{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T17:47:02Z","timestamp":1761587222211,"version":"build-2065373602"},"reference-count":60,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T00:00:00Z","timestamp":1761523200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100006492","name":"Division of Intramural Research, National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI146073"],"award-info":[{"award-number":["R01AI146073"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006492","name":"Division of Intramural Research, National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R21AI148981"],"award-info":[{"award-number":["R21AI148981"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    The\n                    <jats:italic>Neisseria gonorrhoeae<\/jats:italic>\n                    Type IV pilus is a dynamic fiber involved in host cell attachment, DNA transformation, twitching motility, and evading the innate immune system. We previously reported that pilus expression affects iron homeostasis and sensitivity to killing by oxidative (iron-dependent antibiotic streptonigrin and hydrogen peroxide and non-oxidative (antimicrobial peptide LL-37) agents. Here, we use\n                    <jats:italic>in vitro<\/jats:italic>\n                    evolution to identify genes involved in\n                    <jats:italic>N. gonorrhoeae<\/jats:italic>\n                    susceptibility to streptonigrin. We identified a mutation in the NGO0059 locus that encodes HpaC that results in a glycine to cysteine change in position 93. Although HpaC homologs are known as part of a two-component FAD-dependent monooxygenase system consisting of an\n                    <jats:italic>hpaC<\/jats:italic>\n                    reductase and an\n                    <jats:italic>hpaB<\/jats:italic>\n                    monooxygenase,\n                    <jats:italic>Neisseria<\/jats:italic>\n                    lack the monooxygenase. While HpaC increases streptonigrin sensitivity, HpaC also promotes hydrogen peroxide and LL-37 resistance. We tested whether the HpaC effect in streptonigrin, hydrogen peroxide and LL-37 sensitivity involved the Type IV pilus. We determined that HpaC affects streptonigrin independently of the pilus while hydrogen peroxide- and LL-37-mediated killing involves both HpaC and the pilus. We demonstrate that the Gly93Cys change conferred enhanced affinity for FAD and resulted in a loss-of-function phenotype in streptonigrin susceptibility. These data suggest that HpaC\u2019s role in FAD oxidation and reduction impacts pilus-dependent and -independent resistance against neutrophil-mediated killing.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1013607","type":"journal-article","created":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T17:41:01Z","timestamp":1761586861000},"page":"e1013607","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":0,"title":["Flavin affinity for the reductase HpaC differentially sensitizes Neisseria gonorrhoeae during Type IV pilus-dependent killing"],"prefix":"10.1371","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6959-3137","authenticated-orcid":true,"given":"Linda I.","family":"Hu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Egon A.","family":"Ozer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H. S.","family":"Seifert","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2025,10,27]]},"reference":[{"key":"ppat.1013607.ref001","first-page":"197","article-title":"Gonorrhea infection in women: prevalence, effects, screening, and management","volume":"3","author":"CK Walker","year":"2011","journal-title":"Int J Womens Health"},{"issue":"2","key":"ppat.1013607.ref002","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/S1521-6942(02)00125-0","article-title":"Gonococcal arthritis","volume":"17","author":"T Bardin","year":"2003","journal-title":"Best Pract Res Clin Rheumatol"},{"issue":"5","key":"ppat.1013607.ref003","doi-asserted-by":"crossref","DOI":"10.1086\/319204","article-title":"Gonococcemia associated with fatal septic shock","volume":"32","author":"G Thi\u00e9ry","year":"2001","journal-title":"Clin Infect Dis"},{"issue":"4","key":"ppat.1013607.ref004","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1053\/j.spid.2005.06.006","article-title":"Gonococcal infections in neonates and young children","volume":"16","author":"CR Woods","year":"2005","journal-title":"Semin Pediatr Infect