Toroidal surface complexes of bacteriophage 12 are responsible for host-cell attachment

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• 作者：Alejandra Leo-Macias^a ; Garrett Katz^b ; Hui Wei^c ; Alexandra Alimova^c ; A. Katz^d ; William J. Rice^e ; Ruben Diaz-Avalos^e ; Guo-Bin Hu^a ; ¹ ; David L. Stokes^a ; ^e ; Paul Gottlieb^c ; ^f ; ^{pgottl@med.cuny.edu"" rel=""nofollow}
• 关键词：Cystovirus ; Cryo-electron tomography ; ; //www.sciencedirect.com/scidirimg/entities/3d5.gif"" alt=""phi"" title=""phi"" border=""0"">12 six-fold symmetry ; Subtomogram averaging ; ; //www.sciencedirect.com/scidirimg/entities/3d5.gif"" alt=""
• 刊名：Virology
• 出版年：2011
• 出版时间：5 June 2011
• 年：2011
• 卷：414
• 期：2
• 页码：103-109
• 全文大小：1389 K

文摘

Cryo-electron tomography and subtomogram averaging are utilized to determine that the bacteriophage 12, a member of the Cystoviridae family, contains surface complexes that are toroidal in shape, are composed of six globular domains with six-fold symmetry, and have a discrete density connecting them to the virus membrane-envelope surface. The lack of this kind of spike in a reassortant of 12 demonstrates that the gene for the hexameric spike is located in 12's medium length genome segment, likely to the P3 open reading frames which are the proteins involved in viral-host cell attachment. Based on this and on protein mass estimates derived from the obtained averaged structure, it is suggested that each of the globular domains is most likely composed of a total of four copies of P3a and/or P3c proteins. Our findings may have implications in the study of the evolution of the cystovirus species in regard to their host specificity.