Related Experiment Video
Updated: Jun 26, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
Published on: January 2, 2026
Pichia anomala DBVPG 3003 secretes a ubiquitin-like protein that has antimicrobial activity
Jessica De Ingeniis1, Nadia Raffaelli, Maurizio Ciani
1Istituto di Biotecnologie Biochimiche, Università Politecnica delle Marche, Via Ranieri, 60131 Ancona, Italy.
Abstract:
The yeast strain Pichia anomala DBVPG 3003 secretes a killer toxin (Pikt) that has antifungal activity against Brettanomyces/Dekkera sp. yeasts. Pikt interacts with beta-1,6-glucan, consistent with binding to the cell wall of sensitive targets. In contrast to that of toxin K1, secreted by Saccharomyces cerevisiae, Pikt killer activity is not mediated by an increase in membrane permeability. Purification of the toxin yielded a homogeneous protein of about 8 kDa, which showed a marked similarity to ubiquitin in terms of molecular mass and N-terminal sequences. Pikt is also specifically recognized by anti-bovine ubiquitin antibodies and, similar to ubiquitin-like peptides, is not absorbed by DEAE-cellulose. However, Pikt differs from ubiquitin in its sensitivity to proteolytic enzymes. Therefore, Pikt appears to be a novel ubiquitin-like peptide that has killer activity.
Insights
Pichia anomala DBVPG 3003 secretes a novel antifungal peptide, Pikt, similar to ubiquitin. This Pikt peptide exhibits killer activity against Brettanomyces/Dekkera yeasts by interacting with their cell walls.
Area of Science:
- Microbiology
- Mycology
- Biochemistry
Background:
- Brettanomyces/Dekkera yeasts are spoilage organisms in winemaking.
- Pichia anomala produces a killer toxin (Pikt) with antifungal properties.
- Understanding Pikt's mechanism is crucial for controlling yeast spoilage.
Purpose of the Study:
- To characterize the Pichia anomala killer toxin (Pikt).
- To investigate the molecular properties and activity of Pikt.
- To determine if Pikt is related to known yeast toxins or peptides.
Main Methods:
- Purification of Pikt from Pichia anomala culture supernatant.
- Analysis of Pikt's interaction with yeast cell walls (beta-1,6-glucan).
- Comparison of Pikt's molecular mass, N-terminal sequences, and antibody recognition with ubiquitin.
Main Results:
- Pikt has antifungal activity against Brettanomyces/Dekkera yeasts.
- Pikt binds to beta-1,6-glucan in the cell wall of sensitive yeasts.
- Purified Pikt is an 8 kDa protein, similar to ubiquitin in mass and sequence, but sensitive to proteases.
Conclusions:
- Pikt is a novel ubiquitin-like peptide with killer activity.
- Pikt's antifungal mechanism differs from Saccharomyces cerevisiae toxin K1.
- Pikt represents a new class of antifungal agents potentially useful in controlling spoilage yeasts.
More Related Videos
13:34Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
09:26Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis
Published on: May 23, 2021
Related Concept Videos
Gene Regulation in Microbial Communities: Quorum Sensing
Antimicrobial Proteins
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Archaeal Cell Wall
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...