Dis"},{"key":"ppat.1013607.ref005","doi-asserted-by":"crossref","first-page":"3044","DOI":"10.3389\/fimmu.2018.03044","article-title":"Macrophage-Neisseria gonorrhoeae Interactions: A Better Understanding of Pathogen Mechanisms of Immunomodulation","volume":"9","author":"A Escobar","year":"2018","journal-title":"Front Immunol"},{"issue":"3","key":"ppat.1013607.ref006","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1111\/j.1462-5822.2009.01404.x","article-title":"Bacterial membrane vesicles deliver peptidoglycan to NOD1 in epithelial cells","volume":"12","author":"M Kaparakis","year":"2010","journal-title":"Cell Microbiol"},{"issue":"9","key":"ppat.1013607.ref007","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004341","article-title":"Global analysis of neutrophil responses to Neisseria gonorrhoeae reveals a self-propagating inflammatory program","volume":"10","author":"A Sintsova","year":"2014","journal-title":"PLoS Pathog"},{"issue":"3","key":"ppat.1013607.ref008","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/nri1312","article-title":"NOX enzymes and the biology of reactive oxygen","volume":"4","author":"JD Lambeth","year":"2004","journal-title":"Nat Rev Immunol"},{"issue":"2","key":"ppat.1013607.ref009","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1152\/physrev.00012.2018","article-title":"The Neutrophil\u2019s Role During Health and Disease","volume":"99","author":"PX Liew","year":"2019","journal-title":"Physiol Rev"},{"issue":"7","key":"ppat.1013607.ref010","first-page":"3919","article-title":"The antimicrobial peptides and their potential clinical applications","volume":"11","author":"J Lei","year":"2019","journal-title":"Am J Transl Res"},{"issue":"3","key":"ppat.1013607.ref011","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1038\/nrmicro2713","article-title":"A bacterial siren song: intimate interactions between Neisseria and neutrophils","volume":"10","author":"AK Criss","year":"2012","journal-title":"Nat Rev Microbiol"},{"issue":"2","key":"ppat.1013607.ref012","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1111\/j.1365-2958.2005.04839.x","article-title":"The transcriptome response of Neisseria gonorrhoeae to hydrogen peroxide reveals genes with previously uncharacterized roles in oxidative damage protection","volume":"58","author":"EA Stohl","year":"2005","journal-title":"Mol Microbiol"},{"issue":"11","key":"ppat.1013607.ref013","doi-asserted-by":"crossref","first-page":"2257","DOI":"10.1111\/j.1462-5822.2008.01205.x","article-title":"Neisseria gonorrhoeae suppresses the oxidative burst of human polymorphonuclear leukocytes","volume":"10","author":"AK Criss","year":"2008","journal-title":"Cell Microbiol"},{"issue":"1","key":"ppat.1013607.ref014","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.02452-14","article-title":"Neisseria gonorrhoeae elicits extracellular traps in primary neutrophil culture while suppressing the oxidative burst","volume":"6","author":"CW Gunderson","year":"2015","journal-title":"mBio"},{"issue":"7","key":"ppat.1013607.ref015","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1111\/j.1462-5822.2009.01308.x","article-title":"Resistance of Neisseria gonorrhoeae to non-oxidative killing by adherent human polymorphonuclear leucocytes","volume":"11","author":"AK Criss","year":"2009","journal-title":"Cell Microbiol"},{"key":"ppat.1013607.ref016","doi-asserted-by":"crossref","first-page":"77","DOI":"10.3389\/fmicb.2011.00077","article-title":"Resistance of Neisseria gonorrhoeae to neutrophils","volume":"2","author":"MB Johnson","year":"2011","journal-title":"Front Microbiol"},{"issue":"2","key":"ppat.1013607.ref017","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.micpath.2004.04.007","article-title":"A Neisseria gonorrhoeae catalase mutant is more sensitive to hydrogen peroxide and paraquat, an inducer of toxic oxygen radicals","volume":"37","author":"AA Soler-Garc\u00eda","year":"2004","journal-title":"Microb Pathog"},{"issue":"10","key":"ppat.1013607.ref018","doi-asserted-by":"crossref","first-page":"3463","DOI":"10.1128\/JB.188.10.3463-3469.2006","article-title":"Ecf, an alternative sigma factor from Neisseria gonorrhoeae, controls expression of msrAB, which encodes methionine sulfoxide reductase","volume":"188","author":"IC Gunesekere","year":"2006","journal-title":"J Bacteriol"},{"issue":"6","key":"ppat.1013607.ref019","article-title":"The Neisseria gonorrhoeae type IV pilus promotes resistance to hydrogen