Volume 4 Issue 11
Nov.  2013
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Wong H. Hui, Qiyi Tang, Hongrong Liu, Ivo Atanasov, Fenyong Liu, Hua Zhu, Z. Hong Zhou. Protein interactions in the murine cytomegalovirus capsid revealed by cryoEM[J]. Protein&Cell, 2013, 4(11): 833-845. doi: 10.1007/s13238-013-3060-7
Citation: Wong H. Hui, Qiyi Tang, Hongrong Liu, Ivo Atanasov, Fenyong Liu, Hua Zhu, Z. Hong Zhou. Protein interactions in the murine cytomegalovirus capsid revealed by cryoEM[J]. Protein&Cell, 2013, 4(11): 833-845. doi: 10.1007/s13238-013-3060-7

Protein interactions in the murine cytomegalovirus capsid revealed by cryoEM

doi: 10.1007/s13238-013-3060-7
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This research was supported by NIH (AI046420).

  • Received Date: 2013-07-15
  • Rev Recd Date: 2013-08-14
  • Cytomegalovirus (CMV) is distinct among members of the Herpesviridae family for having the largest dsDNA genome (230 kb). Packaging of large dsDNA genome is known to give rise to a highly pressurized viral capsid, but molecular interactions conducive to the formation of CMV capsid resistant to pressurization have not been described. Here, we report a cryo electron microscopy (cryoEM) structure of the murine cytomegalovirus (MCMV) capsid at a 9.1 Å resolution and describe the molecular interactions among the ~3000 protein molecules in the MCMV capsid at the secondary structure level. Secondary structural elements are resolved to provide landmarks for correlating with results from sequence-based prediction and for structure-based homology modeling. The major capsid protein (MCP) upper domain (MCPud) contains α-helices and β-sheets conserved with those in MCPud of herpes simplex virus type 1 (HSV-1), with the largest differences identified as a "saddle loop" region, located at the tip of MCPud and involved in interaction with the smallest capsid protein (SCP). Interactions among the bacteriophage HK97-like floor domain of MCP, the middle domain of MCP, the hook and clamp domains of the triplex proteins (hoop and clamp domains of TRI-1 and clamp domain of TRI-2) contribute to the formation of a mature capsid. These results offer a framework for understanding how cytomegalovirus uses various secondary structural elements of its capsid proteins to build a robust capsid for packaging its large dsDNA genome inside and for attaching unique functional tegument proteins outside.
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