{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T21:54:09Z","timestamp":1776894849796,"version":"3.51.2"},"reference-count":27,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,8,1]],"date-time":"2020-08-01T00:00:00Z","timestamp":1596240000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,1]],"date-time":"2020-08-01T00:00:00Z","timestamp":1596240000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100012155","name":"National Institute for Medical Research Development","doi-asserted-by":"publisher","award":["965442"],"award-info":[{"award-number":["965442"]}],"id":[{"id":"10.13039\/501100012155","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2020,8]]},"DOI":"10.1016\/j.toxicon.2020.05.004","type":"journal-article","created":{"date-parts":[[2020,5,22]],"date-time":"2020-05-22T03:45:15Z","timestamp":1590119115000},"page":"11-19","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":14,"special_numbering":"C","title":["Synergistic antimicrobial activity of melittin with clindamycin on the expression of encoding exfoliative toxin in Staphylococcus aureus"],"prefix":"10.1016","volume":"183","author":[{"given":"Hassan","family":"Mahmoudi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohammad Yousef","family":"Alikhani","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Abbas Ali","family":"Imani Fooladi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2020.05.004_bib1","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1046\/j.1523-1747.2002.01751.x","article-title":"Staphylococcal exfoliative toxin B specifically cleaves desmoglein 1","volume":"118","author":"Amagai","year":"2002","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.toxicon.2020.05.004_bib2","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1007\/s10096-018-3189-7","article-title":"Highly synergistic activity of melittin with imipenem and colistin in biofilm inhibition against multidrug-resistant strong biofilm producer strains of Acinetobacter baumannii","volume":"37","author":"Bardbari","year":"2018","journal-title":"Eur. J. Clin. Microbiol. Infect."},{"key":"10.1016\/j.toxicon.2020.05.004_bib3","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1128\/AAC.48.5.1526-1533.2004","article-title":"Antibacterial activities of rhodamine B-conjugated gelsolin-derived peptides compared to those of the antimicrobial peptides cathelicidin LL37, magainin II, and melittin","volume":"48","author":"Bucki","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.toxicon.2020.05.004_bib4","doi-asserted-by":"crossref","first-page":"6483","DOI":"10.3892\/mmr.2015.4275","article-title":"Melittin, a honeybee venom-derived antimicrobial peptide, may target methicillin-resistant Staphylococcus aureus","volume":"12","author":"Choi","year":"2015","journal-title":"Mol. Med. Rep."},{"key":"10.1016\/j.toxicon.2020.05.004_bib5","series-title":"Performance Standards for Antimicrobial Susceptibility Testing of Anaerobic Bacteria: Informational Supplement: Clinical and Laboratory Standards Institute (CLSI); 2018","author":"Cockerill","year":"2018"},{"key":"10.1016\/j.toxicon.2020.05.004_bib6","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1016\/S0006-291X(03)00999-9","article-title":"A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties","volume":"306","author":"Conlon","year":"2003","journal-title":"Biochem Bioph Res co"},{"key":"10.1016\/j.toxicon.2020.05.004_bib7","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1179\/1973947812Y.0000000007","article-title":"In vitro activities of antimicrobial cationic peptides; melittin and nisin, alone or in combination with antibiotics against Gram-positive bacteria","volume":"24","author":"Dosler","year":"2012","journal-title":"Chemotherapy"},{"key":"10.1016\/j.toxicon.2020.05.004_bib8","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.peptides.2013.08.008","article-title":"In vitro pharmacokinetics of antimicrobial cationic peptides alone and in combination with antibiotics against methicillin resistant Staphylococcus aureus biofilms","volume":"49","author":"Dosler","year":"2013","journal-title":"Peptides"},{"key":"10.1016\/j.toxicon.2020.05.004_bib9","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1128\/AAC.04773-14","article-title":"In vitro spectrum of pexiganan activity when tested against pathogens from diabetic foot infections and with selected resistance mechanisms","volume":"59","author":"flamm","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.toxicon.2020.05.004_bib10","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/j.etap.2013.06.009","article-title":"Melittin: a lytic peptide with anticancer properties","volume":"36","author":"Gajski","year":"2013","journal-title":"Environ. Toxicol. Pharmacol."},{"key":"10.1016\/j.toxicon.2020.05.004_bib11","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.phymed.2014.11.019","article-title":"Pharmacological synergism of bee venom and melittin with antibiotics and plant secondary metabolites against multi-drug resistant microbial pathogens","volume":"22","author":"Issam","year":"2015","journal-title":"Phytomedicine"},{"key":"10.1016\/j.toxicon.2020.05.004_bib12","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/0014-5793(90)81253-K","article-title":"Revised structure of the peptide lactone antibiotic, TL\u2010119 and\/or A\u20103302\u2010B","volume":"270","author":"Kitajima","year":"1990","journal-title":"FEBS Lett."