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Special Issue "Protein Engineering of Yeast"

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SUNY Downstate Health Sciences, New York, NY, USA
Interests: membrane repair; molecular chaperones; protein trafficking and secretion; fibroblast growth factors; oxidative stress; yeast; Saccharomyces cerevisiae

Special Issue Information

Dear Colleagues,

Protein engineering is the purposeful modification of a protein’s sequence, structure, or expression. In a simple example, one’s favorite protein may be altered to facilitate the overexpression of a tagged version in yeast, which generates large quantities of yeast for in vitro investigations. In more complex cases, several foreign enzymes may be expressed in yeast to create a robust metabolic pathway for producing, for example, biofuels or medicines. Bioengineered yeasts have also been used for vaccine development, reprogramming a protein's fate, directed evolution, and protein-based library screening. This Special Issue will highlight the versatility and power of yeast as a platform for protein engineering. Papers describing research using all yeast species are welcome, including Saccharomyces cerevisiae, Cryptococcus neoformans, Pichia pastoris, and Yarrowia lipolytica.

Prof. Dr. William J. Chirico
Guest Editor

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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.

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Keywords

draft-protein engineering
overexpression, mutation
cell surface expression
vaccine development
evolution
drug development
surface biosensors
pathway modeling
yeast

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Research

Open AccessEditor’s ChoiceArticle

Functional Expression of Recombinant Candida auris Proteins in Saccharomyces cerevisiae Enables Azole Susceptibility Evaluation and Drug Discovery

and

J. Fungi 2023, 9(2), 168; https://doi.org/10.3390/jof9020168 - 27 Jan 2023

Cited by 2 | Viewed by 1302

Abstract

Candida auris infections are difficult to treat due to acquired drug resistance against one or multiple antifungal drug classes. The most prominent resistance mechanisms in C. auris are overexpression and point mutations in Erg11, and the overexpression of efflux pump genes CDR1 and MDR1. We report the establishment of a novel platform for molecular analysis and drug screening based on acquired azole-resistance mechanisms found in C. auris. Constitutive functional overexpression of wild-type C. auris Erg11, Erg11 with amino acid substitutions Y132F or K143R and the recombinant efflux pumps Cdr1 and Mdr1 has been achieved in Saccharomyces cerevisiae. Phenotypes were evaluated for standard azoles and the tetrazole VT-1161. Overexpression of CauErg11 Y132F, CauErg11 K143R, and CauMdr1 conferred resistance exclusively to the short-tailed azoles Fluconazole and Voriconazole. Strains overexpressing the Cdr1 protein were pan-azole resistant. While CauErg11 Y132F increased VT-1161 resistance, K143R had no impact. Type II binding spectra showed tight azole binding to the affinity-purified recombinant CauErg11 protein. The Nile Red assay confirmed the efflux functions of CauMdr1 and CauCdr1, which were specifically inhibited by MCC1189 and Beauvericin, respectively. CauCdr1 exhibited ATPase activity that was inhibited by Oligomycin. The S. cerevisiae overexpression platform enables evaluation of the interaction of existing and novel azole drugs with their primary target CauErg11 and their susceptibility to drug efflux. Full article

(This article belongs to the Special Issue Protein Engineering of Yeast)

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Open AccessArticle

Recombinant Expression in Pichia pastoris System of Three Potent Kv1.3 Channel Blockers: Vm24, Anuroctoxin, and Ts6

Jesús Borrego

Muhammad Umair Naseem

Al Nasar Ahmed Sehgal

and

J. Fungi 2022, 8(11), 1215; https://doi.org/10.3390/jof8111215 - 17 Nov 2022

Cited by 1 | Viewed by 1567

Abstract

The Kv1.3 channel has become a therapeutic target for the treatment of various diseases. Several Kv1.3 channel blockers have been characterized from scorpion venom; however, extensive studies require amounts of toxin that cannot be readily obtained directly from venoms. The Pichia pastoris expression system provides a cost-effective approach to overcoming the limitations of chemical synthesis and E. coli recombinant expression. In this work, we developed an efficient system for the production of three potent Kv1.3 channel blockers from different scorpion venoms: Vm24, AnTx, and Ts6. Using the Pichia system, these toxins could be obtained in sufficient quantities (Vm24 1.6 mg/L, AnTx 46 mg/L, and Ts6 7.5 mg/L) to characterize their biological activity. A comparison was made between the activity of tagged and untagged recombinant peptides. Tagged Vm24 and untagged AnTx are nearly equivalent to native toxins in blocking Kv1.3 (Kd = 4.4 pM and Kd = 0.72 nM, respectively), whereas untagged Ts6 exhibits a 53-fold increase in Kd (Kd = 29.1 nM) as compared to the native peptide. The approach described here provides a method that can be optimized for toxin production to develop more selective and effective Kv1.3 blockers with therapeutic potential. Full article

(This article belongs to the Special Issue Protein Engineering of Yeast)

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Special Issue "Protein Engineering of Yeast"

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