Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and Adhesion

Autor: Gisela von Hoven, Amable J. Rivas, Matthias Husmann
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: Toxins, Vol 11, Iss 7, p 412 (2019)
Druh dokumentu: article
ISSN: 2072-6651
11070412
DOI: 10.3390/toxins11070412
Popis: Phobalysin P (PhlyP, for photobacterial lysin encoded on a plasmid) is a recently described small β-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 β-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’s secretome may hold additional clues because it may lead to the identification of proteases activating PhlyP’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.
Databáze: Directory of Open Access Journals
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