},{"key":"10.1016\/j.toxicon.2020.05.004_bib13","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1590\/0001-3765201520130511","article-title":"Antimicrobial activity of apitoxin, melittin and phospholipase A2 of honey bee (Apis mellifera) venom against oral pathogens","volume":"87","author":"Leandro","year":"2015","journal-title":"An. Acad. Bras. Cienc."},{"key":"10.1016\/j.toxicon.2020.05.004_bib14","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2\u2212 \u0394\u0394CT method","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"10.1016\/j.toxicon.2020.05.004_bib15","first-page":"26","article-title":"Isolating melittin from bee venom and evaluating its effect on proliferation of gastric cancer cells","volume":"5","author":"Mahmoodzadeh","year":"2013","journal-title":"Basic Clin. Canc. Res."},{"key":"10.1016\/j.toxicon.2020.05.004_bib16","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.jgar.2016.10.007","article-title":"Molecular analysis of the coagulase gene in clinical and nasal carrier isolates of methicillin-resistant Staphylococcus aureus by restriction fragment length polymorphism","volume":"8","author":"Mahmoudi","year":"2017","journal-title":"J. Glob. Antimicrob. Resist."},{"key":"10.1016\/j.toxicon.2020.05.004_bib17","first-page":"24","article-title":"Study of polymorphism spa gene (encoding protein A) of Staphylococcus aureus in clinical isolates and nasal carriers","volume":"73","author":"Mahmoudi","year":"2015","journal-title":"Tehran Univ. Med. J."},{"key":"10.1016\/j.toxicon.2020.05.004_bib18","doi-asserted-by":"crossref","first-page":"66","DOI":"10.12968\/jowc.2019.28.2.66","article-title":"Biofilm formation and antibiotic resistance in meticillin-resistant and meticillin-sensitive Staphylococcus aureus isolated from burns","volume":"28","author":"Mahmoudi","year":"2019","journal-title":"J. Wound Care"},{"key":"10.1016\/j.toxicon.2020.05.004_bib19","series-title":"Exfoliative Toxins of Staphylococcus aureus. The Rise of Virulence and Antibiotic Resistance in Staphylococcus aureus","first-page":"127","author":"Mariutti","year":"2017"},{"key":"10.1016\/j.toxicon.2020.05.004_bib20","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep29707","article-title":"Evaluation of short synthetic antimicrobial peptides for treatment of drug-resistant and intracellular Staphylococcus aureus","volume":"6","author":"Mohamed","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.toxicon.2020.05.004_bib21","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.jdermsci.2007.05.007","article-title":"Staphylococcal exfoliative toxins:\u201cmolecular scissors\u201d of bacteria that attack the cutaneous defense barrier in mammals","volume":"49","author":"Nishifuji","year":"2008","journal-title":"J. Dermatol. Sci."},{"key":"10.1016\/j.toxicon.2020.05.004_bib22","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.peptides.2014.01.026","article-title":"Functional characterization of naturally occurring melittin peptide isoforms in two honey bee species, Apis mellifera and Apis cerana","volume":"53","author":"Park","year":"2014","journal-title":"Peptides"},{"key":"10.1016\/j.toxicon.2020.05.004_bib23","doi-asserted-by":"crossref","first-page":"5363","DOI":"10.1128\/AAC.03163-14","article-title":"A broad-spectrum antibiofilm peptide enhances antibiotic action against bacterial biofilms","volume":"58","author":"Reffuveille","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.toxicon.2020.05.004_bib24","series-title":"Staphylococcus Aureus.[Updated 2017 Oct 9]. StatPearls [Internet]. Treasure Island","author":"Taylor","year":"2018"},{"key":"10.1016\/j.toxicon.2020.05.004_bib25","doi-asserted-by":"crossref","first-page":"6016","DOI":"10.1016\/S0021-9258(20)65098-0","article-title":"The structure of melittin. II. Interpretation of the structure","volume":"257","author":"Terwilliger","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2020.05.004_bib26","series-title":"Bailey & Scott's Diagnostic Microbiology-E-Book","author":"Tille","year":"2015"},{"key":"10.1016\/j.toxicon.2020.05.004_bib27","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1128\/CMR.00134-14","article-title":"Staphylococcus aureus infections: epidemiology, pathophysiology, clinical manifestations, and management","volume":"28","author":"Tong","year":"2015","journal-title":"Clin. Microbiol. Rev."}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010120302294?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010120302294?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T21:14:39Z","timestamp":1758575679000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010120302294"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,8]]},"references-count":27,"alternative-id":["S0041010120302294"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2020.05.004","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2020,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Synergistic antimicrobial activity of melittin with clindamycin on the expression of encoding exfoliative toxin in Staphylococcus aureus","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2020.05.004","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}