peroxide- and LL-37-mediated killing by modulating the availability of intracellular, labile iron","volume":"18","author":"LI Hu","year":"2022","journal-title":"PLoS Pathog"},{"issue":"6","key":"ppat.1013607.ref020","doi-asserted-by":"crossref","first-page":"2744","DOI":"10.1172\/JCI117290","article-title":"Multiple gonococcal pilin antigenic variants are produced during experimental human infections","volume":"93","author":"HS Seifert","year":"1994","journal-title":"J Clin Invest"},{"issue":"5","key":"ppat.1013607.ref021","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1084\/jem.165.5.1344","article-title":"Gonococcal pilin variants in experimental gonorrhea","volume":"165","author":"J Swanson","year":"1987","journal-title":"J Exp Med"},{"issue":"6800","key":"ppat.1013607.ref022","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1038\/35024105","article-title":"Pilus retraction powers bacterial twitching motility","volume":"407","author":"AJ Merz","year":"2000","journal-title":"Nature"},{"issue":"10","key":"ppat.1013607.ref023","doi-asserted-by":"crossref","first-page":"4743","DOI":"10.1128\/IAI.00687-07","article-title":"Dynamics of Neisseria gonorrhoeae attachment: microcolony development, cortical plaque formation, and cytoprotection","volume":"75","author":"DL Higashi","year":"2007","journal-title":"Infect Immun"},{"issue":"3","key":"ppat.1013607.ref024","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1038\/nrmicro844","article-title":"DNA uptake during bacterial transformation","volume":"2","author":"I Chen","year":"2004","journal-title":"Nat Rev Microbiol"},{"issue":"4","key":"ppat.1013607.ref025","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00399-13","article-title":"Neisseria gonorrhoeae metalloprotease NGO1686 is required for full piliation, and piliation is required for resistance to H2O2- and neutrophil-mediated killing","volume":"4","author":"EA Stohl","year":"2013","journal-title":"mBio"},{"issue":"52","key":"ppat.1013607.ref026","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2312110120","article-title":"How a natural antibiotic uses oxidative stress to kill oxidant-resistant bacteria","volume":"120","author":"A Gupta","year":"2023","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"ppat.1013607.ref027","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.03025-23","article-title":"Development and implementation of a Type I-C CRISPR-based programmable repression system for Neisseria gonorrhoeae","volume":"15","author":"WE Geslewitz","year":"2024","journal-title":"mBio"},{"issue":"8","key":"ppat.1013607.ref028","article-title":"Phase variable DNA repeats in Neisseria gonorrhoeae influence transcription, translation, and protein sequence variation","volume":"2","author":"MA Zelewska","year":"2016","journal-title":"Microb Genom"},{"issue":"1","key":"ppat.1013607.ref029","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1177\/09680519020080010501","article-title":"Phase variable changes in genes lgtA and lgtC within the lgtABCDE operon of Neisseria gonorrhoeae can modulate gonococcal susceptibility to normal human serum","volume":"8","author":"WM Shafer","year":"2002","journal-title":"J Endotoxin Res"},{"issue":"3","key":"ppat.1013607.ref030","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1046\/j.1365-2958.2000.01873.x","article-title":"Phase variation of the gonococcal siderophore receptor FetA","volume":"36","author":"SD Carson","year":"2000","journal-title":"Mol Microbiol"},{"issue":"10","key":"ppat.1013607.ref031","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1128\/AAC.31.10.1507","article-title":"Role of extracellular iron in the action of the quinone antibiotic streptonigrin: mechanisms of killing and resistance of Neisseria gonorrhoeae","volume":"31","author":"MS Cohen","year":"1987","journal-title":"Antimicrob Agents Chemother"},{"issue":"2","key":"ppat.1013607.ref032","first-page":"391","article-title":"A simple assay of the superoxide generation rate with Tiron as an EPR-visible radical scavenger","volume":"13","author":"AN Ledenev","year":"1986","journal-title":"Biochem Int"},{"issue":"3","key":"ppat.1013607.ref033","doi-asserted-by":"crossref","first-page":"2014","DOI":"10.1074\/jbc.M109.056135","article-title":"Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD oxidoreductase (TftC) of Burkholderia cepacia AC1100","volume":"285","author":"BN Webb","year":"2010","journal-title":"J Biol