TY - JOUR
T1 - Toroidal surface complexes of bacteriophage Φ12 are responsible for host-cell attachment
AU - Leo-Macias, Alejandra
AU - Katz, Garrett
AU - Wei, Hui
AU - Alimova, Alexandra
AU - Katz, A.
AU - Rice, William J.
AU - Diaz-Avalos, Ruben
AU - Hu, Guo Bin
AU - Stokes, David L.
AU - Gottlieb, Paul
N1 - Funding Information:
This work is support in part by the National Institute of General Medical Science —grant #SC1 GM092781-01 and the Research Centers in Minority Institutions (NIH/NCRR/RCMI) CCNY /grant G12-RR03060 . The electron microscopy facilities at the New York Structural Biology Center are supported by grant C000087 from the New York State Foundation for Science, Technology and Innovation (NYSTAR) and NIH grant S10 RR017291 . ALM is a recipient of a postdoctoral fellowship from the Spanish Ministry of Science. We wish to thank Dr. Leonard Mindich of the Public Health Research Institute of UMDNJ, Newark, NJ, for the generous gift of ϕ2954 and ϕ2996.
PY - 2011/6/5
Y1 - 2011/6/5
N2 - Cryo-electron tomography and subtomogram averaging are utilized to determine that the bacteriophage Φ12, 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 Φ12 demonstrates that the gene for the hexameric spike is located in Φ12'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.
AB - Cryo-electron tomography and subtomogram averaging are utilized to determine that the bacteriophage Φ12, 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 Φ12 demonstrates that the gene for the hexameric spike is located in Φ12'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.
KW - Cryo-electron tomography
KW - Cystovirus
KW - Subtomogram averaging
KW - Φ12 six-fold symmetry
KW - Φ12 surface proteins
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U2 - 10.1016/j.virol.2011.03.020
DO - 10.1016/j.virol.2011.03.020
M3 - Article
C2 - 21489589
AN - SCOPUS:79955912515
SN - 0042-6822
VL - 414
SP - 103
EP - 109
JO - Virology
JF - Virology
IS - 2
ER -