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dc.contributor.authorSirohi, Devika
dc.contributor.authorChen, Zhenguo
dc.contributor.authorSun, Lei
dc.contributor.authoret al.
dc.date.accessioned2022-09-05T16:43:17Z
dc.date.available2022-09-05T16:43:17Z
dc.date.issued2016-06
dc.identifier.urihttps://www.science.org/doi/full/10.1126/science.aaf5316en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12663/2949
dc.description.abstractThe recent rapid spread of Zika virus and its unexpected linkage to birth defects and an autoimmune neurological syndrome have generated worldwide concern. Zika virus is a flavivirus like the dengue, yellow fever, and West Nile viruses. We present the 3.8 angstrom resolution structure of mature Zika virus, determined by cryo–electron microscopy (cryo-EM). The structure of Zika virus is similar to other known flavivirus structures, except for the ~10 amino acids that surround the Asn154 glycosylation site in each of the 180 envelope glycoproteins that make up the icosahedral shell. The carbohydrate moiety associated with this residue, which is recognizable in the cryo-EM electron density, may function as an attachment site of the virus to host cells. This region varies not only among Zika virus strains but also in other flaviviruses, which suggests that differences in this region may influence virus transmission and disease.en_US
dc.languageEnglishen_US
dc.subjectZika Research Projecten_US
dc.subjectZika Virusen_US
dc.subjectZika Virus Infectionen_US
dc.subjectFlavivirusen_US
dc.titleThe 3.8 Å resolution cryo-EM structure of Zika virusen_US
eihealth.countryOthersen_US
eihealth.categoryEpidemiology and epidemiological studiesen_US
eihealth.typeResearch protocol informationen_US
eihealth.maincategorySave Lives / Salvar Vidasen_US
dc.relation.ispartofjournalScienceen_US
dc.contributor.corporatenamePurdue Universityen_US
dc.contributor.corporatenameUnited States of America. National Institutes of Health Clinical Centeren_US


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