds of hydrophobin and hydrophobin-like candidates. In many of these fungi, we have identified candidates that are not captured by "traditional models", and so have been overlooked by scientific study. We will uncover the evolutionary relationships among our candidate proteins and consider them in the context of each of their ecological niches. This work aims to establish a comprehensive catalog of hydrophobins and hydrophobin-like proteins across the fungal kingdom to guide the identification, classification and study of these proteins in the future.

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1 - West Virginia University
2 - Aalto University

Fungal diversity

Presentation Type: Oral Paper
Session: MY4, Mycology: Endophytes, Communities, Hydrophobins, and Transporters
Location: /
Date: Wednesday, July 21st, 2021
Time: 12:30 PM(EDT)
Number: MY4001
Abstract ID:879
Candidate for Awards:None

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