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Authors: Hoven, Gisela von
Rivas, Amable J.
Husmann, Matthias
Title: Phobalysin: fisheye view of membrane perforation, repair, chemotaxis and adhesion
Online publication date: 8-Nov-2019
Year of first publication: 2019
Language: english
Abstract: Phobalysin P (PhlyP, for photobacterial lysin encoded on a plasmid) is a recently described small %26beta;-pore forming toxin of Photobacterium damselae subsp. damselae (Pdd). This organism, belonging to the family of Vibrionaceae, is an emerging pathogen of fish and various marine animals, which occasionally causes life-threatening soft tissue infections and septicemia in humans. By using genetically modified Pdd strains, PhlyP was found to be an important virulence factor. More recently, in vitro studies with purified PhlyP elucidated some basic consequences of pore formation. Being the first bacterial small %26beta;-pore forming toxin shown to trigger calcium-influx dependent membrane repair, PhlyP has advanced to a revealing model toxin to study this important cellular function. Further, results from co-culture experiments employing various Pdd strains and epithelial cells together with data on other bacterial toxins indicate that limited membrane damage may generally enhance the association of bacteria with target cells. Thereby, remodeling of plasma membrane and cytoskeleton during membrane repair could be involved. In addition, a chemotaxis-dependent attack-and track mechanism influenced by environmental factors like salinity may contribute to PhlyP-dependent association of Pdd with cells. Obviously, a synoptic approach is required to capture the regulatory links governing the interaction of Pdd with target cells. The characterization of Pdd%26rsquo;s secretome may hold additional clues because it may lead to the identification of proteases activating PhlyP%26rsquo;s pro-form. Current findings on PhlyP support the notion that pore forming toxins are not just killer proteins but serve bacteria to fulfill more subtle functions, like accessing their host.
DDC: 610 Medizin
610 Medical sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 04 Medizin
Place: Mainz
URN: urn:nbn:de:hebis:77-publ-594084
Version: Published version
Publication type: Zeitschriftenaufsatz
License: CC BY
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Journal: Toxins
Pages or article number: Art. 412
Publisher: MDPI
Publisher place: Basel
Issue date: 2019
ISSN: 2072-6651
Publisher URL:
Publisher DOI: 10.3390/toxins11070412
Appears in collections:JGU-Publikationen

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