สืบค้นงานวิจัย
The immunoreactive exo-1,3-β-glucanase from the pathogenic oomycete pythium insidiosum is temperature regulated and exhibits glycoside hydrolase activity
Keeratijarut A. - ไม่ระบุหน่วยงาน
ชื่อเรื่อง (EN): The immunoreactive exo-1,3-β-glucanase from the pathogenic oomycete pythium insidiosum is temperature regulated and exhibits glycoside hydrolase activity
ผู้แต่ง / หัวหน้าโครงการ (EN): Keeratijarut A.
บทคัดย่อ (EN): The oomycete organism, Pythium insidiosum, is the etiologic agent of the life-threatening infectious disease called "pythiosis". Diagnosis and treatment of pythiosis is difficult and challenging. Novel methods for early diagnosis and effective treatment are urgently needed. Recently, we reported a 74-kDa immunodominant protein of P. insidiosum, which could be a diagnostic target, vaccine candidate, and virulence factor. The protein was identified as a putative exo-1,3-ß-glucanase (Exo1). This study reports on genetic, immunological, and biochemical characteristics of Exo1. The full-length exo1 coding sequence (2,229 bases) was cloned. Phylogenetic analysis showed that exo1 is grouped with glucanase-encoding genes of other oomycetes, and is far different from glucanase-encoding genes of fungi. exo1 was up-regulated upon exposure to body temperature, and its gene product is predicted to contain BglC and X8 domains, which are involved in carbohydrate transport, binding, and metabolism. Based on its sequence, Exo1 belongs to the Glycoside Hydrolase family 5 (GH5). Exo1, expressed in E. coli, exhibited ß-glucanase and cellulase activities. Exo1 is a major intracellular immunoreactive protein that can trigger host immune responses during infection. Since GH5 enzyme-encoding genes are not present in human genomes, Exo1 could be a useful target for drug and vaccine development against this pathogen. © 2015 Keeratijarut et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
บทคัดย่อ: ไม่พบข้อมูลจากหน่วยงานต้นทาง
ภาษา (EN): en
เอกสารแนบ (EN): https://www.scopus.com/inward/record.uri?eid=2-s2.0-84942852380&doi=10.1371%2fjournal.pone.0135239&partnerID=40&md5=874bc0bf301f39ae73e3afb9b5483a96
เผยแพร่โดย (EN): มหาวิทยาลัยมหิดล
คำสำคัญ (EN): Transcription, Genetic
เจ้าของลิขสิทธิ์ (EN): มหาวิทยาลัยมหิดล
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The immunoreactive exo-1,3-β-glucanase from the pathogenic oomycete pythium insidiosum is temperature regulated and exhibits glycoside hydrolase activity
Keeratijarut A.
มหาวิทยาลัยมหิดล
ไม่ระบุวันที่เผยแพร่
Transcriptome analysis reveals pathogenicity and evolutionary history of the pathogenic oomycete Pythium insidiosum The elicitin-like glycoprotein, ELI025, is secreted by the pathogenic oomycete pythium insidiosum and evades host antibody responses Biochemical and genetic analyses of the oomycete Pythium insidiosum provide new insights into clinical identification and urease-based evolution of metabolismrelated traits Single nucleotide polymorphism-based multiplex PCR for identification and genotyping of the oomycete Pythium insidiosum from humans, animals and the environment Evaluation of ethanol concentration, temperature and shaking time of extracted Thai Jasmine rice on cholinesterase enzyme activity Geographic variation in the elicitin-like glycoprotein, ELI025, of Pythium insidiosum isolated from human and animal subjects A novel bacteriocin from Enterococcus faecalis 478 exhibits a potent activity against vancomycin-resistant enterococci Effect of temperature on fimbrial gene expression and adherence of enteroaggregative Escherichia coli Mangosteen peel extract exhibits cellular antioxidant activity by induction of catalase and heme oxygenase-1 mRNA expression Agrobacterium tumefaciens estC, encoding an enzyme containing esterase activity, Is Regulated by EstR, a regulator in the MarR family
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