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The elicitin-like glycoprotein, ELI025, is secreted by the pathogenic oomycete pythium insidiosum and evades host antibody responses
Lerksuthirat T. - ไม่ระบุหน่วยงาน
ชื่อเรื่อง (EN): The elicitin-like glycoprotein, ELI025, is secreted by the pathogenic oomycete pythium insidiosum and evades host antibody responses
ผู้แต่ง / หัวหน้าโครงการ (EN): Lerksuthirat T.
บทคัดย่อ (EN): Pythium insidiosum is a unique oomycete that can infect humans and animals. Patients with a P. insidiosum infection (pythiosis) have high rates of morbidity and mortality. The pathogen resists conventional antifungal drugs. Information on the biology and pathogenesis of P. insidiosum is limited. Many pathogens secrete proteins, known as effectors, which can affect the host response and promote the infection process. Elicitins are secretory proteins and are found only in the oomycetes, primarily in Phytophthora and Pythium species. In plant-pathogenic oomycetes, elicitins function as pathogen-associated molecular pattern molecules, sterol carriers, and plant defense stimulators. Recently, we reported a number of elicitin-encoding genes from the P. insidiosum transcriptome. The function of elicitins during human infections is unknown. One of the P. insidiosum elicitin-encoding genes, ELI025, is highly expressed and up-regulated at body temperature. This study aims to characterize the biochemical, immunological, and genetic properties of the elicitin protein, ELI025. A 12.4-kDa recombinant ELI025 protein (rELI025) was expressed in Escherichia coli. Rabbit anti-rELI025 antibodies reacted strongly with the native ELI025 in P. insidiosum 's culture medium. The detected ELI025 had two isoforms: glycosylated and non-glycosylated. ELI025 was not immunoreactive with sera from pythiosis patients. The region near the transcriptional start site of ELI025 contained conserved oomycete core promoter elements. In conclusion, ELI025 is a small, abundant, secreted glycoprotein that evades host antibody responses. ELI025 is a promising candidate for development of diagnostic and therapeutic targets for pythiosis. © 2015 Lerksuthirat et al.
บทคัดย่อ: ไม่พบข้อมูลจากหน่วยงานต้นทาง
ภาษา (EN): en
เอกสารแนบ (EN): https://www.scopus.com/inward/record.uri?eid=2-s2.0-84925764194&doi=10.1371%2fjournal.pone.0118547&partnerID=40&md5=98a6454d0089590ede00c3a1bc5a46cc
เผยแพร่โดย (EN): มหาวิทยาลัยมหิดล
คำสำคัญ (EN): Transcriptome
เจ้าของลิขสิทธิ์ (EN): มหาวิทยาลัยมหิดล
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Lerksuthirat T.. "The elicitin-like glycoprotein, ELI025, is secreted by the pathogenic oomycete pythium insidiosum and evades host antibody responses". ไม่ระบุหน่วยงาน. ม.ป.ป.

Lerksuthirat T.. "The elicitin-like glycoprotein, ELI025, is secreted by the pathogenic oomycete pythium insidiosum and evades host antibody responses". ไม่ระบุหน่วยงาน. ม.ป.ป.. Print.



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The elicitin-like glycoprotein, ELI025, is secreted by the pathogenic oomycete pythium insidiosum and evades host antibody responses
Lerksuthirat T.
มหาวิทยาลัยมหิดล
ไม่ระบุวันที่เผยแพร่
Geographic variation in the elicitin-like glycoprotein, ELI025, of Pythium insidiosum isolated from human and animal subjects Transcriptome analysis reveals pathogenicity and evolutionary history of the pathogenic oomycete Pythium insidiosum The immunoreactive exo-1,3-β-glucanase from the pathogenic oomycete pythium insidiosum is temperature regulated and exhibits glycoside hydrolase activity Single nucleotide polymorphism-based multiplex PCR for identification and genotyping of the oomycete Pythium insidiosum from humans, animals and the environment Biochemical and genetic analyses of the oomycete Pythium insidiosum provide new insights into clinical identification and urease-based evolution of metabolismrelated traits HIV-1 envelope glycoproteins from diverse clades differentiate antibody responses and durability among vaccinees ScFv Antibody Specific to Cassiicolin, a Host-Selective Toxin of Corynespora cassiicola Shared and organism-specific host responses to childhood diarrheal diseases revealed by whole blood transcript profiling P-glycoprotein transporter in drug development Who acquires infection from whom and how? Disentangling multi-host and multimode transmission dynamics in the ‘elimination’ era
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