Chem"},{"issue":"5","key":"ppat.1013607.ref034","doi-asserted-by":"crossref","DOI":"10.1016\/j.chembiol.2019.02.011","article-title":"Multi-metal restriction by calprotectin impacts de novo flavin biosynthesis in Acinetobacter baumannii","volume":"26","author":"J Wang","year":"2019","journal-title":"Cell Chemical Biology"},{"issue":"18","key":"ppat.1013607.ref035","doi-asserted-by":"crossref","DOI":"10.3390\/molecules28186699","article-title":"Advances in 4-hydroxyphenylacetate-3-hydroxylase monooxygenase","volume":"28","author":"K Yang","year":"2023","journal-title":"Molecules"},{"key":"ppat.1013607.ref036","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/S0014-5793(02)02659-5","article-title":"The presence of 4-hydroxyphenylacetic acid in human saliva and the possibility of its nitration by salivary nitrite in the stomach","volume":"518","author":"U Takahama","year":"2002","journal-title":"FEBS Lett"},{"issue":"2","key":"ppat.1013607.ref037","article-title":"4-Hydroxyphenylacetate 3-Hydroxylase (4HPA3H): A Vigorous Monooxygenase for Versatile O-Hydroxylation Applications in the Biosynthesis of Phenolic Derivatives","volume":"25","author":"P Sun","year":"2024","journal-title":"Int J Mol Sci"},{"issue":"21","key":"ppat.1013607.ref038","doi-asserted-by":"crossref","first-page":"5550","DOI":"10.1046\/j.1432-1033.2001.02490.x","article-title":"A novel two-protein component flavoprotein hydroxylase: p-hydroxyphenylacetate hydroxylase from Acinetobacter baumanii","volume":"268","author":"P Chaiyen","year":"2001","journal-title":"Eur J Biochem"},{"issue":"3","key":"ppat.1013607.ref039","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1002\/prot.21534","article-title":"Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity","volume":"70","author":"S-H Kim","year":"2008","journal-title":"Proteins"},{"issue":"45","key":"ppat.1013607.ref040","doi-asserted-by":"crossref","first-page":"33107","DOI":"10.1074\/jbc.M703440200","article-title":"Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8","volume":"282","author":"S-H Kim","year":"2007","journal-title":"J Biol Chem"},{"issue":"3","key":"ppat.1013607.ref041","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1007\/s00253-013-4958-y","article-title":"Catalytic activity of the two-component flavin-dependent monooxygenase from Pseudomonas aeruginosa toward cinnamic acid derivatives","volume":"98","author":"T Furuya","year":"2014","journal-title":"Appl Microbiol Biotechnol"},{"issue":"28","key":"ppat.1013607.ref042","doi-asserted-by":"crossref","first-page":"26435","DOI":"10.1074\/jbc.M501988200","article-title":"A two-component hydroxylase involved in the assimilation of 3-hydroxyphenyl acetate in Pseudomonas putida","volume":"280","author":"E Arias-Barrau","year":"2005","journal-title":"J Biol Chem"},{"issue":"12","key":"ppat.1013607.ref043","doi-asserted-by":"crossref","first-page":"4167","DOI":"10.1128\/aem.61.12.4167-4171.1995","article-title":"Polymer production by Klebsiella pneumoniae 4-hydroxyphenylacetic acid hydroxylase genes cloned in Escherichia coli","volume":"61","author":"A Gibello","year":"1995","journal-title":"Appl Environ Microbiol"},{"issue":"2","key":"ppat.1013607.ref044","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1128\/AEM.66.2.481-486.2000","article-title":"Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase","volume":"66","author":"L Xun","year":"2000","journal-title":"Appl Environ Microbiol"},{"issue":"3","key":"ppat.1013607.ref045","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1128\/JB.182.3.627-636.2000","article-title":"Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new Flavin:NAD(P)H reductase subfamily","volume":"182","author":"B Gal\u00e1n","year":"2000","journal-title":"J Bacteriol"},{"issue":"1","key":"ppat.1013607.ref046","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/S0021-9258(17)42327-1","article-title":"Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme","volume":"269","author":"U Arunachalam","year":"1994","journal-title":"J Biol Chem"},{"issue":"29","key":"ppat.1013607.ref047","doi-asserted-by":"crossref","first-page":"8611","DOI":"10.1021\/bi7006614","article-title":"Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase","volume":"46","author":"J Sucharitakul","year":"2007","journal-title":"Biochemistry"},{"issue":"2","key":"ppat.1013607.ref048","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1021\/bi901454u","article-title":"Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: