Structural evolution of the P22-like phages: Comparison of Sf6 and P22 procapsid and virion architectures

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• 作者：Kristin N. Parent^a ; Eddie B. Gilcrease^b ; Sherwood R. Casjens^b ; ^{sherwood.casjens@path.utah.edu} ; Timothy S. Baker^a ; ^c ; ^tsb@ucsd.edu
• 关键词：a.a. ; amino acid ; cryoEM ; cryo electron microscopy ; CP ; coat protein ; 3D ; three-dimensional ; gp ; gene product ; omp ; outer membrane protein
• 刊名：Virology
• 出版年：2012
• 期刊代码：108_00426822
• 类别：imm
• 出版时间：5 June, 2012
• 卷：427
• 期：2
• 页码：177-188
• 文件大小：2277 K

摘要

Coat proteins of tailed, dsDNA phages and in herpesviruses include a conserved core similar to the bacteriophage HK97 subunit. This core is often embellished with other domains such as the telokin Ig-like domain of phage P22. Eighty-six P22-like phages and prophages with sequenced genomes share a similar set of virion assembly genes and, based on comparisons of twelve viral assembly proteins (structural and assembly/packaging chaperones), these phages are classified into three groups (P22-like, Sf6-like, and CUS-3-like). We used cryo-electron microscopy and 3D image reconstruction to determine the structures of Sf6 procapsids and virions (~ 7 脜 resolution), and the structure of the entire, asymmetric Sf6 virion (16-脜 resolution). The Sf6 coat protein is similar to that of P22 yet it has differences in the telokin domain and in its overall quaternary organization. Thermal stability and agarose gel experiments show that Sf6 virions are slightly less stable than those of P22. Finally, bacterial host outer membrane proteins A and C were identified in lipid vesicles that co-purify with Sf6 particles, but are not components of the capsid.