Tobacco mosaic virus assembly and disassembly: determinants in pathogenicity and resistance.
The structural proteins of plant viruses have evolved to self-associate into complex macromolecules that are centrally involved in virus biology. In this review, the structural and biophysical properties of the Tobacco mosaic virus (TMV) coat protein (CP) are addressed in relation to its role in host resistance and disease development. TMV CP affects the display of several specific virus and host responses, including cross-protection, systemic virus movement, hypersensitive disease resistance, and symptom development. Studies indicate that the three-dimensional structure of CP is critical to the control of these responses, either directly through specific structural motifs or indirectly via alterations in CP assembly. Thus, both the structure and assembly of the TMV CP function as determinants in the induction of disease and resistance responses.
Culver
James N
JN
Center for Agricultural Biotechnology, University of Maryland Biotechnology Institute, College Park 20742, USA. jc216@umail.umd.edu
D001692:Biological Transport / Q000502:physiology; D002213:Capsid / Q000737:chemistry / Q000378:metabolism; D036022:Capsid Proteins; D007113:Immunity, Innate / Q000235:genetics / Q000502:physiology; D010935:Plant Diseases / Q000235:genetics / Q000821:virology*; D010942:Plant Viruses / Q000235:genetics / Q000472:pathogenicity; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014026:Nicotiana / Q000235:genetics / Q000821:virology*; D014027:Tobacco Mosaic Virus / Q000472:pathogenicity* / Q000502:physiology; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019065:Virus Assembly / Q000502:physiology*
D036022:Capsid Proteins; D014764:Viral Proteins; C083292:coat protein, Tobacco necrosis virus (Nebraska)