Abstract:
:The coat protein (CP) of alfalfa mosaic virus (AMV) strain 425 assembles to bacilliform or rod-shaped particles in the presence of nucleic acids or to T = 1 empty icosahedral particles in the absence of nucleic acids. To study the determinants of CP assembly, recombinant CPs (rCPs) that contained a (His)(6) region were expressed in Escherichia coli. Wt rCP and a mutant rCP, which lacked the last nine amino acids of the C terminus (amino acids 213-221), assembled to particles that were identical in electron micrographs. However, a mutant rCP, which lacked the last 18 amino acids of the C terminus (amino acids 204-221), did not assemble. Likewise, a mutant with alanine substitutions at W(191), F(197), and P(198) did not assemble. Furthermore rCP with a single alanine substitution at W(191) did not assemble, whereas the rCP, which had an arginine and an alanine substitution at A(196) and F(197), respectively, formed rod-shaped particles. The mutations that prevented assembly prevented dimer formation, which indicates that dimers are the minimal building blocks of particles. Our results indicate that two separate regions in the C terminus of AMV CP are critical for dimer formation and assembly and that changes in key amino acids in one of the regions affect both assembly and particle morphology.
journal_name
Virologyjournal_title
Virologyauthors
Choi J,Loesch-Fries LSdoi
10.1006/viro.1999.9805subject
Has Abstractpub_date
1999-07-20 00:00:00pages
182-9issue
1eissn
0042-6822issn
1096-0341pii
S0042-6822(99)99805-7journal_volume
260pub_type
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