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Publication Open Access การแสดงออกของรีคอมบิแนนท์โปรตีนเปลือกนอกของเชื้อไวรัสโรคขนและจงอยปากผิดปกติโดยใช้ระบบเชื้อยิสต์ Pichiapastoris(2557) ลดาวัลย์ สาริยา; ปรุศก์ สุกใส; อดิศักดิ์ ส่งแจ้ง; ภิรมย์ พรมพิราม; มหาวิทยาลัยมหิดล. คณะสัตวแพทยศาสตร์. ศูนย์เฝ้าระวังและติดตามโรคจากสัตว์ป่า สัตว์ต่างถิ่นและสัตว์อพยพdeformities. Development of vaccine and detection of the disease is difficult and ineffective due to this virus could not be cultured in tissue or cell lines and embryonated eggs. The aim of this study was to express recombinant capsid protein of BFDV using... Pichia pastoris system. The recombinant protein was purified by affinity binding with Ni-NTA resin. From the results, the time point of protein expression was 48 hours after inducing with methanol. The recombinant capsid protein was expressedPublication Open Access การแสดงออกของรีคอมบิแนนท์โปรตีนเปลือกนอกของเชื้อไวรัสโรคขนและจงอยปากผิดปกติโดยใช้ระบบเชื้อยิสต์ Pichiapastoris(2557) ลดาวัลย์ สาริยา; ปรุศก์ สุกใส; อดิศักดิ์ ส่งแจ้ง; ภิรมย์ พรมพิราม; มหาวิทยาลัยมหิดล. คณะสัตวแพทยศาสตร์. ศูนย์เฝ้าระวังและติดตามโรคจากสัตว์ป่่า สัตว์ต่างถิ่นและสัตว์อพยพ; มหาวิทยาลัยมหิดล. คณะแพทยศาสตร์ศิริราชพยาบาล. หน่วยวิจัยโรคไข้เลือดออก. Development of vaccine and detection of the disease is difficult and ineffective due to this virus could not be cultured in tissue or cell lines and embryonated eggs. The aim of this study was to express recombinant capsid protein of BFDV using Pichia pastoris... system. The recombinant protein was purified by affinity binding with Ni-NTA resin. From the results, the time point of protein expression was 48 hours after inducing with methanol. The recombinant capsid protein was expressed in inclusion bodies formItem Open Access Development of quantitative polymerase chain reaction assay for detection of scale drop disease virus (SDDV) in Asian sea bass(Mahidol University, 2021) Sukhontip Sriisan; Chuenchit Boonchird; Siripong Thitamadee; Saengchan SenapinGreen qPCR assay for rapid detection of SDDV. Specific primers targeting a 135-bp fragment of ATPase coding gene and a 121-bp fragment of major capsid protein (MCP) coding gene of the SDDV genome were newly designed. The optimized qPCR conditions usingPublication Open Access Inhibition of p38MAPK and CD137 signaling reduce dengue virus-induced TNF-α secretion and apoptosis(2013) Amar Nagila; Janjuree Netsawang; Aroonroong Suttitheptumrong; Atthapan Morchang; Sasiprapa Khunchai; Chatchawan Srisawat; Chunya Puttikhunt; Sansanee Noisakran; Pa-thai Yenchitsomanus; Thawornchai Limjindaporn; Mahidol University. Faculty of Medicine Siriraj Hospital. Division of Molecular Medicinethe molecular mechanisms of DENV-induced hepatic injury could facilitate the development of alternate chemotherapeutic agents and improved therapies. Findings: The p38 mitogen-activated protein kinase (MAPK) participates in both apoptosis-related signalingPublication Open Access Inhibition of protein kinase C promotes dengue virus replication(2016) Warobon Noppakunmongkolchai; Teera Poyomtip; Thichakorn Jittawuttipoka; Natthanej Luplertlop; Anavaj Sakuntabhai; Sarin Chimnaronk; Siwanon Jirawatnotai; Rutaiwan Tohtong; Mahidol University. Faculty of Science. Systems Biology of Diseases Research Unit-stranded RNA genome, which encodes ten viral proteins. Thus, the viral life cycle is necessarily rely on or regulated by host factors. Methods: In silico analyses in conjunction with in vitro kinase assay were used to study kinases that potentially... indicated that the non-structural protein 5 (NS5), especially the RNA-dependent RNA polymerase (RdRp) domain, contains conserved phosphorylation sites for protein kinase C (PKC). Phosphorylation of NS5 RdRp was further verified by PKC in vitro kinase assayPublication Open Access Proteomic analysis of Chikungunya virus infected microgial cells(2012-04) Bizunesh Abere; Nitwara Wikan; Sukathida Ubol; Prasert Auewarakul; Atchara Paemanee; Suthathip Kittisenachai; Sittiruk Roytrakul; Duncan R. Smith; Mahidol University. Institute of Molecular Biosciences. Molecular Pathology Laboratory; Mahidol University. Faculty of Science. Department of Microbiology; Mahidol University. Center for Emerging and Neglected Infectious Disease.analysis of CHIKV infected and mock infected cells identified some 1455 individual proteins, of which 90 proteins, belonging to diverse cellular pathways, were significantly down regulated at a significance level of p<0.01. Analysis of the protein profilePublication Open Access Dengue 2 infection of HepG2 liver cells results in endoplasmic reticulum stress and induction of multiple pathways of cell death(2013) Chutima Thepparit; Khakpoor, Atefeh; Sarawut Khongwichit; Nitwara Wikan; Chanida Fongsaran; Pimjai Chingsuwanrote; Patcharee Panraksa; Smith, Duncan R; Mahidol University. Institute of Molecular Biosciences. Molecular Pathology Laboratory; Mahidol University. Center for Emerging and Neglected