tailieunhanh - Báo cáo khoa học: Crystal structures of Nipah and Hendra virus fusion core proteins

The Nipah and Hendra viruses are highly pathogenic paramyxoviruses that recently emerged from flying foxes to cause serious disease outbreaks in humans and livestock in Australia, Malaysia, Singapore and Bangladesh. Their unique genetic constitution, high virulence and wide host range set them apart from other paramyxoviruses. These characteristics have led to their classification into the new genus Henpaviruswithin the family Para-myxoviridae and to their designation as Biosafety Level 4 pathogens. . | ễFEBS Journal Crystal structures of Nipah and Hendra virus fusion core proteins Zhiyong Lou1 2 Yanhui Xu1 2 Kehui Xiang1 Nan Su1 Lan Qin1 Xu Li1 George F. Gao3 Mark Bartlam1 2 and Zihe Rao1 2 4 1 Tsinghua-Nankai-IBP Joint Research Group for StructuralBiology Tsinghua University Beijing China 2 NationalLaboratory of Biomacromolecules IBP Chinese Academy of Sciences Beijing China 3 Center for Molecular Virology Institute of Microbiology Chinese Academy of Sciences Beijing China 4 Nankai University Tiangin China Keywords crystal structure fusion core Hendra virus heptad repeat Nipah virus Correspondence Z. Rao Laboratory of StructuralBiology Life Sciences Building Tsinghua University Beijing 100084 China Fax 86 10 62773145 Tel 86 10 62771493 E-mail raozh@ These authors contributed equally to this work Received 28 June 2006 revised 7 August 2006 accepted 10 August 2006 doi The Nipah and Hendra viruses are highly pathogenic paramyxoviruses that recently emerged from flying foxes to cause serious disease outbreaks in humans and livestock in Australia Malaysia Singapore and Bangladesh. Their unique genetic constitution high virulence and wide host range set them apart from other paramyxoviruses. These characteristics have led to their classification into the new genus Henpavirus within the family Para-myxoviridae and to their designation as Biosafety Level 4 pathogens. The fusion protein an enveloped glycoprotein essential for viral entry belongs to the family of class I fusion proteins and is characterized by the presence of two heptad repeat HR regions HR1 and HR2. These two regions associate to form a fusion-active hairpin conformation that juxtaposes the viral and cellular membranes to facilitate membrane fusion and enable subsequent viral entry. The Hendra and Nipah virus fusion core proteins were crystallized and their structures determined to A resolution. The Nipah and Hendra fusion core structures are .

• Báo cáo khoa học
• scientific reports
• Report medicine
• traditional medicine
• medical knowledge
• cytoplasm
• analysis of cytoplasmic
• BMC Plant Biology
• Upland cotton
• Restorer gene
• High throughput sequencing
• Cytoplasmic male sterility
• Plant Biology
• Multi omics analysis
• Brassica napus
• Naturally exists
• Mitochondrial genome functions
• BMC Genomics
• RNA sequencing
• Restorer of fertility
• Sterile phenotype
• Parental genes
• Binding miRNAs
• Triple hybrids
• Gossypium bickii
• Proteomic analysis
• medical research
• biochemistry
• molecular Biology
• microRNA genes
• hemoglobin
• medical analysis
• environmental medicine
• human disease
• Crystal structure
• biochemical studies
• Gossypium hirsutum L
• Photosensitive genetic male sterile
• Differentially expressed genes
• Transcriptome analysis
• RNA Seq
• mammals
• tài liệu báo cáo nghiên cứu khoa học
• cách trình bày báo cáo
• kiến thức bệnh thú y
• báo cáo bệnh thú y
• các nghiên về bệnh thú ý
• scientific research
• Human telomeric
• Structural features
• hormone medicine
• under construction
• molecular
• biosynthesis
• genetics
• PPR protein
• Targeted mutagenesis
• Nuclear restorer gene
• Structure function relationship
• Rubber tree
• Hevea brasiliensis
• Genome sequencing
• Anther transcriptome
• Hybrid wheat
• Pistil like
• Skeletal muscle
• Wnt signaling pathway
• Enzyme activity
• Cytoplasmic surface
• Fertility restorer
• Plant breeders
• Nuclear genes