Pichia Anomala DBVPG 3003 Secretes a Ubiquitin-like Protein That Has Antimicrobial Activity

Overview

Journal Appl Environ Microbiol

Specialties Environmental Health
Microbiology

Date 2008 Dec 31

PMID 19114528

Citations 13

Authors

Jessica De Ingeniis

Nadia Raffaelli

Maurizio Ciani

Ilaria Mannazzu

Affiliations

Soon will be listed here.

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.

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