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A Unique Human Norovirus Lineage with a Distinct HBGA Binding Interface
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نویسنده
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liu w. ,chen y. ,jiang x. ,xia m. ,yang y. ,tan m. ,li x. ,rao z.
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منبع
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plos pathogens - 2015 - دوره : 11 - شماره : 7
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چکیده
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Norovirus (nov) causes epidemic acute gastroenteritis in humans,whereby histo-blood group antigens (hbgas) play an important role in host susceptibility. each of the two major genogroups (gi and gii) of human novs recognizes a unique set of hbgas through a distinct binding interface that is conserved within a genogroup,indicating a distinct evolutionary path for each genogroup. here,we characterize a lewis a (lea) antigen binding strain (oif virus) in the gii.21 genotype that does not share the conserved gii binding interface,revealing a new evolution lineage with a distinct hbga binding interface. sequence alignment showed that the major residues contributing to the new hbga binding interface are conserved among most members of the gii.21,as well as a closely related gii.13 genotype. in addition,we found that glycerol inhibits oif binding to hbgas,potentially allowing production of cheap antivirals against human novs. taken together,our results reveal a new evolutionary lineage of novs selected by hbgas,a finding that is important for understanding the diversity and widespread nature of novs. © 2015 liu et al.
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آدرس
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school of life sciences,university of science and technology of china,hefei,anhui, China, national laboratory of biomacromolecules,institute of biophysics,chinese academy of sciences,beijing, China, division of infectious diseases,cincinnati children’s hospital medical center,cincinnati,oh,united states,university of cincinnati college of medicine,cincinnati,oh, United States, division of infectious diseases,cincinnati children’s hospital medical center,cincinnati,oh, United States, national laboratory of biomacromolecules,institute of biophysics,chinese academy of sciences,beijing, China, division of infectious diseases,cincinnati children’s hospital medical center,cincinnati,oh,united states,university of cincinnati college of medicine,cincinnati,oh, United States, national laboratory of biomacromolecules,institute of biophysics,chinese academy of sciences,beijing, China, national laboratory of biomacromolecules,institute of biophysics,chinese academy of sciences,beijing, China
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Authors
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