{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T11:05:40Z","timestamp":1789643140894,"version":"4.0.0"},"reference-count":33,"publisher":"American Society for Microbiology","issue":"15","license":[{"start":{"date-parts":[[2016,8,1]],"date-time":"2016-08-01T00:00:00Z","timestamp":1470009600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000072","name":"HHS | NIH | National Institute of Dental and Craniofacial Research","doi-asserted-by":"publisher","award":["DE017382"],"award-info":[{"award-number":["DE017382"]}],"id":[{"id":"10.13039\/100000072","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2016,8]]},"abstract":"ABSTRACT<\/jats:title>\n \n The Gram-positive bacterium\n Actinomyces<\/jats:named-content>\n oris<\/jats:italic>\n , a key colonizer in the development of oral biofilms, contains 18 LPXTG motif-containing proteins, including fimbrillins that constitute two fimbrial types critical for adherence, biofilm formation, and polymicrobial interactions. Export of these protein precursors, which harbor a signal peptide, is thought to be mediated by the Sec machine and require cleavage of the signal peptide by type I signal peptidases (SPases). Like many Gram-positive bacteria,\n A. oris<\/jats:named-content>\n expresses two SPases, named LepB1 and LepB2. The latter has been linked to suppression of lethal \u201cglyco-stress,\u201d caused by membrane accumulation of the LPXTG motif-containing glycoprotein GspA when the housekeeping sortase\n srtA<\/jats:italic>\n is genetically disrupted. Consistent with this finding, we show here that a mutant lacking\n lepB2<\/jats:italic>\n and\n srtA<\/jats:italic>\n was unable to produce high levels of glycosylated GspA and hence was viable. However, deletion of neither\n lepB1<\/jats:italic>\n nor\n lepB2<\/jats:italic>\n abrogated the signal peptide cleavage and glycosylation of GspA, indicating redundancy of SPases for GspA. In contrast, the\n lepB2<\/jats:italic>\n deletion mutant failed to assemble the wild-type levels of type 1 and 2 fimbriae, which are built by the shaft fimbrillins FimP and FimA, respectively; this phenotype was attributed to aberrant cleavage of the fimbrillin signal peptides. Furthermore, the\n lepB2<\/jats:italic>\n mutants, including the catalytically inactive S101A and K169A variants, exhibited significant defects in polymicrobial interactions and biofilm formation. Conversely,\n lepB1<\/jats:italic>\n was dispensable for the aforementioned processes. These results support the idea that LepB2 is specifically utilized for processing of fimbrial proteins, thus providing an experimental model with which to study the basis of type I SPase specificity.\n <\/jats:p>\n \n IMPORTANCE<\/jats:bold>\n Sec-mediated translocation of bacterial protein precursors across the cytoplasmic membrane involves cleavage of their signal peptide by a signal peptidase (SPase). Like many Gram-positive bacteria,\n A. oris<\/jats:named-content>\n expresses two SPases, LepB1 and LepB2. The latter is a genetic suppressor of lethal \u201cglyco-stress\u201d caused by membrane accumulation of glycosylated GspA when the housekeeping sortase\n srtA<\/jats:italic>\n is genetically disrupted. We show here that LepB1 and LepB2 are capable of processing GspA, whereas only LepB2 is required for cleavage of fimbrial signal peptides. This is the first example of a type I SPase dedicated to LPXTG motif-containing fimbrial proteins. Thus,\n A. oris<\/jats:named-content>\n provides an experimental model with which to investigate the specificity mechanism of type I SPases.\n <\/jats:p>","DOI":"10.1128\/jb.00353-16","type":"journal-article","created":{"date-parts":[[2016,5,24]],"date-time":"2016-05-24T04:45:55Z","timestamp":1464065155000},"page":"2064-2073","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":21,"title":["A Type I Signal Peptidase Is Required for Pilus Assembly in the Gram-Positive, Biofilm-Forming Bacterium Actinomyces\n oris<\/i>"],"prefix":"10.1128","volume":"198","author":[{"given":"Sara D.","family":"Siegel","sequence":"first","affiliation":[{"name":"Department of Microbiology & Molecular Genetics, University of Texas Health Science Center, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chenggang","family":"Wu","sequence":"additional","affiliation":[{"name":"Department of Microbiology & Molecular Genetics, University of Texas Health Science Center, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hung","family":"Ton-That","sequence":"additional","affiliation":[{"name":"Department of Microbiology & Molecular Genetics, University of Texas Health Science Center, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1128\/9781555817107.ch5","volume-title":"Genomic inquiries into oral bacterial communities","author":"Ton-That H","year":"2011","unstructured":"Ton-That H, Das A, Mishra A. 2011. Actinomyces oris fimbriae: an adhesive principle in bacterial biofilms and tissue tropism, p 63\u201377. In Kolenbrander PE (ed), Genomic inquiries into oral bacterial communities. ASM Press, Washington, DC."},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1177\/10454411990100020101"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01952-06"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00173-11"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07745.x"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2010.07252.x"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1321417111"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1111\/mmi.12780"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2013.12.003"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2004.04.014"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.70.1.192-221.2006"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07887.x"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.resmic.2004.10.011"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M115.672253"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00769-15"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gku673"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.00811-10"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1038\/nprot.2008.73"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00093-12"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00248-014-0400-y"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00500-13"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.00467-15"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkt1103"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1111\/mmi.13023"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1002\/pro.757"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2004.05.006"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2013.11.009"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00627-09"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01520-07"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jsb.2013.05.021"},{"key":"e_1_3_3_32_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0099135"},{"key":"e_1_3_3_33_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.185.9.2910-2919.2003"},{"key":"e_1_3_3_34_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/22.22.4673"}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.00353-16","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.00353-16","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T17:41:11Z","timestamp":1627580471000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/JB.00353-16"}},"subtitle":[],"editor":[{"given":"O.","family":"Schneewind","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2016,8]]},"references-count":33,"journal-issue":{"issue":"15","published-print":{"date-parts":[[2016,8]]}},"alternative-id":["10.1128\/JB.00353-16"],"URL":"https:\/\/doi.org\/10.1128\/jb.00353-16","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,8]]},"assertion":[{"value":"2016-04-27","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2016-05-15","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2016-07-13","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}