{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T13:05:10Z","timestamp":1788354310941,"version":"build-2803163510"},"reference-count":156,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2019,7,19]],"date-time":"2019-07-19T00:00:00Z","timestamp":1563494400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Microbiol Spectr"],"published-print":{"date-parts":[[2019,7,19]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The pathogenesis of clostridial myonecrosis or gas gangrene involves an interruption to the blood supply to the infected tissues, often via a traumatic wound, anaerobic growth of the infecting clostridial cells, the production of extracellular toxins, and toxin-mediated cell and tissue damage. This review focuses on host-pathogen interactions in\n            <jats:italic>Clostridium perfringens<\/jats:italic>\n            -mediated and\n            <jats:italic>Clostridium septicum<\/jats:italic>\n            -mediated myonecrosis. The major toxins involved are\n            <jats:italic>C. perfringens<\/jats:italic>\n            \u03b1-toxin, which has phospholipase C and sphingomyelinase activity, and\n            <jats:italic>C. septicum<\/jats:italic>\n            \u03b1-toxin, a \u03b2-pore-forming toxin that belongs to the aerolysin family. Although these toxins are cytotoxic, their effects on host cells are quite complex, with a range of intracellular cell signaling pathways induced by their action on host cell membranes.\n          <\/jats:p>","DOI":"10.1128\/microbiolspec.gpp3-0024-2018","type":"journal-article","created":{"date-parts":[[2019,7,27]],"date-time":"2019-07-27T12:45:32Z","timestamp":1564231532000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":27,"title":["Histotoxic Clostridial Infections"],"prefix":"10.1128","volume":"7","author":[{"given":"Masahiro","family":"Nagahama","sequence":"first","affiliation":[{"name":"Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Yamashiro-cho, Tokushima 770-8514, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masaya","family":"Takehara","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Yamashiro-cho, Tokushima 770-8514, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julian I.","family":"Rood","sequence":"additional","affiliation":[{"name":"Infection and Immunity Program, Monash Biomedicine Discovery Institute and Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Aldape MJ Bryant AE. 2012. Life-threatening clostridial infections. Anaerobe 18: 254\u2013259 http:\/\/dx.doi.org\/10.1016\/j.anaerobe.2011.11.001. [PubMed]","DOI":"10.1016\/j.anaerobe.2011.11.001"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Bryant AE. 2017. Necrotizing soft-tissue infections. N Engl J Med 377: 2253\u20132265 http:\/\/dx.doi.org\/10.1056\/NEJMra1600673. [PubMed]","DOI":"10.1056\/NEJMra1600673"},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Musher DM Watson DA Eddy H Hamill RJ Gyorkey F Rosen H Mader J. 1990. Spontaneous nontraumatic gangrene due to Clostridium septicum . Rev Infect Dis 12: 286\u2013296 http:\/\/dx.doi.org\/10.1093\/clinids\/12.2.286.","DOI":"10.1093\/clinids\/12.2.286"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","unstructured":"Srivastava I Aldape MJ Bryant AE Stevens DL. 2017. Spontaneous C. septicum gas gangrene: a literature review. Anaerobe 48: 165\u2013171 http:\/\/dx.doi.org\/10.1016\/j.anaerobe.2017.07.008. [PubMed]","DOI":"10.1016\/j.anaerobe.2017.07.008"},{"key":"e_1_3_2_6_2","doi-asserted-by":"crossref","unstructured":"Kimura AC Higa JI Levin RM Simpson G Vargas Y Vugia DJ. 2004. Outbreak of necrotizing fasciitis due to Clostridium sordellii among black-tar heroin users. Clin Infect Dis 38: e87\u2013e91 http:\/\/dx.doi.org\/10.1086\/383471. [PubMed]","DOI":"10.1086\/383471"},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","unstructured":"Assadian O Assadian A Senekowitsch C Makristathis A Hagm\u00fcller G. 2004. Gas gangrene due to Clostridium perfringens in two injecting drug users in Vienna Austria. Wien Klin Wochenschr 116: 264\u2013267 http:\/\/dx.doi.org\/10.1007\/BF03041058. [PubMed]","DOI":"10.1007\/BF03041058"},{"key":"e_1_3_2_8_2","doi-asserted-by":"crossref","unstructured":"Gonzales y Tucker RD Frazee B. 2014. View from the front lines: an emergency medicine perspective on clostridial infections in injection drug users. Anaerobe 30: 108\u2013115 http:\/\/dx.doi.org\/10.1016\/j.anaerobe.2014.09.005. [PubMed]","DOI":"10.1016\/j.anaerobe.2014.09.005"},{"key":"e_1_3_2_9_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Rood JI. 2006. Histotoxic clostridia p 715\u2013725. In Fischetti VA Novick RP Ferretti JJ Portnoy DA Rood JI (ed) Gram-Positive Pathogens 2nd ed. ASM Press Washington DC. http:\/\/dx.doi.org\/10.1128\/9781555816513.ch58","DOI":"10.1128\/9781555816513.ch58"},{"key":"e_1_3_2_10_2","doi-asserted-by":"crossref","unstructured":"Ohtani K. 2016. Gene regulation by the VirS\/VirR system in Clostridium perfringens . Anaerobe 41: 5\u20139 http:\/\/dx.doi.org\/10.1016\/j.anaerobe.2016.06.003. [PubMed]","DOI":"10.1016\/j.anaerobe.2016.06.003"},{"key":"e_1_3_2_11_2","doi-asserted-by":"crossref","unstructured":"Ohtani K Yuan Y Hassan S Wang R Wang Y Shimizu T. 2009. Virulence gene regulation by the agr system in Clostridium perfringens . J Bacteriol 191: 3919\u20133927 http:\/\/dx.doi.org\/10.1128\/JB.01455-08. [PubMed]","DOI":"10.1128\/JB.01455-08"},{"key":"e_1_3_2_12_2","doi-asserted-by":"crossref","unstructured":"Ma M Li J McClane BA. 2015. Structure-function analysis of peptide signaling in the Clostridium perfringens Agr-like quorum sensing system. J Bacteriol 197: 1807\u20131818 http:\/\/dx.doi.org\/10.1128\/JB.02614-14. [PubMed]","DOI":"10.1128\/JB.02614-14"},{"key":"e_1_3_2_13_2","doi-asserted-by":"crossref","unstructured":"Titball R Rood J. 2000. Bacterial phospholipases p 529\u2013556. In Aktories K Just I (ed) Bacterial Protein Toxins . Springer Berlin Germany. http:\/\/dx.doi.org\/10.1007\/978-3-662-05971-5_23","DOI":"10.1007\/978-3-662-05971-5_23"},{"key":"e_1_3_2_14_2","doi-asserted-by":"crossref","unstructured":"Macfarlane MG Knight BCJG. 1941. The biochemistry of bacterial toxins: the lecithinase activity of Cl. welchii toxins. Biochem J 35: 884\u2013902 http:\/\/dx.doi.org\/10.1042\/bj0350884. [PubMed]","DOI":"10.1042\/bj0350884"},{"key":"e_1_3_2_15_2","doi-asserted-by":"crossref","unstructured":"Williamson ED Titball RW. 1993. A genetically engineered vaccine against the alpha-toxin of Clostridium perfringens protects mice against experimental gas gangrene. Vaccine 11: 1253\u20131258 http:\/\/dx.doi.org\/10.1016\/0264-410X(93)90051-X.","DOI":"10.1016\/0264-410X(93)90051-X"},{"key":"e_1_3_2_16_2","doi-asserted-by":"crossref","unstructured":"Awad MM Bryant AE Stevens DL Rood JI. 1995. Virulence studies on chromosomal \u03b1-toxin and \u03b8-toxin mutants constructed by allelic exchange provide genetic evidence for the essential role of \u03b1-toxin in Clostridium perfringens -mediated gas gangrene. Mol Microbiol 15: 191\u2013202 http:\/\/dx.doi.org\/10.1111\/j.1365-2958.1995.tb02234.x. [PubMed]","DOI":"10.1111\/j.1365-2958.1995.tb02234.x"},{"key":"e_1_3_2_17_2","doi-asserted-by":"crossref","unstructured":"Tweten RK. 2005. Cholesterol-dependent cytolysins a family of versatile