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Atomic Model of Rabbit Hemorrhagic Disease Virus by Cryo-Electron Microscopy and Crystallography
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نویسنده
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wang x. ,xu f. ,liu j. ,gao b. ,liu y. ,zhai y. ,ma j. ,zhang k. ,baker t.s. ,schulten k. ,zheng d. ,pang h. ,sun f.
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منبع
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plos pathogens - 2013 - دوره : 9 - شماره : 1
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چکیده
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Rabbit hemorrhagic disease,first described in china in 1984,causes hemorrhagic necrosis of the liver. its etiological agent,rabbit hemorrhagic disease virus (rhdv),belongs to the lagovirus genus in the family caliciviridae. the detailed molecular structure of any lagovirus capsid has yet to be determined. here,we report a cryo-electron microscopic (cryoem) reconstruction of wild-type rhdv at 6.5 å resolution and the crystal structures of the shell (s) and protruding (p) domains of its major capsid protein,vp60,each at 2.0 å resolution. from these data we built a complete atomic model of the rhdv capsid. vp60 has a conserved s domain and a specific p2 sub-domain that differs from those found in other caliciviruses. as seen in the shell portion of the rhdv cryoem map,which was resolved to ~5.5 å,the n-terminal arm domain of vp60 folds back onto its cognate s domain. sequence alignments of vp60 from six groups of rhdv isolates revealed seven regions of high variation that could be mapped onto the surface of the p2 sub-domain and suggested three putative pockets might be responsible for binding to histo-blood group antigens. a flexible loop in one of these regions was shown to interact with rabbit tissue cells and contains an important epitope for anti-rhdv antibody production. our study provides a reliable,pseudo-atomic model of a lagovirus and suggests a new candidate for an efficient vaccine that can be used to protect rabbits from rhdv infection. © 2013 wang et al.
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آدرس
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national laboratory of biomacromolecules,institute of biophysics (ibp),chinese academy of sciences (cas),beijing,china,university of chinese academy of sciences,beijing, China, department of biochemistry and molecular biology,college of life sciences,beijing normal university,beijing, China, state key laboratory of veterinary biotechnology,harbin veterinary research institute,chinese academy of agricultural science,harbin, China, national laboratory of biomacromolecules,institute of biophysics (ibp),chinese academy of sciences (cas),beijing,china,university of chinese academy of sciences,beijing, China, beckman institute and department of physics,university of illinois at urbana-champaign,urbana,il, United States, national laboratory of biomacromolecules,institute of biophysics (ibp),chinese academy of sciences (cas),beijing, China, national laboratory of biomacromolecules,institute of biophysics (ibp),chinese academy of sciences (cas),beijing,china,university of chinese academy of sciences,beijing, China, national laboratory of biomacromolecules,institute of biophysics (ibp),chinese academy of sciences (cas),beijing,china,university of chinese academy of sciences,beijing, China, department of chemistry and biochemistry and division of biological sciences,university of california-san diego,la jolla,ca, United States, beckman institute and department of physics,university of illinois at urbana-champaign,urbana,il, United States, analytical and testing center,beijing normal university,beijing, China, school of medicine,tsinghua university,beijing, China, national laboratory of biomacromolecules,institute of biophysics (ibp),chinese academy of sciences (cas),beijing, China
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Authors
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