期刊
NATURE STRUCTURAL BIOLOGY
卷 10, 期 11, 页码 907-912出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsb990
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资金
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [P01AI045976, P01AI055672] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM033050] Funding Source: NIH RePORTER
- NIAID NIH HHS [P01 AI055672, P01 AI045976] Funding Source: Medline
- NIGMS NIH HHS [R37 GM033050] Funding Source: Medline
Improved technology for reconstructing cryo-electron microscopy (cryo-EM) images has now made it possible to determine secondary structural features of membrane proteins in enveloped viruses. The structure of mature dengue virus particles was determined to a resolution of 9.5 Angstrom by cryo-EM and image reconstruction techniques, establishing the secondary structural disposition of the 180 envelope ( E) and 180 membrane ( M) proteins in the lipid envelope. The alpha-helical stem regions of the E molecules, as well as part of the N-terminal section of the M proteins, are buried in the outer leaflet of the viral membrane. The anchor regions of E and the M proteins each form antiparallel E-E and M-M transmembrane alpha-helices, leaving their C termini on the exterior of the viral membrane, consistent with the predicted topology of the unprocessed polyprotein. This is one of only a few determinations of the disposition of transmembrane proteins in situ and shows that the nucleocapsid core and envelope proteins do not have a direct interaction in the mature virus.
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