pore-forming toxins. Infect Immun 73: 6199\u20136209 http:\/\/dx.doi.org\/10.1128\/IAI.73.10.6199-6209.2005. [PubMed]","DOI":"10.1128\/IAI.73.10.6199-6209.2005"},{"key":"e_1_3_2_18_2","doi-asserted-by":"crossref","unstructured":"Gilbert RJ. 2010. Cholesterol-dependent cytolysins. Adv Exp Med Biol 677: 56\u201366 http:\/\/dx.doi.org\/10.1007\/978-1-4419-6327-7_5. [PubMed]","DOI":"10.1007\/978-1-4419-6327-7_5"},{"key":"e_1_3_2_19_2","doi-asserted-by":"crossref","unstructured":"Awad MM Rood JI. 1997. Isolation of \u03b1-toxin \u03b8-toxin and \u03ba-toxin mutants of Clostridium perfringens by Tn 916 mutagenesis. Microb Pathog 22: 275\u2013284 http:\/\/dx.doi.org\/10.1006\/mpat.1996.0115. [PubMed]","DOI":"10.1006\/mpat.1996.0115"},{"key":"e_1_3_2_20_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Tweten RK Awad MM Rood JI Bryant AE. 1997. Clostridial gas gangrene: evidence that \u03b1 and \u03b8 toxins differentially modulate the immune response and induce acute tissue necrosis. J Infect Dis 176: 189\u2013195 http:\/\/dx.doi.org\/10.1086\/514022. [PubMed]","DOI":"10.1086\/514022"},{"key":"e_1_3_2_21_2","doi-asserted-by":"crossref","unstructured":"Awad MM Ellemor DM Boyd RL Emmins JJ Rood JI. 2001. Synergistic effects of \u03b1-toxin and perfringolysin O in Clostridium perfringens -mediated gas gangrene. Infect Immun 69: 7904\u20137910 http:\/\/dx.doi.org\/10.1128\/IAI.69.12.7904-7910.2001. [PubMed]","DOI":"10.1128\/IAI.69.12.7904-7910.2001"},{"key":"e_1_3_2_22_2","doi-asserted-by":"crossref","unstructured":"Ellemor DM Baird RN Awad MM Boyd RL Rood JI Emmins JJ. 1999. Use of genetically manipulated strains of Clostridium perfringens reveals that both alpha-toxin and theta-toxin are required for vascular leukostasis to occur in experimental gas gangrene. Infect Immun 67: 4902\u20134907.","DOI":"10.1128\/IAI.67.9.4902-4907.1999"},{"key":"e_1_3_2_23_2","doi-asserted-by":"crossref","unstructured":"Low L-Y Harrison PF Gould J Powell DR Choo JM Forster SC Chapman R Gearing LJ Cheung JK Hertzog P Rood JI. 2018. Concurrent host-pathogen transcriptional responses in a Clostridium perfringens murine myonecrosis infection. MBio 9: e00473-18 http:\/\/dx.doi.org\/10.1128\/mBio.00473-18. [PubMed]","DOI":"10.1128\/mBio.00473-18"},{"key":"e_1_3_2_24_2","doi-asserted-by":"crossref","unstructured":"Gordon VM Benz R Fujii K Leppla SH Tweten RK. 1997. Clostridium septicum alpha-toxin is proteolytically activated by furin. Infect Immun 65: 4130\u20134134.","DOI":"10.1128\/iai.65.10.4130-4134.1997"},{"key":"e_1_3_2_25_2","doi-asserted-by":"crossref","unstructured":"Sellman BR Kagan BL Tweten RK. 1997. Generation of a membrane-bound oligomerized pre-pore complex is necessary for pore formation by Clostridium septicum alpha toxin. Mol Microbiol 23: 551\u2013558 http:\/\/dx.doi.org\/10.1046\/j.1365-2958.1997.d01-1876.x. [PubMed]","DOI":"10.1046\/j.1365-2958.1997.d01-1876.x"},{"key":"e_1_3_2_26_2","doi-asserted-by":"crossref","unstructured":"Kennedy CL Krejany EO Young LF O\u2019Connor JR Awad MM Boyd RL Emmins JJ Lyras D Rood JI. 2005. The alpha-toxin of Clostridium septicum is essential for virulence. Mol Microbiol 57: 1357\u20131366 http:\/\/dx.doi.org\/10.1111\/j.1365-2958.2005.04774.x. [PubMed]","DOI":"10.1111\/j.1365-2958.2005.04774.x"},{"key":"e_1_3_2_27_2","doi-asserted-by":"crossref","unstructured":"Titball RW. 1993. Bacterial phospholipases C. Microbiol Rev 57: 347\u2013366.","DOI":"10.1128\/mr.57.2.347-366.1993"},{"key":"e_1_3_2_28_2","doi-asserted-by":"crossref","unstructured":"Titball RW Naylor CE Basak AK. 1999. The Clostridium perfringens \u03b1-toxin. Anaerobe 5: 51\u201364 http:\/\/dx.doi.org\/10.1006\/anae.1999.0191. [PubMed]","DOI":"10.1006\/anae.1999.0191"},{"key":"e_1_3_2_29_2","doi-asserted-by":"crossref","unstructured":"Sakurai J Nagahama M Oda M. 2004. Clostridium perfringens alpha-toxin: characterization and mode of action. J Biochem 136: 569\u2013574 http:\/\/dx.doi.org\/10.1093\/jb\/mvh161. [PubMed]","DOI":"10.1093\/jb\/mvh161"},{"key":"e_1_3_2_30_2","doi-asserted-by":"crossref","unstructured":"Uzal FA Freedman JC Shrestha A Theoret JR Garcia J Awad MM Adams V Moore RJ Rood JI McClane BA. 2014. Towards an understanding of the role of Clostridium perfringens toxins in human and animal disease. Future Microbiol 9: 361\u2013377 http:\/\/dx.doi.org\/10.2217\/fmb.13.168. [PubMed]","DOI":"10.2217\/fmb.13.168"},{"key":"e_1_3_2_31_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Bryant AE. 2002. The role of clostridial toxins in the pathogenesis of gas gangrene. Clin Infect Dis 35 (Suppl 1) : S93\u2013S100 http:\/\/dx.doi.org\/10.1086\/341928. [PubMed]","DOI":"10.1086\/341928"},{"key":"e_1_3_2_32_2","doi-asserted-by":"crossref","unstructured":"Naylor CE Eaton JT Howells A Justin N Moss DS Titball RW Basak AK. 1998. Structure of the key toxin in gas gangrene. Nat Struct Biol 5: 738\u2013746 http:\/\/dx.doi.org\/10.1038\/1447. [PubMed]","DOI":"10.1038\/1447"},{"key":"e_1_3_2_33_2","doi-asserted-by":"crossref","unstructured":"Gilmore MS Cruz-Rodz AL Leimeister-W\u00e4chter M Kreft J Goebel W. 1989. A Bacillus cereus cytolytic determinant cereolysin AB which comprises the phospholipase C and sphingomyelinase genes: nucleotide sequence and genetic linkage. J Bacteriol 171: 744\u2013753 http:\/\/dx.doi.org\/10.1128\/jb.171.2.744-753.1989. [PubMed]","DOI":"10.1128\/jb.171.2.744-753.1989"},{"key":"e_1_3_2_34_2","doi-asserted-by":"crossref","unstructured":"Tso JY Siebel C. 1989. Cloning and expression of the phospholipase C gene from Clostridium perfringens and Clostridium bifermentans . Infect Immun 57: 468\u2013476.","DOI":"10.1128\/iai.57.2.468-476.1989"},{"key":"e_1_3_2_35_2","doi-asserted-by":"crossref","unstructured":"Vazquez-Boland J-A Kocks C Dramsi S Ohayon H Geoffroy C Mengaud J Cossart P. 1992. Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread. Infect Immun 60: 219\u2013230.","DOI":"10.1128\/iai.60.1.219-230.1992"},{"key":"e_1_3_2_36_2","doi-asserted-by":"crossref","unstructured":"Hough E Hansen LK Birknes B Jynge K Hansen S Hordvik A Little C Dodson E Derewenda Z. 1989. High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus . Nature 338: 357\u2013360 http:\/\/dx.doi.org\/10.1038\/338357a0. [PubMed]","DOI":"10.1038\/338357a0"},{"key":"e_1_3_2_37_2","doi-asserted-by":"crossref","unstructured":"Nagahama M Mukai M Morimitsu S Ochi S Sakurai J. 2002. Role of the C-domain in the biological activities of Clostridium perfringens alpha-toxin. Microbiol Immunol 46: 647\u2013655 http:\/\/dx.doi.org\/10.1111\/j.1348-0421.2002.tb02748.x. [PubMed]","DOI":"10.1111\/j.1348-0421.2002.tb02748.x"},{"key":"e_1_3_2_38_2","doi-asserted-by":"crossref","unstructured":"Guillouard I Alzari PM Saliou B Cole ST. 1997. The carboxy-terminal C2-like domain of the alpha-toxin from Clostridium perfringens mediates calcium-dependent membrane recognition. Mol Microbiol 26: 867\u2013876 http:\/\/dx.doi.org\/10.1046\/j.1365-2958.1997.6161993.x. [PubMed]","DOI":"10.1046\/j.1365-2958.1997.6161993.x"},{"key":"e_1_3_2_39_2","doi-asserted-by":"crossref","unstructured":"Naylor CE Jepson M Crane DT Titball RW Miller J Basak AK Bolgiano B. 1999. Characterisation of the calcium-binding C-terminal domain of Clostridium perfringens alpha-toxin. J Mol Biol 294: 757\u2013770 http:\/\/dx.doi.org\/10.1006\/jmbi.1999.3279. [PubMed]","DOI":"10.1006\/jmbi.1999.3279"},{"key":"e_1_3_2_40_2","unstructured":"Nagahama M Nakayama T Kobayashi K Sakurai J. 1995. Site-directed mutagenesis studies on the zinc-binding domain of Clostridium perfringens alpha toxin. Jpn J Med Sci Biol 48: 265\u2013266."