Protein-protein interactions in an alphavirus membrane.
Using homobifunctional chemical cross-linkers with various span distances, we have determined the near-neighbor associations and planar organization of the E1 and E2 envelope glycoproteins which compose the icosahedral surface of Sindbis virus. We have found that E1-E2 heterodimers, which form the virus protomeric units, exist in two conformationally distinct forms, reflecting their nonequivalent positions in the icosahedron. Three of these heterodimers form the trimeric morphologic units (capsomeres) which are held together by central E1-E1 interactions. In addition, we present data which suggest that E2-E2 interactions organize the capsomeres into pentameric and hexameric geometric units and that E1-E1 interactions between capsomeres maintain the icosahedral lattice in mature virions.
Anthony
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Cell Research Institute, University of Texas, Austin 78713-7640.
Brown
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D000524:Alphavirus / Q000378:metabolism; D000818:Animals; D002460:Cell Line; D003432:Cross-Linking Reagents / Q000494:pharmacology; D003902:Detergents; D004229:Dithiothreitol / Q000494:pharmacology; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008961:Models, Structural; D008970:Molecular Weight; D017830:Octoxynol; D011092:Polyethylene Glycols; D012845:Sindbis Virus / Q000378:metabolism* / Q000648:ultrastructure; D014759:Viral Envelope Proteins / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure
D003432:Cross-Linking Reagents; D003902:Detergents; D046911:Macromolecular Substances; D014759:Viral Envelope Proteins; D011092:Polyethylene Glycols; D017830:Octoxynol; D004229:Dithiothreitol