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Capsids assembly

Raman difference spectroscopy has also been used to understand the molecular mechanism of viral core assemblies yielding information on viral subunits from precursor and mature states. Benevides et al. employed Raman difference spectroscopy to investigate conformational changes of the protein building blocks of the icosahedral core of a double-stranded RNA (p6 virus during viral procapsid and capsid assembly [18],... [Pg.442]

White LJ, Hardy ME, Estes MK (1997), Biochemical characterization of a smaller form of recombinant Norwalk virus capsids assembled in insect cells, J. Virol. 71 8066-8072. [Pg.458]

Kegel, W.K., and van der Schoot, P. "Competing hydrophobic and screened Coulomb interactions in hepatitis b virus capsid assembly". Biophys.. 86, 3905-3913 (2004). [Pg.75]

Zlotnick A et al (2000) Mechanism of capsid assembly for an icosahedral plant vims. Virology 277 450-456... [Pg.110]

Human cytomegalovirus (HCMV) disease is the most common life-threatening opportunistic viral infection in the inmunocompromised. HCMV protease, a serine protease, plays a critical role in capsid assembly and viral maturation and is an attractive target for antiviral chemotherapy. Slater et al investigated the interaction of various 1,4-naphthoquinones derivatives with HCMV protease. They identified potent irreversible naphthoquinones inhibitors of HCMV protease which covalently modify... [Pg.750]

Grimes et al., 1998 Reinisch et al, 2000 Wikoff et at, 2000). Likewise, advances in electron cryomicroscopy and image reconstruction techniques allow time-resolved investigations of structural transitions associated with capsid assembly and maturation (Conway et al., 2001 Lawton et al, 1997). These developments have been paralleled by refinements in the molecular approaches used for sample preparation, with the result that synthesis of assembly intermediates and end products has become routine for many viruses. [Pg.2]

Truncated versions of the nucleocapsid protein that lacked various portions of the N terminus revealed that deletion of the first 32 amino acids interfered with assembly, but this deletion did not eliminate interaction of the coat protein with nucleic acid. When present in small amounts, this mutant coat protein could be incorporated into capsids assembled from the wild-type protein. However, when present in large amounts, the mutant coat protein inhibited assembly of the wild-type protein. [Pg.20]

Fig. 8. HK97 assembly and maturation. (A) Negatively stained electron micrograph of a mature dsDNA-filled capsid, with noncontractile tail and accessory proteins. (B) Steps in capsid assembly and maturation (see text in vitro conditions are in boldface, and in vivo conditions or components that differ from the in vitro conditions are in italic) (Conway et al, 1995). (C) Chemistry of the cross-linking reaction. Fig. 8. HK97 assembly and maturation. (A) Negatively stained electron micrograph of a mature dsDNA-filled capsid, with noncontractile tail and accessory proteins. (B) Steps in capsid assembly and maturation (see text in vitro conditions are in boldface, and in vivo conditions or components that differ from the in vitro conditions are in italic) (Conway et al, 1995). (C) Chemistry of the cross-linking reaction.
Zlotnick, A., Reddy, V. S., Dasgupta, R., Schneemann, A., Ray, W. J., Jr., Rueckert, R. R., and Johnson, J. E. (1994). Capsid assembly in a family of animal viruses primes an autoproteolytic maturation that depends on a single aspartic acid residue. J. Biol. Chem. 269, 13680-13684. [Pg.258]


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