},{"key":"e_1_3_2_41_2","doi-asserted-by":"crossref","unstructured":"Nagahama M Michiue K Sakurai J. 1996. Membrane-damaging action of Clostridium perfringens alpha-toxin on phospholipid liposomes. Biochim Biophys Acta 1280: 120\u2013126.","DOI":"10.1016\/0005-2736(95)00288-X"},{"key":"e_1_3_2_42_2","doi-asserted-by":"crossref","unstructured":"Vachieri SG Clark GC Alape-Gir\u00f3n A Flores-D\u00edaz M Justin N Naylor CE Titball RW Basak AK. 2010. Comparison of a nontoxic variant of Clostridium perfringens \u03b1-toxin with the toxic wild-type strain. Acta Crystallogr D Biol Crystallogr 66: 1067\u20131074 http:\/\/dx.doi.org\/10.1107\/S090744491003369X. [PubMed]","DOI":"10.1107\/S090744491003369X"},{"key":"e_1_3_2_43_2","doi-asserted-by":"crossref","unstructured":"Eaton JT Naylor CE Howells AM Moss DS Titball RW Basak AK. 2002. Crystal structure of the C. perfringens alpha-toxin with the active site closed by a flexible loop region. J Mol Biol 319: 275\u2013281 http:\/\/dx.doi.org\/10.1016\/S0022-2836(02)00290-5.","DOI":"10.1016\/S0022-2836(02)00290-5"},{"key":"e_1_3_2_44_2","doi-asserted-by":"crossref","unstructured":"Clark GC Briggs DC Karasawa T Wang X Cole AR Maegawa T Jayasekera PN Naylor CE Miller J Moss DS Nakamura S Basak AK Titball RW. 2003. Clostridium absonum alpha-toxin: new insights into clostridial phospholipase C substrate binding and specificity. J Mol Biol 333: 759\u2013769 http:\/\/dx.doi.org\/10.1016\/j.jmb.2003.07.016. [PubMed]","DOI":"10.1016\/j.jmb.2003.07.016"},{"key":"e_1_3_2_45_2","doi-asserted-by":"crossref","unstructured":"Nagahama M Otsuka A Sakurai J. 2006. Role of tyrosine-57 and -65 in membrane-damaging and sphingomyelinase activities of Clostridium perfringens alpha-toxin. Biochim Biophys Acta 1762: 110\u2013114 http:\/\/dx.doi.org\/10.1016\/j.bbadis.2005.10.002. [PubMed]","DOI":"10.1016\/j.bbadis.2005.10.002"},{"key":"e_1_3_2_46_2","doi-asserted-by":"crossref","unstructured":"Alape-Gir\u00f3n A Flores-D\u00edaz M Guillouard I Naylor CE Titball RW Rucavado A Lomonte B Basak AK Guti\u00e9rrez JM Cole ST Thelestam M. 2000. Identification of residues critical for toxicity in Clostridium perfringens phospholipase C the key toxin in gas gangrene. Eur J Biochem 267: 5191\u20135197 http:\/\/dx.doi.org\/10.1046\/j.1432-1327.2000.01588.x. [PubMed]","DOI":"10.1046\/j.1432-1327.2000.01588.x"},{"key":"e_1_3_2_47_2","doi-asserted-by":"crossref","unstructured":"Urbina P Flores-D\u00edaz M Alape-Gir\u00f3n A Alonso A Go\u00f1i FM. 2011. Effects of bilayer composition and physical properties on the phospholipase C and sphingomyelinase activities of Clostridium perfringens \u03b1-toxin. Biochim Biophys Acta 1808: 279\u2013286 http:\/\/dx.doi.org\/10.1016\/j.bbamem.2010.08.011. [PubMed]","DOI":"10.1016\/j.bbamem.2010.08.011"},{"key":"e_1_3_2_48_2","doi-asserted-by":"crossref","unstructured":"Nagahama M Otsuka A Oda M Singh RK Ziora ZM Imagawa H Nishizawa M Sakurai J. 2007. Effect of unsaturated bonds in the sn-2 acyl chain of phosphatidylcholine on the membrane-damaging action of Clostridium perfringens alpha-toxin toward liposomes. Biochim Biophys Acta 1768: 2940\u20132945 http:\/\/dx.doi.org\/10.1016\/j.bbamem.2007.08.016. [PubMed]","DOI":"10.1016\/j.bbamem.2007.08.016"},{"key":"e_1_3_2_49_2","doi-asserted-by":"crossref","unstructured":"Moe PC Heuck AP. 2010. Phospholipid hydrolysis caused by Clostridium perfringens \u03b1-toxin facilitates the targeting of perfringolysin O to membrane bilayers. Biochemistry 49: 9498\u20139507 http:\/\/dx.doi.org\/10.1021\/bi1013886. [PubMed]","DOI":"10.1021\/bi1013886"},{"key":"e_1_3_2_50_2","doi-asserted-by":"crossref","unstructured":"Fujii Y Sakurai J. 1989. Contraction of the rat isolated aorta caused by Clostridium perfringens alpha toxin (phospholipase C): evidence for the involvement of arachidonic acid metabolism. Br J Pharmacol 97: 119\u2013124 http:\/\/dx.doi.org\/10.1111\/j.1476-5381.1989.tb11931.x. [PubMed]","DOI":"10.1111\/j.1476-5381.1989.tb11931.x"},{"key":"e_1_3_2_51_2","doi-asserted-by":"crossref","unstructured":"Sakurai J Fujii Y Shirotani M. 1990. Contraction induced by Clostridium perfringens alpha toxin in the isolated rat ileum. Toxicon 28: 411\u2013418 http:\/\/dx.doi.org\/10.1016\/0041-0101(90)90079-M.","DOI":"10.1016\/0041-0101(90)90079-M"},{"key":"e_1_3_2_52_2","doi-asserted-by":"crossref","unstructured":"Ochi S Miyawaki T Matsuda H Oda M Nagahama M Sakurai J. 2002. Clostridium perfringens alpha-toxin induces rabbit neutrophil adhesion. Microbiology 148: 237\u2013245 http:\/\/dx.doi.org\/10.1099\/00221287-148-1-237. [PubMed]","DOI":"10.1099\/00221287-148-1-237"},{"key":"e_1_3_2_53_2","doi-asserted-by":"crossref","unstructured":"Oda M Ikari S Matsuno T Morimune Y Nagahama M Sakurai J. 2006. Signal transduction mechanism involved in Clostridium perfringens alpha-toxin-induced superoxide anion generation in rabbit neutrophils. Infect Immun 74: 2876\u20132886 http:\/\/dx.doi.org\/10.1128\/IAI.74.5.2876-2886.2006. [PubMed]","DOI":"10.1128\/IAI.74.5.2876-2886.2006"},{"key":"e_1_3_2_54_2","doi-asserted-by":"crossref","unstructured":"Oda M Kabura M Takagishi T Suzue A Tominaga K Urano S Nagahama M Kobayashi K Furukawa K Furukawa K Sakurai J. 2012. Clostridium perfringens alpha-toxin recognizes the GM1a-TrkA complex. J Biol Chem 287: 33070\u201333079 http:\/\/dx.doi.org\/10.1074\/jbc.M112.393801. [PubMed]","DOI":"10.1074\/jbc.M112.393801"},{"key":"e_1_3_2_55_2","doi-asserted-by":"crossref","unstructured":"Sakurai J Ochi S Tanaka H. 1993. Evidence for coupling of Clostridium perfringens alpha-toxin-induced hemolysis to stimulated phosphatidic acid formation in rabbit erythrocytes. Infect Immun 61: 3711\u20133718.","DOI":"10.1128\/iai.61.9.3711-3718.1993"},{"key":"e_1_3_2_56_2","doi-asserted-by":"crossref","unstructured":"Sakurai J Ochi S Tanaka H. 1994. Regulation of Clostridium perfringens alpha-toxin-activated phospholipase C in rabbit erythrocyte membranes. Infect Immun 62: 717\u2013721.","DOI":"10.1128\/iai.62.2.717-721.1994"},{"key":"e_1_3_2_57_2","doi-asserted-by":"crossref","unstructured":"Ochi S Oda M Matsuda H Ikari S Sakurai J. 2004. Clostridium perfringens alpha-toxin activates the sphingomyelin metabolism system in sheep erythrocytes. J Biol Chem 279: 12181\u201312189 http:\/\/dx.doi.org\/10.1074\/jbc.M307046200. [PubMed]","DOI":"10.1074\/jbc.M307046200"},{"key":"e_1_3_2_58_2","doi-asserted-by":"crossref","unstructured":"Oda M Matsuno T Shiihara R Ochi S Yamauchi R Saito Y Imagawa H Nagahama M Nishizawa M Sakurai J. 2008. The relationship between the metabolism of sphingomyelin species and the hemolysis of sheep erythrocytes induced by Clostridium perfringens alpha-toxin. J Lipid Res 49: 1039\u20131047 http:\/\/dx.doi.org\/10.1194\/jlr.M700587-JLR200. [PubMed]","DOI":"10.1194\/jlr.M700587-JLR200"},{"key":"e_1_3_2_59_2","doi-asserted-by":"crossref","unstructured":"Tsukamoto K Kozai Y Ihara H Kohda T Mukamoto M Tsuji T Kozaki S. 2008. Identification of the receptor-binding