a system composed of a small flavin reductase and a large flavin-dependent oxygenase","volume":"49","author":"S Chakraborty","year":"2010","journal-title":"Biochemistry"},{"issue":"24","key":"ppat.1013607.ref049","doi-asserted-by":"crossref","first-page":"7509","DOI":"10.1021\/bi034092r","article-title":"Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase","volume":"42","author":"TM Louie","year":"2003","journal-title":"Biochemistry"},{"key":"ppat.1013607.ref050","unstructured":"Gene Help [Internet]. Bethesda (MD): National Center for Biotechnology Information (US) [Internet]. Bethesda (MD): National Center for Biotechnology Information (US); 2008 Apr 21 [updated 2018 Apr 9]. https:\/\/www.ncbi.nlm.nih.gov\/books\/NBK3840\/"},{"issue":"7","key":"ppat.1013607.ref051","doi-asserted-by":"crossref","first-page":"2162","DOI":"10.1128\/jb.175.7.2162-2167.1993","article-title":"Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range","volume":"175","author":"MA Prieto","year":"1993","journal-title":"J Bacteriol"},{"issue":"1","key":"ppat.1013607.ref052","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1128\/jb.143.1.302-306.1980","article-title":"Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli","volume":"143","author":"RA Cooper","year":"1980","journal-title":"J Bacteriol"},{"key":"ppat.1013607.ref053","doi-asserted-by":"crossref","first-page":"124","DOI":"10.12688\/wellcomeopenres.14826.1","article-title":"Open-access bacterial population genomics: BIGSdb software, the PubMLST.org website and their applications","volume":"3","author":"KA Jolley","year":"2018","journal-title":"Wellcome Open Res"},{"issue":"24","key":"ppat.1013607.ref054","doi-asserted-by":"crossref","first-page":"7145","DOI":"10.1128\/JB.185.24.7145-7152.2003","article-title":"FarR regulates the farAB-encoded efflux pump of Neisseria gonorrhoeae via an MtrR regulatory mechanism","volume":"185","author":"E-H Lee","year":"2003","journal-title":"J Bacteriol"},{"issue":"4","key":"ppat.1013607.ref055","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1046\/j.1365-2958.1999.01530.x","article-title":"The farAB-encoded efflux pump mediates resistance of gonococci to long-chained antibacterial fatty acids","volume":"33","author":"EH Lee","year":"1999","journal-title":"Mol Microbiol"},{"issue":"13","key":"ppat.1013607.ref056","doi-asserted-by":"crossref","first-page":"4569","DOI":"10.1128\/JB.00286-07","article-title":"Differential regulation of ponA and pilMNOPQ expression by the MtrR transcriptional regulatory protein in Neisseria gonorrhoeae","volume":"189","author":"JP Folster","year":"2007","journal-title":"J Bacteriol"},{"issue":"9","key":"ppat.1013607.ref057","doi-asserted-by":"crossref","DOI":"10.1002\/cpz1.70000","article-title":"Genetic Manipulation of Neisseria gonorrhoeae and Commensal Neisseria Species","volume":"4","author":"JP Dillard","year":"2024","journal-title":"Curr Protoc"},{"issue":"5","key":"ppat.1013607.ref058","article-title":"Discovery of a New Neisseria gonorrhoeae Type IV Pilus Assembly Factor, TfpC","volume":"11","author":"LI Hu","year":"2020","journal-title":"Mbio"},{"issue":"4","key":"ppat.1013607.ref059","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1046\/j.1365-2958.1998.01089.x","article-title":"Differential roles of homologous recombination pathways in Neisseria gonorrhoeae pilin antigenic variation, DNA transformation and DNA repair","volume":"30","author":"IJ Mehr","year":"1998","journal-title":"Mol Microbiol"},{"key":"ppat.1013607.ref060","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1007\/978-1-4939-0554-6_12","article-title":"Identification of mutations in laboratory-evolved microbes from next-generation sequencing data using breseq","volume":"1151","author":"DE Deatherage","year":"2014","journal-title":"Methods Mol Biol"}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1013607","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T17:41:10Z","timestamp":1761586870000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1013607"}},"subtitle":[],"editor":[{"given":"William M","family":"Shafer","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2025,10,27]]},"references-count":60,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2025,10,27]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1013607","relation":{},"ISSN":["1553-7374"],"issn-type":[{"type":"electronic","value":"1553-7374"}],"subject":[],"published":{"date-parts":[[2025,10,27]]}}}