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Pubmed ID: 14528291
Publication Date: 2003/10/05

Visualization of membrane protein domains by cryo-electron microscopy of dengue virus.


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 A 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.
Authors: Zhang Wei , Chipman Paul R , Corver Jeroen , Johnson Peter R , Zhang Ying , Mukhopadhyay Suchetana , Baker Timothy S , Strauss James H , Rossmann Michael G , Kuhn Richard J ,

Reference:

  1. ncbi.nlm.nih.gov. [Last access 2003/10/05].

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