sites in the carboxyl-terminal half of the heavy chain of botulinum neurotoxin types C and D. Microb Pathog 44: 484\u2013493 http:\/\/dx.doi.org\/10.1016\/j.micpath.2007.12.003. [PubMed]","DOI":"10.1016\/j.micpath.2007.12.003"},{"key":"e_1_3_2_60_2","doi-asserted-by":"crossref","unstructured":"Oda M Shiihara R Ohmae Y Kabura M Takagishi T Kobayashi K Nagahama M Inoue M Abe T Setsu K Sakurai J. 2012. Clostridium perfringens alpha-toxin induces the release of IL-8 through a dual pathway via TrkA in A549 cells. Biochim Biophys Acta 1822: 1581\u20131589 http:\/\/dx.doi.org\/10.1016\/j.bbadis.2012.06.007. [PubMed]","DOI":"10.1016\/j.bbadis.2012.06.007"},{"key":"e_1_3_2_61_2","doi-asserted-by":"crossref","unstructured":"Yamazaki Y Horibata Y Nagatsuka Y Hirabayashi Y Hashikawa T. 2007. Fucoganglioside alpha-fucosyl(alpha-galactosyl)-GM1: a novel member of lipid membrane microdomain components involved in PC12 cell neuritogenesis. Biochem J 407: 31\u201340 http:\/\/dx.doi.org\/10.1042\/BJ20070090. [PubMed]","DOI":"10.1042\/BJ20070090"},{"key":"e_1_3_2_62_2","doi-asserted-by":"crossref","unstructured":"Ichikawa N Iwabuchi K Kurihara H Ishii K Kobayashi T Sasaki T Hattori N Mizuno Y Hozumi K Yamada Y Arikawa-Hirasawa E. 2009. Binding of laminin-1 to monosialoganglioside GM1 in lipid rafts is crucial for neurite outgrowth. J Cell Sci 122: 289\u2013299 http:\/\/dx.doi.org\/10.1242\/jcs.030338. [PubMed]","DOI":"10.1242\/jcs.030338"},{"key":"e_1_3_2_63_2","doi-asserted-by":"crossref","unstructured":"Takagishi T Oda M Kabura M Kurosawa M Tominaga K Urano S Ueda Y Kobayashi K Kobayashi T Sakurai J Terao Y Nagahama M. 2015. Clostridium perfringens alpha-toxin induces Gm1a clustering and Trka phosphorylation in the host cell membrane. PLoS One 10: e0120497 http:\/\/dx.doi.org\/10.1371\/journal.pone.0120497. [PubMed]","DOI":"10.1371\/journal.pone.0120497"},{"key":"e_1_3_2_64_2","doi-asserted-by":"crossref","unstructured":"Ueda Y Makino A Murase-Tamada K Sakai S Inaba T Hullin-Matsuda F Kobayashi T. 2013. Sphingomyelin regulates the transbilayer movement of diacylglycerol in the plasma membrane of Madin-Darby canine kidney cells. FASEB J 27: 3284\u20133297 http:\/\/dx.doi.org\/10.1096\/fj.12-226548. [PubMed]","DOI":"10.1096\/fj.12-226548"},{"key":"e_1_3_2_65_2","doi-asserted-by":"crossref","unstructured":"Oda M Terao Y Sakurai J Nagahama M. 2015. Membrane-binding mechanism of Clostridium perfringens alpha-toxin. Toxins (Basel) 7: 5268\u20135275 http:\/\/dx.doi.org\/10.3390\/toxins7124880. [PubMed]","DOI":"10.3390\/toxins7124880"},{"key":"e_1_3_2_66_2","doi-asserted-by":"crossref","unstructured":"Flores-D\u00edaz M Alape-Gir\u00f3n A Clark G Catimel B Hirabayashi Y Nice E Guti\u00e9rrez JM Titball R Thelestam M. 2005. A cellular deficiency of gangliosides causes hypersensitivity to Clostridium perfringens phospholipase C. J Biol Chem 280: 26680\u201326689 http:\/\/dx.doi.org\/10.1074\/jbc.M500278200. [PubMed]","DOI":"10.1074\/jbc.M500278200"},{"key":"e_1_3_2_67_2","doi-asserted-by":"crossref","unstructured":"Monturiol-Gross L Flores-D\u00edaz M Pineda-Padilla MJ Castro-Castro AC Alape-Giron A. 2014. Clostridium perfringens phospholipase C induced ROS production and cytotoxicity require PKC MEK1 and NF\u03baB activation. PLoS One 9: e86475 http:\/\/dx.doi.org\/10.1371\/journal.pone.0086475. [PubMed]","DOI":"10.1371\/journal.pone.0086475"},{"key":"e_1_3_2_68_2","doi-asserted-by":"crossref","unstructured":"Flores-D\u00edaz M Monturiol-Gross L Naylor C Alape-Gir\u00f3n A Flieger A. 2016. Bacterial sphingomyelinases and phospholipases as virulence factors. Microbiol Mol Biol Rev 80: 597\u2013628 http:\/\/dx.doi.org\/10.1128\/MMBR.00082-15. [PubMed]","DOI":"10.1128\/MMBR.00082-15"},{"key":"e_1_3_2_69_2","doi-asserted-by":"crossref","unstructured":"Andrews NW Almeida PE Corrotte M. 2014. Damage control: cellular mechanisms of plasma membrane repair. Trends Cell Biol 24: 734\u2013742 http:\/\/dx.doi.org\/10.1016\/j.tcb.2014.07.008. [PubMed]","DOI":"10.1016\/j.tcb.2014.07.008"},{"key":"e_1_3_2_70_2","doi-asserted-by":"crossref","unstructured":"Amulic B Cazalet C Hayes GL Metzler KD Zychlinsky A. 2012. Neutrophil function: from mechanisms to disease. Annu Rev Immunol 30: 459\u2013489 http:\/\/dx.doi.org\/10.1146\/annurev-immunol-020711-074942. [PubMed]","DOI":"10.1146\/annurev-immunol-020711-074942"},{"key":"e_1_3_2_71_2","doi-asserted-by":"crossref","unstructured":"Dale DC Boxer L Liles WC. 2008. The phagocytes: neutrophils and monocytes. Blood 112: 935\u2013945 http:\/\/dx.doi.org\/10.1182\/blood-2007-12-077917. [PubMed]","DOI":"10.1182\/blood-2007-12-077917"},{"key":"e_1_3_2_72_2","doi-asserted-by":"crossref","unstructured":"Manz MG Boettcher S. 2014. Emergency granulopoiesis. Nat Rev Immunol 14: 302\u2013314 http:\/\/dx.doi.org\/10.1038\/nri3660. [PubMed]","DOI":"10.1038\/nri3660"},{"key":"e_1_3_2_73_2","doi-asserted-by":"crossref","unstructured":"Wirths S Bugl S Kopp HG. 2014. Neutrophil homeostasis and its regulation by danger signaling. Blood 123: 3563\u20133566 http:\/\/dx.doi.org\/10.1182\/blood-2013-11-516260. [PubMed]","DOI":"10.1182\/blood-2013-11-516260"},{"key":"e_1_3_2_74_2","doi-asserted-by":"crossref","unstructured":"Nauseef WM Borregaard N. 2014. Neutrophils at work. Nat Immunol 15: 602\u2013611 http:\/\/dx.doi.org\/10.1038\/ni.2921. [PubMed]","DOI":"10.1038\/ni.2921"},{"key":"e_1_3_2_75_2","doi-asserted-by":"crossref","unstructured":"Martinon F Tschopp J. 2005. NLRs join TLRs as innate sensors of pathogens. Trends Immunol 26: 447\u2013454 http:\/\/dx.doi.org\/10.1016\/j.it.2005.06.004. [PubMed]","DOI":"10.1016\/j.it.2005.06.004"},{"key":"e_1_3_2_76_2","doi-asserted-by":"crossref","unstructured":"Hajishengallis G Lambris JD. 2011. Microbial manipulation of receptor crosstalk in innate immunity. Nat Rev Immunol 11: 187\u2013200 http:\/\/dx.doi.org\/10.1038\/nri2918. [PubMed]","DOI":"10.1038\/nri2918"},{"key":"e_1_3_2_77_2","doi-asserted-by":"crossref","unstructured":"Beutler B. 2000. Tlr4: central component of the sole mammalian LPS sensor. Curr Opin Immunol 12: 20\u201326 http:\/\/dx.doi.org\/10.1016\/S0952-7915(99)00046-1.","DOI":"10.1016\/S0952-7915(99)00046-1"},{"key":"e_1_3_2_78_2","doi-asserted-by":"crossref","unstructured":"Texereau J Chiche JD Taylor W Choukroun G Comba B Mira JP. 2005. The importance of Toll-like receptor 2 polymorphisms in severe infections. Clin Infect Dis 41 (Suppl 7) : S408\u2013S415 http:\/\/dx.doi.org\/10.1086\/431990. [PubMed]","DOI":"10.1086\/431990"},{"key":"e_1_3_2_79_2","doi-asserted-by":"crossref","unstructured":"Dziarski R. 2003. Recognition of bacterial peptidoglycan by the innate immune system. Cell Mol Life Sci 60: 1793\u20131804 http:\/\/dx.doi.org\/10.1007\/s00018-003-3019-6. [PubMed]","DOI":"10.1007\/s00018-003-3019-6"},{"key":"e_1_3_2_80_2","doi-asserted-by":"crossref","unstructured":"Takeuchi O Hoshino K Kawai T Sanjo H Takada H Ogawa T Takeda K Akira S. 1999. Differential roles of TLR2 and TLR4 in recognition of Gram-negative and Gram-positive bacterial cell wall components. Immunity 11: 443\u2013451 http:\/\/dx.doi.org\/10.1016\/S1074-7613(00)80119-3.","DOI":"10.1016\/S1074-7613(00)80119-3"},{"key":"e_1_3_2_81_2","doi-asserted-by":"crossref","unstructured":"Demetri GD Griffin JD. 1991. Granulocyte colony-stimulating