Open AccessFrom structure of the complex to understanding of the biology
Author(s) -
Rossmann Michael G.,
Arisaka Fumio,
Battisti Anthony J.,
Bowman Valorie D.,
Chipman Paul R.,
Fokine Andrei,
Hafenstein Susan,
Kanamaru Shuji,
Kostyuchenko Victor A.,
Mesyanzhinov Vadim V.,
Shneider Mikhail M.,
Morais Marc C.,
Leiman Petr G.,
Palermo Laura M.,
Parrish Colin R.,
Xiao Chuan
Publication year - 2007
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444906047330
Subject(s) - icosahedral symmetry , parvovirus , cryo electron microscopy , biology , vertex (graph theory) , bacteriophage , canine parvovirus , biophysics , parvoviridae , genome , dna , binding site , capsid , crystallography , physics , virus , virology , chemistry , genetics , mathematics , graph , discrete mathematics , escherichia coli , gene
The most extensive structural information on viruses relates to apparently icosahedral virions and is based on X‐ray crystallography and on cryo‐electron microscopy (cryo‐EM) single‐particle reconstructions. Both techniques lean heavily on imposing icosahedral symmetry, thereby obscuring any deviation from the assumed symmetry. However, tailed bacteriophages have icosahedral or prolate icosahedral heads that have one obvious unique vertex where the genome can enter for DNA packaging and exit when infecting a host cell. The presence of the tail allows cryo‐EM reconstructions in which the special vertex is used to orient the head in a unique manner. Some very large dsDNA icosahedral viruses also develop special vertices thought to be required for infecting host cells. Similarly, preliminary cryo‐EM data for the small ssDNA canine parvovirus complexed with receptor suggests that these viruses, previously considered to be accurately icosahedral, might have some asymmetric properties that generate one preferred receptor‐binding site on the viral surface. Comparisons are made between rhinoviruses that bind receptor molecules uniformly to all 60 equivalent binding sites, canine parvovirus, which appears to have a preferred receptor‐binding site, and bacteriophage T4, which gains major biological advantages on account of its unique vertex and tail organelle.