Infectious DiseasesIn response to DENV infection, HepG2 cells showed the induction of both the ER resident unfolded protein response as well as the Noxa/PUMA stress response pathways. Proteolytic activation of caspases 4, 7, 8 and 9 was observed as well as changesPublication Open Access Genetic variations in regions of bovine and bovine-like enteroviral 5’UTR from cattle, Indian bison and goat feces(2016) Nathamon Kosoltanapiwat; Marnoch Yindee; Chavez, Irwin Fernandez; Pornsawan Leaungwutiwong; Poom Adisakwattana; Pratap Singhasivanon; Charin Thawornkuno; Narin Thippornchai; Amporn Rungruengkitkun; Juthamas Soontorn; Sasipan Pearsiriwuttipong; Mahidol University. Faculty of Tropical Medicine. Department of Microbiology and ImmunologyBackground: Bovine enteroviruses (BEV) are members of the genus Enterovirus in the family Picornaviridae. They are predominantly isolated from cattle feces, but also are detected in feces of other animals, including goats and deer. These viruses are found in apparently healthy animals, as well as in animals with clinical signs and several studies reported recently suggest a potential role of BEV in causing disease in animals. In this study, we surveyed the presence of BEV in domestic and wild animals in Thailand, and assessed their genetic variability. Methods: Viral RNA was extracted from fecal samples of cattle, domestic goats, Indian bison (gaurs), and deer. The 5’ untranslated region (5’UTR) was amplified by nested reverse transcription-polymerase chain reaction (RT-PCR) with primers specific to BEV 5’UTR. PCR products were sequenced and analyzed phylogenetically using the neighbor-joining algorithm to observe genetic variations in regions of the bovine and bovine-like enteroviral 5’UTR found in this study. Results: BEV and BEV-like sequences were detected in the fecal samples of cattle (40/60, 67 %), gaurs (3/30, 10 %), and goats (11/46, 24 %). Phylogenetic analyses of the partial 5’UTR sequences indicated that different BEV variants (both EV-E and EV-F species) co-circulated in the domestic cattle, whereas the sequences from gaurs and goats clustered according to the animal species, suggesting that these viruses are host species-specific. Conclusions: Varieties of BEV and BEV-like 5’UTR sequences were detected in fecal samples from both domestic and wild animals. To our knowledge, this is the first report of the genetic variability of BEV in Thailand.Publication Open Access Permeability changes of integrin-containing multivesicular structures triggered by picornavirus entry.(2014-10-09) Pan Soonsawad; แพน สุ่นสวัสดิ์; Wattana Weerachatyanukul; วัฒนา วีรชาติยานุกูล; Paavolainen, Lassi; Upla, Paula; Rintanen, Nina; Espinoza, Juan; McNerney, Gregory; Marjomäki, Varpu; Cheng, R. Holland; Mahidol University. Faculty of Dentistry. Department of AnatomyCellular uptake of clustered α2β1-integrin induces the formation of membrane compartments that subsequently mature into a multivesicular body (MVB). Enhanced internalization mediated by clustered integrins was observed upon infection by the picornavirus echovirus 1 (EVI). We elucidated the structural features of virus-induced MVBs (vMVBs) in comparison to antibody-induced control MVBs (mock infection) by means of high-pressure cryo fixation of cells followed by immuno electron tomography during early entry of the virus. Three-dimensional tomograms revealed a marked increase in the size and complexity of these vMVBs and the intraluminal vesicles (ILVs) at 2 and 3.5 hours post infection (p.i.), in contrast to the control MVBs without virus. Breakages in the membranes of vMVBs were detected from tomograms after 2 and especially after 3.5 h suggesting that these breakages could facilitate the genome release to the cytoplasm. The in situ neutral-red labeling of viral genome showed that virus uncoating starts as early as 30 min p.i., while an increase of permeability was detected in the vMVBs between 1 and 3 hours p.i., based on a confocal microscopy assay. Altogether, the data show marked morphological changes in size and permeability of the endosomes in the infectious entry pathway of this non-enveloped enterovirus and suggest that the formed breakages facilitate the transfer of the genome to the cytoplasm for replication.Publication Open Access Enzymatic analysis of recombinant Japanese encephalitis virus NS2B(H)-NS3pro protease with fluorogenic model peptide substrates(2012-05) Muhammad Junaid; Chakard Chalayut; Anna Sehgelmeble Torrejon; Chanan Angsuthanasombat; Iryna Shutava; Maris Lapins; Jarl E. S. Wikberg; Gerd Katzenmeier; Mahidol University. Institute of Molecular Biosciences. Laboratory of Molecular and Cellular Microbiology(SOE-PCR) and cloned into the pTrcHisA vector. Hexahistidine-tagged NS2B(H)-NS3pro, expressed in E. coli as soluble protein, was purified to >95% purity by a single-step immobilized metal affinity chromatography. SDS-PAGE and immunoblotting
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