factor and its receptor. Blood 78: 2791\u20132808.","DOI":"10.1182\/blood.V78.11.2791.2791"},{"key":"e_1_3_2_82_2","doi-asserted-by":"crossref","unstructured":"Boettcher S Gerosa RC Radpour R Bauer J Ampenberger F Heikenwalder M Kopf M Manz MG. 2014. Endothelial cells translate pathogen signals into G-CSF-driven emergency granulopoiesis. Blood 124: 1393\u20131403 http:\/\/dx.doi.org\/10.1182\/blood-2014-04-570762. [PubMed]","DOI":"10.1182\/blood-2014-04-570762"},{"key":"e_1_3_2_83_2","doi-asserted-by":"crossref","unstructured":"Lieschke GJ Grail D Hodgson G Metcalf D Stanley E Cheers C Fowler KJ Basu S Zhan YF Dunn AR. 1994. Mice lacking granulocyte colony-stimulating factor have chronic neutropenia granulocyte and macrophage progenitor cell deficiency and impaired neutrophil mobilization. Blood 84: 1737\u20131746.","DOI":"10.1182\/blood.V84.6.1737.bloodjournal8461737"},{"key":"e_1_3_2_84_2","doi-asserted-by":"crossref","unstructured":"Liu F Wu HY Wesselschmidt R Kornaga T Link DC. 1996. Impaired production and increased apoptosis of neutrophils in granulocyte colony-stimulating factor receptor-deficient mice. Immunity 5: 491\u2013501 http:\/\/dx.doi.org\/10.1016\/S1074-7613(00)80504-X.","DOI":"10.1016\/S1074-7613(00)80504-X"},{"key":"e_1_3_2_85_2","doi-asserted-by":"crossref","unstructured":"Bryant AE. 2003. Biology and pathogenesis of thrombosis and procoagulant activity in invasive infections caused by group A streptococci and Clostridium perfringens . Clin Microbiol Rev 16: 451\u2013462 http:\/\/dx.doi.org\/10.1128\/CMR.16.3.451-462.2003. [PubMed]","DOI":"10.1128\/CMR.16.3.451-462.2003"},{"key":"e_1_3_2_86_2","doi-asserted-by":"crossref","unstructured":"McNee JW Dunn JS. 1917. The method of spread of gas gangrene into living tissue. BMJ 1: 4\u2013729 http:\/\/dx.doi.org\/10.1136\/bmj.1.2944.726. [PubMed]","DOI":"10.1136\/bmj.1.2944.726"},{"key":"e_1_3_2_87_2","doi-asserted-by":"crossref","unstructured":"Bryant AE Chen RY Nagata Y Wang Y Lee CH Finegold S Guth PH Stevens DL. 2000. Clostridial gas gangrene. II. Phospholipase C-induced activation of platelet gpIIbIIIa mediates vascular occlusion and myonecrosis in Clostridium perfringens gas gangrene. J Infect Dis 182: 808\u2013815 http:\/\/dx.doi.org\/10.1086\/315757. [PubMed]","DOI":"10.1086\/315757"},{"key":"e_1_3_2_88_2","doi-asserted-by":"crossref","unstructured":"Bryant AE Chen RY Nagata Y Wang Y Lee CH Finegold S Guth PH Stevens DL. 2000. Clostridial gas gangrene. I. Cellular and molecular mechanisms of microvascular dysfunction induced by exotoxins of Clostridium perfringens . J Infect Dis 182: 799\u2013807 http:\/\/dx.doi.org\/10.1086\/315756. [PubMed]","DOI":"10.1086\/315756"},{"key":"e_1_3_2_89_2","doi-asserted-by":"crossref","unstructured":"Hickey MJ Kwan RY Awad MM Kennedy CL Young LF Hall P Cordner LM Lyras D Emmins JJ Rood JI. 2008. Molecular and cellular basis of microvascular perfusion deficits induced by Clostridium perfringens and Clostridium septicum . PLoS Pathog 4: e1000045 http:\/\/dx.doi.org\/10.1371\/journal.ppat.1000045. [PubMed]","DOI":"10.1371\/journal.ppat.1000045"},{"key":"e_1_3_2_90_2","doi-asserted-by":"crossref","unstructured":"Bryant AE Bayer CR Aldape MJ Wallace RJ Titball RW Stevens DL. 2006. Clostridium perfringens phospholipase C-induced platelet\/leukocyte interactions impede neutrophil diapedesis. J Med Microbiol 55: 495\u2013504 http:\/\/dx.doi.org\/10.1099\/jmm.0.46390-0. [PubMed]","DOI":"10.1099\/jmm.0.46390-0"},{"key":"e_1_3_2_91_2","doi-asserted-by":"crossref","unstructured":"Takehara M Takagishi T Seike S Ohtani K Kobayashi K Miyamoto K Shimizu T Nagahama M. 2016. Clostridium perfringens alpha-toxin impairs innate immunity via inhibition of neutrophil differentiation. Sci Rep 6: 28192 http:\/\/dx.doi.org\/10.1038\/srep28192. [PubMed]","DOI":"10.1038\/srep28192"},{"key":"e_1_3_2_92_2","doi-asserted-by":"crossref","unstructured":"Basu S Hodgson G Katz M Dunn AR. 2002. Evaluation of role of G-CSF in the production survival and release of neutrophils from bone marrow into circulation. Blood 100: 854\u2013861 http:\/\/dx.doi.org\/10.1182\/blood.V100.3.854. [PubMed]","DOI":"10.1182\/blood.V100.3.854"},{"key":"e_1_3_2_93_2","doi-asserted-by":"crossref","unstructured":"Diaz O M\u00e9barek-Azzam S Benzaria A Dubois M Lagarde M N\u00e9moz G Prigent AF. 2005. Disruption of lipid rafts stimulates phospholipase D activity in human lymphocytes: implication in the regulation of immune function. J Immunol 175: 8077\u20138086 http:\/\/dx.doi.org\/10.4049\/jimmunol.175.12.8077. [PubMed]","DOI":"10.4049\/jimmunol.175.12.8077"},{"key":"e_1_3_2_94_2","doi-asserted-by":"crossref","unstructured":"Ostrom RS Insel PA. 2004. The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology. Br J Pharmacol 143: 235\u2013245 http:\/\/dx.doi.org\/10.1038\/sj.bjp.0705930. [PubMed]","DOI":"10.1038\/sj.bjp.0705930"},{"key":"e_1_3_2_95_2","doi-asserted-by":"crossref","unstructured":"Simons K Toomre D. 2000. Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1: 31\u201339 http:\/\/dx.doi.org\/10.1038\/35036052. [PubMed]","DOI":"10.1038\/35036052"},{"key":"e_1_3_2_96_2","doi-asserted-by":"crossref","unstructured":"Kolesnick RN Kr\u00f6nke M. 1998. Regulation of ceramide production and apoptosis. Annu Rev Physiol 60: 643\u2013665 http:\/\/dx.doi.org\/10.1146\/annurev.physiol.60.1.643. [PubMed]","DOI":"10.1146\/annurev.physiol.60.1.643"},{"key":"e_1_3_2_97_2","doi-asserted-by":"crossref","unstructured":"Ochi S Oda M Nagahama M Sakurai J. 2003. Clostridium perfringens alpha-toxin-induced hemolysis of horse erythrocytes is dependent on Ca2+ uptake. Biochim Biophys Acta 1613: 79\u201386 http:\/\/dx.doi.org\/10.1016\/S0005-2736(03)00140-8.","DOI":"10.1016\/S0005-2736(03)00140-8"},{"key":"e_1_3_2_98_2","doi-asserted-by":"crossref","unstructured":"Chang HH Wang TP Chen PK Lin YY Liao CH Lin TK Chiang YW Lin WB Chiang CY Kau JH Huang HH Hsu HL Liao CY Sun DS. 2013. Erythropoiesis suppression is associated with anthrax lethal toxin-mediated pathogenic progression. PLoS One 8: e71718 http:\/\/dx.doi.org\/10.1371\/journal.pone.0071718. [PubMed]","DOI":"10.1371\/journal.pone.0071718"},{"key":"e_1_3_2_99_2","doi-asserted-by":"crossref","unstructured":"Takagishi T Takehara M Seike S Miyamoto K Kobayashi K Nagahama M. 2017. Clostridium perfringens \u03b1-toxin impairs erythropoiesis by inhibition of erythroid differentiation. Sci Rep 7: 5217 http:\/\/dx.doi.org\/10.1038\/s41598-017-05567-8. [PubMed]","DOI":"10.1038\/s41598-017-05567-8"},{"key":"e_1_3_2_100_2","doi-asserted-by":"crossref","unstructured":"Simon TG Bradley J Jones A Carino G. 2014. Massive intravascular hemolysis from Clostridium perfringens septicemia: a review. J Intensive Care Med 29: 327\u2013333 http:\/\/dx.doi.org\/10.1177\/0885066613498043. [PubMed]","DOI":"10.1177\/0885066613498043"},{"key":"e_1_3_2_101_2","doi-asserted-by":"crossref","unstructured":"Konstantinidis DG Pushkaran S Johnson JF Cancelas JA Manganaris S Harris CE Williams DA Zheng Y Kalfa TA. 2012. Signaling and cytoskeletal requirements in erythroblast enucleation. Blood 119: 6118\u20136127 http:\/\/dx.doi.org\/10.1182\/blood-2011-09-379263. [PubMed]","DOI":"10.1182\/blood-2011-09-379263"},{"key":"e_1_3_2_102_2","doi-asserted-by":"crossref","unstructured":"Verherstraeten