{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T22:55:19Z","timestamp":1791327319014,"version":"4.3.1"},"reference-count":48,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2017,2,14]],"date-time":"2017-02-14T00:00:00Z","timestamp":1487030400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2017,3,8]],"date-time":"2017-03-08T00:00:00Z","timestamp":1488931200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100010801","name":"Xunta de Galicia","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100010801","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100004543","name":"Chinese Scholarship Council","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100004543","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2017,3,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Membrane repair emerges as an innate defense protecting target cells against bacterial pore-forming toxins. Here, we report the first paradigm of Ca\n            <jats:sup>2+<\/jats:sup>\n            -dependent repair following attack by a small \u03b2-pore-forming toxin, namely, plasmid-encoded phobalysin of\n            <jats:italic>Photobacterium damselae<\/jats:italic>\n            subsp.\n            <jats:italic>damselae<\/jats:italic>\n            . In striking contrast,\n            <jats:italic>Vibrio cholerae<\/jats:italic>\n            cytolysin, the closest ortholog of phobalysin, subverted repair. Mutational analysis uncovered a role of channel width in toxicity and repair. Thus, the replacement of serine at phobalysin\u00b4s presumed channel narrow point with the bulkier tryptophan, the corresponding residue in\n            <jats:italic>Vibrio cholerae<\/jats:italic>\n            cytolysin (W318), modulated Ca\n            <jats:sup>2+<\/jats:sup>\n            influx, lysosomal exocytosis, and membrane repair. And yet, replacing tryptophan (W318) with serine in\n            <jats:italic>Vibrio cholerae<\/jats:italic>\n            cytolysin enhanced toxicity. The data reveal divergent strategies evolved by two related small \u03b2-pore-forming toxins to manipulate target cells: phobalysin leads to fulminant perturbation of ion concentrations, closely followed by Ca\n            <jats:sup>2+<\/jats:sup>\n            influx-dependent membrane repair. In contrast,\n            <jats:italic>V.\u00a0cholerae<\/jats:italic>\n            cytolysin causes insidious perturbations and escapes control by the cellular wounded membrane repair-like response.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            Previous studies demonstrated that large transmembrane pores, such as those formed by perforin or bacterial toxins of the cholesterol-dependent cytolysin family, trigger rapid, Ca\n            <jats:sup>2+<\/jats:sup>\n            influx-dependent repair mechanisms. In contrast, recovery from attack by the small \u03b2-pore-forming\n            <jats:italic>Staphylococcus aureus<\/jats:italic>\n            alpha-toxin or aerolysin is slow in comparison and does not depend on extracellular Ca\n            <jats:sup>2+<\/jats:sup>\n            . To further elucidate the scope of Ca\n            <jats:sup>2+<\/jats:sup>\n            influx-dependent repair and understand its limitations, we compared the cellular responses to phobalysin and\n            <jats:italic>V.\u00a0cholerae<\/jats:italic>\n            cytolysin, two related small \u03b2-pore-forming toxins which create membrane pores of slightly different sizes. The data indicate that the channel width of a small \u03b2-pore-forming toxin is a critical determinant of both primary toxicity and susceptibility to Ca\n            <jats:sup>2+<\/jats:sup>\n            -dependent repair.\n          <\/jats:p>","DOI":"10.1128\/mbio.02083-16","type":"journal-article","created":{"date-parts":[[2017,2,15]],"date-time":"2017-02-15T01:10:19Z","timestamp":1487121019000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":20,"title":["Repair of a Bacterial Small \u03b2-Barrel Toxin Pore Depends on Channel Width"],"prefix":"10.1128","volume":"8","author":[{"given":"Gisela","family":"von Hoven","sequence":"first","affiliation":[{"name":"Institute of Medical Microbiology and Hygiene, University Medical Center, Johannes Gutenberg University, Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amable J.","family":"Rivas","sequence":"additional","affiliation":[{"name":"Institute of Medical Microbiology and Hygiene, University Medical Center, Johannes Gutenberg University, Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudia","family":"Neukirch","sequence":"additional","affiliation":[{"name":"Institute of Medical Microbiology and Hygiene, University Medical Center, Johannes Gutenberg University, Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martina","family":"Meyenburg","sequence":"additional","affiliation":[{"name":"Institute of Medical Microbiology and Hygiene, University Medical Center, Johannes Gutenberg University, Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qianqian","family":"Qin","sequence":"additional","affiliation":[{"name":"Institute of Medical Microbiology and Hygiene, University Medical Center, Johannes Gutenberg University, Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sapun","family":"Parekh","sequence":"additional","affiliation":[{"name":"Max Planck Institute for Polymer Research, Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nadja","family":"Hellmann","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biophysics, Faculty of Biology, Johannes Gutenberg University Mainz, Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias","family":"Husmann","sequence":"additional","affiliation":[{"name":"Institute of Medical Microbiology and Hygiene, University Medical Center, Johannes Gutenberg University, Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0882-4010(86)90027-6"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2012.04.006"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.52.1.50-55.1986"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1113380"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.chom.2012.08.005"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(83)90069-7"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1006\/mpat.1994.1065"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.051429498"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2014.09.005"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2011.01600.x"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.chom.2011.01.005"},{"key":"e_1_3_2_13_2","first-page":"195","article-title":"Calcium and wound healing in Xenopus early embryos","volume":"67","author":"Stanisstreet M","year":"1982","unstructured":"Stanisstreet M . 1982. 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