Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and Adhesion
Phobalysin P (PhlyP, for photobacterial lysin encoded on a plasmid) is a recently described small β-pore forming toxin of <i>Photobacterium damselae</i> subsp. <i>damselae (Pdd).</i> This organism, belonging to the family of <i>Vibrionaceae,</i> is an eme...
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| Format: | Article |
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MDPI AG
2019-07-01
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| Series: | Toxins |
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| Online Access: | https://www.mdpi.com/2072-6651/11/7/412 |
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| author | Gisela von Hoven Amable J. Rivas Matthias Husmann |
| author_facet | Gisela von Hoven Amable J. Rivas Matthias Husmann |
| author_sort | Gisela von Hoven |
| collection | DOAJ |
| description | Phobalysin P (PhlyP, for photobacterial lysin encoded on a plasmid) is a recently described small β-pore forming toxin of <i>Photobacterium damselae</i> subsp. <i>damselae (Pdd).</i> This organism, belonging to the family of <i>Vibrionaceae,</i> 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 <i>Pdd</i> 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 <i>Pdd</i> 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 <i>attack-and track</i> mechanism influenced by environmental factors like salinity may contribute to PhlyP-dependent association of <i>Pdd</i> with cells. Obviously, a synoptic approach is required to capture the regulatory links governing the interaction of <i>Pdd</i> with target cells. The characterization of <i>Pdd’s</i> 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. |
| first_indexed | 2024-04-11T11:03:02Z |
| format | Article |
| id | doaj.art-7ddc4e4202de483aae822ed1eb5f925d |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-04-11T11:03:02Z |
| publishDate | 2019-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-7ddc4e4202de483aae822ed1eb5f925d2022-12-22T04:28:29ZengMDPI AGToxins2072-66512019-07-0111741210.3390/toxins11070412toxins11070412Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and AdhesionGisela von Hoven0Amable J. Rivas1Matthias Husmann2Institute of Medical Microbiology and Hygiene, University Medical Center, Johannes Gutenberg-University, 55128 Mainz, GermanyInstitute of Medical Microbiology and Hygiene, University Medical Center, Johannes Gutenberg-University, 55128 Mainz, GermanyInstitute of Medical Microbiology and Hygiene, University Medical Center, Johannes Gutenberg-University, 55128 Mainz, GermanyPhobalysin P (PhlyP, for photobacterial lysin encoded on a plasmid) is a recently described small β-pore forming toxin of <i>Photobacterium damselae</i> subsp. <i>damselae (Pdd).</i> This organism, belonging to the family of <i>Vibrionaceae,</i> 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 <i>Pdd</i> 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 <i>Pdd</i> 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 <i>attack-and track</i> mechanism influenced by environmental factors like salinity may contribute to PhlyP-dependent association of <i>Pdd</i> with cells. Obviously, a synoptic approach is required to capture the regulatory links governing the interaction of <i>Pdd</i> with target cells. The characterization of <i>Pdd’s</i> 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.https://www.mdpi.com/2072-6651/11/7/412<i>Photobacterium damselae </i>subsp. <i>damselae</i>phobalysinpore forming toxinmembrane repairadhesionchemotaxis |
| spellingShingle | Gisela von Hoven Amable J. Rivas Matthias Husmann Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and Adhesion Toxins <i>Photobacterium damselae </i>subsp. <i>damselae</i> phobalysin pore forming toxin membrane repair adhesion chemotaxis |
| title | Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and Adhesion |
| title_full | Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and Adhesion |
| title_fullStr | Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and Adhesion |
| title_full_unstemmed | Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and Adhesion |
| title_short | Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and Adhesion |
| title_sort | phobalysin fisheye view of membrane perforation repair chemotaxis and adhesion |
| topic | <i>Photobacterium damselae </i>subsp. <i>damselae</i> phobalysin pore forming toxin membrane repair adhesion chemotaxis |
| url | https://www.mdpi.com/2072-6651/11/7/412 |
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