S Goossens E Valgaeren B Pardon B Timbermont L Haesebrouck F Ducatelle R Deprez P Wade KR Tweten R Van Immerseel F. 2015. Perfringolysin O: the underrated Clostridium perfringens toxin? Toxins (Basel) 7: 1702\u20131721 http:\/\/dx.doi.org\/10.3390\/toxins7051702. [PubMed]","DOI":"10.3390\/toxins7051702"},{"key":"e_1_3_2_103_2","doi-asserted-by":"crossref","unstructured":"Popoff MR. 2014. Clostridial pore-forming toxins: powerful virulence factors. Anaerobe 30: 220\u2013238 http:\/\/dx.doi.org\/10.1016\/j.anaerobe.2014.05.014. [PubMed]","DOI":"10.1016\/j.anaerobe.2014.05.014"},{"key":"e_1_3_2_104_2","doi-asserted-by":"crossref","unstructured":"Katayama S Dupuy B Garnier T Cole ST. 1995. Rapid expansion of the physical and genetic map of the chromosome of Clostridium perfringens CPN50. J Bacteriol 177: 5680\u20135685 http:\/\/dx.doi.org\/10.1128\/jb.177.19.5680-5685.1995. [PubMed]","DOI":"10.1128\/jb.177.19.5680-5685.1995"},{"key":"e_1_3_2_105_2","doi-asserted-by":"crossref","unstructured":"Shimizu T Ohtani K Hirakawa H Ohshima K Yamashita A Shiba T Ogasawara N Hattori M Kuhara S Hayashi H. 2002. Complete genome sequence of Clostridium perfringens an anaerobic flesh-eater. Proc Natl Acad Sci USA 99: 996\u20131001 http:\/\/dx.doi.org\/10.1073\/pnas.022493799. [PubMed]","DOI":"10.1073\/pnas.022493799"},{"key":"e_1_3_2_106_2","doi-asserted-by":"crossref","unstructured":"Myers GS Rasko DA Cheung JK Ravel J Seshadri R DeBoy RT Ren Q Varga J Awad MM Brinkac LM Daugherty SC Haft DH Dodson RJ Madupu R Nelson WC Rosovitz MJ Sullivan SA Khouri H Dimitrov GI Watkins KL Mulligan S Benton J Radune D Fisher DJ Atkins HS Hiscox T Jost BH Billington SJ Songer JG McClane BA Titball RW Rood JI Melville SB Paulsen IT. 2006. Skewed genomic variability in strains of the toxigenic bacterial pathogen Clostridium perfringens . Genome Res 16: 1031\u20131040 http:\/\/dx.doi.org\/10.1101\/gr.5238106. [PubMed]","DOI":"10.1101\/gr.5238106"},{"key":"e_1_3_2_107_2","doi-asserted-by":"crossref","unstructured":"Hassan KA Elbourne LD Tetu SG Melville SB Rood JI Paulsen IT. 2014. Genomic analyses of Clostridium perfringens isolates from five toxinotypes. Res Microbiol 166: 255\u2013263. [PubMed]","DOI":"10.1016\/j.resmic.2014.10.003"},{"key":"e_1_3_2_108_2","doi-asserted-by":"crossref","unstructured":"Kiu R Caim S Alexander S Pachori P Hall LJ. 2017. Probing genomic aspects of the multi-host pathogen Clostridium perfringens reveals significant pangenome diversity and a diverse array of virulence factors. Front Microbiol 8: 2485 http:\/\/dx.doi.org\/10.3389\/fmicb.2017.02485. [PubMed]","DOI":"10.3389\/fmicb.2017.02485"},{"key":"e_1_3_2_109_2","doi-asserted-by":"crossref","unstructured":"Tweten RK. 1988. Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from Clostridium perfringens : significant homology with the genes for streptolysin O and pneumolysin. Infect Immun 56: 3235\u20133240.","DOI":"10.1128\/iai.56.12.3235-3240.1988"},{"key":"e_1_3_2_110_2","doi-asserted-by":"crossref","unstructured":"Rossjohn J Feil SC McKinstry WJ Tweten RK Parker MW. 1997. Structure of a cholesterol-binding thiol-activated cytolysin and a model of its membrane form. Cell 89: 685\u2013692 http:\/\/dx.doi.org\/10.1016\/S0092-8674(00)80251-2.","DOI":"10.1016\/S0092-8674(00)80251-2"},{"key":"e_1_3_2_111_2","doi-asserted-by":"crossref","unstructured":"Shatursky O Heuck AP Shepard LA Rossjohn J Parker MW Johnson AE Tweten RK. 1999. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell 99: 293\u2013299 http:\/\/dx.doi.org\/10.1016\/S0092-8674(00)81660-8.","DOI":"10.1016\/S0092-8674(00)81660-8"},{"key":"e_1_3_2_112_2","doi-asserted-by":"crossref","unstructured":"Rosado CJ Buckle AM Law RH Butcher RE Kan WT Bird CH Ung K Browne KA Baran K Bashtannyk-Puhalovich TA Faux NG Wong W Porter CJ Pike RN Ellisdon AM Pearce MC Bottomley SP Emsley J Smith AI Rossjohn J Hartland EL Voskoboinik I Trapani JA Bird PI Dunstone MA Whisstock JC. 2007. A common fold mediates vertebrate defense and bacterial attack. Science 317: 1548\u20131551 http:\/\/dx.doi.org\/10.1126\/science.1144706. [PubMed]","DOI":"10.1126\/science.1144706"},{"key":"e_1_3_2_113_2","doi-asserted-by":"crossref","unstructured":"Tweten RK Hotze EM Wade KR. 2015. The unique molecular choreography of giant pore formation by the cholesterol-dependent cytolysins of Gram-positive bacteria. Annu Rev Microbiol 69: 323\u2013340 http:\/\/dx.doi.org\/10.1146\/annurev-micro-091014-104233. [PubMed]","DOI":"10.1146\/annurev-micro-091014-104233"},{"key":"e_1_3_2_114_2","doi-asserted-by":"crossref","unstructured":"Farrand AJ LaChapelle S Hotze EM Johnson AE Tweten RK. 2010. Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc Natl Acad Sci U S A 107: 4341\u20134346 http:\/\/dx.doi.org\/10.1073\/pnas.0911581107. [PubMed]","DOI":"10.1073\/pnas.0911581107"},{"key":"e_1_3_2_115_2","doi-asserted-by":"crossref","unstructured":"Harris RW Sims PJ Tweten RK. 1991. Evidence that Clostridium perfringens theta-toxin induces colloid-osmotic lysis of erythrocytes. Infect Immun 59: 2499\u20132501.","DOI":"10.1128\/iai.59.7.2499-2501.1991"},{"key":"e_1_3_2_116_2","doi-asserted-by":"crossref","unstructured":"Park JM Ng VH Maeda S Rest RF Karin M. 2004. Anthrolysin O and other Gram-positive cytolysins are toll-like receptor 4 agonists. J Exp Med 200: 1647\u20131655 http:\/\/dx.doi.org\/10.1084\/jem.20041215. [PubMed]","DOI":"10.1084\/jem.20041215"},{"key":"e_1_3_2_117_2","doi-asserted-by":"crossref","unstructured":"Ribet D Hamon M Gouin E Nahori MA Impens F Neyret-Kahn H Gevaert K Vandekerckhove J Dejean A Cossart P. 2010. Listeria monocytogenes impairs SUMOylation for efficient infection. Nature 464: 1192\u20131195 http:\/\/dx.doi.org\/10.1038\/nature08963. [PubMed]","DOI":"10.1038\/nature08963"},{"key":"e_1_3_2_118_2","doi-asserted-by":"crossref","unstructured":"Asmuth DM Olson RD Hackett SP Bryant AE Tweten RK Tso JY Zollman T Stevens DL. 1995. Effects of Clostridium perfringens recombinant and crude phospholipase C and theta-toxin on rabbit hemodynamic parameters. J Infect Dis 172: 1317\u20131323 http:\/\/dx.doi.org\/10.1093\/infdis\/172.5.1317. [PubMed]","DOI":"10.1093\/infdis\/172.5.1317"},{"key":"e_1_3_2_119_2","doi-asserted-by":"crossref","unstructured":"Bryant AE Bergstrom R Zimmerman GA Salyer JL Hill HR Tweten RK Sato H Stevens DL. 1993. Clostridium perfringens invasiveness is enhanced by effects of theta toxin upon PMNL structure and function: the roles of leukocytotoxicity and expression of CD11\/CD18 adherence glycoprotein. FEMS Immunol Med Microbiol 7: 321\u2013336 http:\/\/dx.doi.org\/10.1111\/j.1574-695X.1993.tb00414.x. [PubMed]","DOI":"10.1111\/j.1574-695X.1993.tb00414.x"},{"key":"e_1_3_2_120_2","doi-asserted-by":"crossref","unstructured":"Bryant AE Stevens DL. 1996. Phospholipase C and perfringolysin O from Clostridium perfringens upregulate endothelial cell-leukocyte adherence molecule 1 and intercellular leukocyte adherence molecule 1 expression and induce interleukin-8 synthesis in cultured human umbilical vein endothelial cells. Infect Immun 64: 358\u2013362.","DOI":"10.1128\/iai.64.1.358-362.1996"},{"key":"e_1_3_2_121_2","doi-asserted-by":"crossref","unstructured":"Bunting M Lorant DE Bryant AE Zimmerman GA McIntyre TM Stevens DL Prescott SM. 1997. Alpha