کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8749202 | 1593666 | 2018 | 35 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of a novel potential peptide import system in Treponema denticola
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کلمات کلیدی
qRT-PCRcRNATreponema denticolaABC transporter - ABC حمل کنندهcDNA - cDNAComplementary DNA - DNA تکمیلیcomplementary RNA - RNA مکملanalysis of variance - تحلیل واریانسANOVA - تحلیل واریانس Analysis of variancePeptide uptake - جذب پپتیدtwo-dimensional - دو بعدیquantitative reverse transcription-PCR - رونویسی معکوس PCRpolymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
ایمنی شناسی و میکروب شناسی
میکروب شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Treponema denticola is a major etiologic agent of chronic periodontitis. On the outer sheath of T. denticola, several proteins, such as the major outer sheath protein and dentilisin were detected, and among them, a 95â¯kDa protein which has not yet been characterized. The aim of this study was to characterize the function of this 95â¯kDa protein containing gene cluster. A gene encoding this 95â¯kDa protein (TDE_1072) of T. denticola was inactivated by homologous recombination. We compared growth curves between the TDE_1072 mutant and wild-type strains as well as differences in gene expression by DNA microarray analysis. Differential expression of genes identified by microarray analysis was confirmed by quantitative reverse transcription-polymerase chain reaction. The proteins encoded by TDE_1072, TDE_1073, TDE_1074, TDE_1075, and TDE_1076 shared respective similarities to the substrate-binding domain (DppA) of an ABC-type dipeptide/oligopeptide/nickel transport system, and to the permease components (DppB and DppC) and ATPase components (DppD and DppF) of an ABC-type dipeptide/oligopeptide/nickel transport system. Inactivation of dppA attenuated the growth of T. denticola and dppA-dppF were co-transcribed. In contrast, expression of oppB-oppF was up-regulated in the mutant. Our findings indicate that TDE_1072 may be a potential periplasmic solute binding protein encoded by dppA that is involved in the organization of a peptide uptake system with dppB-dppF.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Microbial Pathogenesis - Volume 123, October 2018, Pages 467-472
Journal: Microbial Pathogenesis - Volume 123, October 2018, Pages 467-472
نویسندگان
Tomohiro Asai, Kazuko Okamoto-Shibayama, Yuichiro Kikuchi, Kazuyuki Ishihara,