toxin from Clostridium perfringens induces proinflammatory changes in endothelial cells. J Clin Invest 100: 565\u2013574 http:\/\/dx.doi.org\/10.1172\/JCI119566. [PubMed]","DOI":"10.1172\/JCI119566"},{"key":"e_1_3_2_122_2","doi-asserted-by":"crossref","unstructured":"Whately R Zimmerman G Stevens D Parker C McIntyre T Prescott S. 1989. The regulation of platelet activating factor synthesis in endothelial cells: the role of calcium and protein kinase. J Biol Chem 11: 6325\u20136333.","DOI":"10.1016\/S0021-9258(18)83351-8"},{"key":"e_1_3_2_123_2","doi-asserted-by":"crossref","unstructured":"Bryant AE Bayer CR Hayes-Schroer SM Stevens DL. 2003. Activation of platelet gpIIbIIIa by phospholipase C from Clostridium perfringens involves store-operated calcium entry. J Infect Dis 187: 408\u2013417 http:\/\/dx.doi.org\/10.1086\/367964. [PubMed]","DOI":"10.1086\/367964"},{"key":"e_1_3_2_124_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Mitten J Henry C. 1987. Effects of \u03b1 and \u03b8 toxins from Clostridium perfringens on human polymorphonuclear leukocytes. J Infect Dis 156: 324\u2013333 http:\/\/dx.doi.org\/10.1093\/infdis\/156.2.324. [PubMed]","DOI":"10.1093\/infdis\/156.2.324"},{"key":"e_1_3_2_125_2","doi-asserted-by":"crossref","unstructured":"Stevens DL. 2000. The pathogenesis of clostridial myonecrosis. Int J Med Microbiol 290: 497\u2013502 http:\/\/dx.doi.org\/10.1016\/S1438-4221(00)80074-0.","DOI":"10.1016\/S1438-4221(00)80074-0"},{"key":"e_1_3_2_126_2","doi-asserted-by":"crossref","unstructured":"O\u2019Brien DK Melville SB. 2000. The anaerobic pathogen can escape the phagosome of macrophages under aerobic conditions. Cell Microbiol 2: 505\u2013519 http:\/\/dx.doi.org\/10.1046\/j.1462-5822.2000.00074.x. [PubMed]","DOI":"10.1046\/j.1462-5822.2000.00074.x"},{"key":"e_1_3_2_127_2","doi-asserted-by":"crossref","unstructured":"O\u2019Brien DK Melville SB. 2004. Effects of Clostridium perfringens alpha-toxin (PLC) and perfringolysin O (PFO) on cytotoxicity to macrophages on escape from the phagosomes of macrophages and on persistence of C. perfringens in host tissues. Infect Immun 72: 5204\u20135215 http:\/\/dx.doi.org\/10.1128\/IAI.72.9.5204-5215.2004. [PubMed]","DOI":"10.1128\/IAI.72.9.5204-5215.2004"},{"key":"e_1_3_2_128_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Troyer BE Merrick DT Mitten JE Olson RD. 1988. Lethal effects and cardiovascular effects of purified \u03b1- and \u03b8-toxins from Clostridium perfringens . J Infect Dis 157: 272\u2013279 http:\/\/dx.doi.org\/10.1093\/infdis\/157.2.272. [PubMed]","DOI":"10.1093\/infdis\/157.2.272"},{"key":"e_1_3_2_129_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Bryant AE. 1997. Pathogenesis of Clostridium perfringens infection: mechanisms and mediators of shock. Clin Infect Dis 25 (Suppl 2) : S160\u2013S164 http:\/\/dx.doi.org\/10.1086\/516249. [PubMed]","DOI":"10.1086\/516249"},{"key":"e_1_3_2_130_2","doi-asserted-by":"crossref","unstructured":"Knapp O Maier E Mkaddem SB Benz R Bens M Chenal A Geny B Vandewalle A Popoff MR. 2010. Clostridium septicum alpha-toxin forms pores and induces rapid cell necrosis. Toxicon 55: 61\u201372 http:\/\/dx.doi.org\/10.1016\/j.toxicon.2009.06.037. [PubMed]","DOI":"10.1016\/j.toxicon.2009.06.037"},{"key":"e_1_3_2_131_2","doi-asserted-by":"crossref","unstructured":"Dal Peraro M van der Goot FG. 2016. Pore-forming toxins: ancient but never really out of fashion. Nat Rev Microbiol 14: 77\u201392 http:\/\/dx.doi.org\/10.1038\/nrmicro.2015.3. [PubMed]","DOI":"10.1038\/nrmicro.2015.3"},{"key":"e_1_3_2_132_2","doi-asserted-by":"crossref","unstructured":"Rossjohn J Buckley JT Hazes B Murzin AG Read RJ Parker MW. 1997. Aerolysin and pertussis toxin share a common receptor-binding domain. EMBO J 16: 3426\u20133434 http:\/\/dx.doi.org\/10.1093\/emboj\/16.12.3426. [PubMed]","DOI":"10.1093\/emboj\/16.12.3426"},{"key":"e_1_3_2_133_2","doi-asserted-by":"crossref","unstructured":"Melton JA Parker MW Rossjohn J Buckley JT Tweten RK. 2004. The identification and structure of the membrane-spanning domain of the Clostridium septicum alpha toxin. J Biol Chem 279: 14315\u201314322 http:\/\/dx.doi.org\/10.1074\/jbc.M313758200. [PubMed]","DOI":"10.1074\/jbc.M313758200"},{"key":"e_1_3_2_134_2","doi-asserted-by":"crossref","unstructured":"Ballard J Sokolov Y Yuan W-L Kagan BL Tweten RK. 1993. Activation and mechanism of Clostridium septicum alpha toxin. Mol Microbiol 10: 627\u2013634 http:\/\/dx.doi.org\/10.1111\/j.1365-2958.1993.tb00934.x. [PubMed]","DOI":"10.1111\/j.1365-2958.1993.tb00934.x"},{"key":"e_1_3_2_135_2","doi-asserted-by":"crossref","unstructured":"Sellman BR Tweten RK. 1997. The propeptide of Clostridium septicum alpha toxin functions as an intramolecular chaperone and is a potent inhibitor of alpha toxin-dependent cytolysis. Mol Microbiol 25: 429\u2013440 http:\/\/dx.doi.org\/10.1046\/j.1365-2958.1997.4541820.x. [PubMed]","DOI":"10.1046\/j.1365-2958.1997.4541820.x"},{"key":"e_1_3_2_136_2","doi-asserted-by":"crossref","unstructured":"Gordon VM Nelson KL Buckley JT Stevens VL Tweten RK Elwood PC Leppla SH. 1999. Clostridium septicum alpha toxin uses glycosylphosphatidylinositol-anchored protein receptors. J Biol Chem 274: 27274\u201327280 http:\/\/dx.doi.org\/10.1074\/jbc.274.38.27274. [PubMed]","DOI":"10.1074\/jbc.274.38.27274"},{"key":"e_1_3_2_137_2","doi-asserted-by":"crossref","unstructured":"Shin DJ Lee JJ Choy HE Hong Y. 2004. Generation and characterization of Clostridium septicum alpha toxin mutants and their use in diagnosing paroxysmal nocturnal hemoglobinuria. Biochem Biophys Res Commun 324: 753\u2013760 http:\/\/dx.doi.org\/10.1016\/j.bbrc.2004.09.104. [PubMed]","DOI":"10.1016\/j.bbrc.2004.09.104"},{"key":"e_1_3_2_138_2","doi-asserted-by":"crossref","unstructured":"Melton-Witt JA Bentsen LM Tweten RK. 2006. Identification of functional domains of Clostridium septicum alpha toxin. Biochemistry 45: 14347\u201314354 http:\/\/dx.doi.org\/10.1021\/bi061334p. [PubMed]","DOI":"10.1021\/bi061334p"},{"key":"e_1_3_2_139_2","doi-asserted-by":"crossref","unstructured":"Mukamoto M Kimura R Hang\u2019ombe MB Kohda T Kozaki S. 2013. Analysis of tryptophan-rich region in Clostridium septicum alpha-toxin involved with binding to glycosylphosphatidylinositol-anchored proteins. Microbiol Immunol 57: 163\u2013169 http:\/\/dx.doi.org\/10.1111\/1348-0421.12017. [PubMed]","DOI":"10.1111\/1348-0421.12017"},{"key":"e_1_3_2_140_2","doi-asserted-by":"crossref","unstructured":"Kennedy CL Lyras D Cordner LM Melton-Witt J Emmins JJ Tweten RK Rood JI. 2009. Pore-forming activity of alpha-toxin is essential for Clostridium septicum -mediated myonecrosis. Infect Immun 77: 943\u2013951 http:\/\/dx.doi.org\/10.1128\/IAI.01267-08. [PubMed]","DOI":"10.1128\/IAI.01267-08"},{"key":"e_1_3_2_141_2","doi-asserted-by":"crossref","unstructured":"Kennedy CL Smith DJ Lyras D Chakravorty A Rood JI. 2009. Programmed cellular necrosis mediated by the pore-forming alpha-toxin from Clostridium septicum . PLoS Pathog 5: e1000516 http:\/\/dx.doi.org\/10.1371\/journal.ppat.1000516. [PubMed]","DOI":"10.1371\/journal.ppat.1000516"},{"key":"e_1_3_2_142_2","doi-asserted-by":"crossref","unstructured":"Hang\u2019ombe MB Kohda T Mukamoto M Kozaki S. 2005. Relationship between Clostridium septicum alpha-toxin activity and binding to erythrocyte membranes. J Vet Med Sci 67: 69\u201374 http:\/\/dx.doi.org\/10.1292\/jvms.67.69. [PubMed]","DOI":"10.1292\/jvms.67.69"},{"key":"e_1_3_2_143_2","doi-asserted-by":"crossref","unstructured":"Hang\u2019ombe MB Mukamoto M Kohda T Sugimoto N Kozaki S. 2004. Cytotoxicity of Clostridium septicum alpha-toxin: its oligomerization in detergent resistant membranes of mammalian cells. Microb Pathog 37: 279\u2013286 http:\/\/dx.doi.org\/10.1016\/j.micpath.2004.09.001. [PubMed]","DOI":"10.1016\/j.micpath.2004.09.001"},{"key":"e_1_3_2_144_2","doi-asserted-by":"crossref","unstructured":"Chakravorty A Awad MM Cheung JK Hiscox TJ Lyras D Rood JI. 2015. The pore-forming \u03b1-toxin from Clostridium septicum activates the MAPK pathway in a Ras-c-Raf-dependent and independent manner. Toxins (Basel) 7: 516\u2013534 http:\/\/dx.doi.org\/10.3390\/toxins7020516. [PubMed]","DOI":"10.3390\/toxins7020516"},{"key":"e_1_3_2_145_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Bisno AL Chambers HF Dellinger EP Goldstein EJ Gorbach SL Hirschmann JV Kaplan SL Montoya JG Wade JC Infectious Diseases Society of America. 2014. Practice guidelines for the diagnosis and management of skin and soft tissue infections: 2014 update by the Infectious Diseases Society of America. Clin Infect Dis 59: e10\u2013e52 http:\/\/dx.doi.org\/10.1093\/cid\/ciu296. [PubMed]","DOI":"10.1093\/cid\/ciu296"},{"key":"e_1_3_2_146_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Maier KA Laine BM Mitten JE. 1987. Comparison of clindamycin rifampin tetracycline metronidazole and penicillin for efficacy in prevention of experimental gas gangrene due to Clostridium perfringens . J Infect Dis 155: 220\u2013228 http:\/\/dx.doi.org\/10.1093\/infdis\/155.2.220. [PubMed]","DOI":"10.1093\/infdis\/155.2.220"},{"key":"e_1_3_2_147_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Laine BM Mitten JE. 1987. Comparison of single and combination antimicrobial agents for prevention of experimental gas gangrene caused by Clostridium perfringens . Antimicrob Agents Chemother 31: 312\u2013316 http:\/\/dx.doi.org\/10.1128\/AAC.31.2.312. [PubMed]","DOI":"10.1128\/AAC.31.2.312"},{"key":"e_1_3_2_148_2","doi-asserted-by":"crossref","unstructured":"Oda M Kihara A Yoshioka H Saito Y Watanabe N Uoo K Higashihara M Nagahama M Koide N Yokochi T Sakurai J. 2008. Effect of erythromycin on biological activities induced by Clostridium perfringens \u03b1-toxin. J Pharmacol Exp Ther 327: 934\u2013940 http:\/\/dx.doi.org\/10.1124\/jpet.108.143677. [PubMed]","DOI":"10.1124\/jpet.108.143677"},{"key":"e_1_3_2_149_2","doi-asserted-by":"crossref","unstructured":"Chakravorty A Awad MM Hiscox TJ Cheung JK Choo JM Lyras D Rood JI. 2014. Opioid analgesics stop the development of clostridial gas gangrene. J Infect Dis 210: 483\u2013492 http:\/\/dx.doi.org\/10.1093\/infdis\/jiu101. [PubMed]","DOI":"10.1093\/infdis\/jiu101"},{"key":"e_1_3_2_150_2","doi-asserted-by":"crossref","unstructured":"Stevens DL Titball RW Jepson M Bayer CR Hayes-Schroer SM Bryant AE. 2004. Immunization with the C-domain of alpha-toxin prevents lethal infection localizes tissue injury and promotes host response to challenge with Clostridium perfringens . J Infect Dis 190: 767\u2013773 http:\/\/dx.doi.org\/10.1086\/422691. [PubMed]","DOI":"10.1086\/422691"},{"key":"e_1_3_2_151_2","doi-asserted-by":"crossref","unstructured":"Nagahama M Oda M Kobayashi K Ochi S Takagishi T Shibutani M Sakurai J. 2013. A recombinant carboxy-terminal domain of alpha-toxin protects mice against Clostridium perfringens . Microbiol Immunol 57: 340\u2013345 http:\/\/dx.doi.org\/10.1111\/1348-0421.12036. [PubMed]","DOI":"10.1111\/1348-0421.12036"},{"key":"e_1_3_2_152_2","doi-asserted-by":"crossref","unstructured":"Aronoff DM. 2013. Clostridium novyi sordellii and tetani: mechanisms of disease. Anaerobe 24: 98\u2013101 http:\/\/dx.doi.org\/10.1016\/j.anaerobe.2013.08.009. [PubMed]","DOI":"10.1016\/j.anaerobe.2013.08.009"},{"key":"e_1_3_2_153_2","doi-asserted-by":"crossref","unstructured":"J\u00f3\u017awiak J Grzela T Jankowska-Steifer E Komar A Moskalewski S Martirosian G. 2007. Lethal factor of Clostridium histolyticum kills cells by apoptosis. FEMS Immunol Med Microbiol 49: 296\u2013303 http:\/\/dx.doi.org\/10.1111\/j.1574-695X.2006.00204.x. [PubMed]","DOI":"10.1111\/j.1574-695X.2006.00204.x"},{"key":"e_1_3_2_154_2","doi-asserted-by":"crossref","unstructured":"Genth H Pauillac S Schelle I Bouvet P Bouchier C Varela-Chavez C Just I Popoff MR. 2014. Haemorrhagic toxin and lethal toxin from Clostridium sordellii strain vpi9048: molecular characterization and comparative analysis of substrate specificity of the large clostridial glucosylating toxins. Cell Microbiol 16: 1706\u20131721 http:\/\/dx.doi.org\/10.1111\/cmi.12321. [PubMed]","DOI":"10.1111\/cmi.12321"},{"key":"e_1_3_2_155_2","doi-asserted-by":"crossref","unstructured":"Hausmann R Albert F Geissd\u00f6rfer W Betz P. 2004. Clostridium fallax associated with sudden death in a 16-year-old boy. J Med Microbiol 53: 581\u2013583 http:\/\/dx.doi.org\/10.1099\/jmm.0.05495-0. [PubMed]","DOI":"10.1099\/jmm.0.05495-0"},{"key":"e_1_3_2_156_2","doi-asserted-by":"crossref","unstructured":"Biswas R K D Sistla S Chandra Sistla S Amaranathan A. 2017. Clostridium perfringens : a bacterial pathogen gaining recognition in necrotizing pancreatitis. Anaerobe 47: 111\u2013114 http:\/\/dx.doi.org\/10.1016\/j.anaerobe.2017.05.006. [PubMed]","DOI":"10.1016\/j.anaerobe.2017.05.006"},{"key":"e_1_3_2_157_2","doi-asserted-by":"crossref","unstructured":"Rychener L InAlbon S Djordjevic SP Chowdhury PR Ziech RE de Vargas AC Frey J Falquet L. 2017. Clostridium chauvoei an evolutionary dead-end pathogen. Front Microbiol 8: 1054 http:\/\/dx.doi.org\/10.3389\/fmicb.2017.01054. [PubMed]","DOI":"10.3389\/fmicb.2017.01054"}],"container-title":["Microbiology Spectrum"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/microbiolspec.GPP3-0024-2018","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/microbiolspec.GPP3-0024-2018","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,8]],"date-time":"2022-03-08T08:29:25Z","timestamp":1646728165000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/microbiolspec.GPP3-0024-2018"}},"subtitle":[],"editor":[{"given":"Vincent A.","family":"Fischetti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]},{"given":"Richard P.","family":"Novick","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]},{"given":"Joseph J.","family":"Ferretti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]},{"given":"Daniel A.","family":"Portnoy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]},{"given":"Julian I.","family":"Rood","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2019,7,19]]},"references-count":156,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2019,7,19]]}},"alternative-id":["10.1128\/microbiolspec.GPP3-0024-2018"],"URL":"https:\/\/doi.org\/10.1128\/microbiolspec.gpp3-0024-2018","relation":{},"ISSN":["2165-0497"],"issn-type":[{"value":"2165-0497","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,7,19]]},"assertion":[{"value":"2018-03-19","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2019-07-26","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"7.4.17"}}