Application): The major goal of this work is to determine the molecular mechanism employed by six proteins that are unique to the enveloped form of vaccinia to produce enveloped virions. The hypothesis that interactions among these six proteins are required for efficient envelopment of vaccinia virus will be tested. These interactions will be delineated by identifying specific domains on these six proteins that are required for the envelopment and to test these identified domains for interaction with the six proteins. Identification of these regions and subsequently what they interact with will not only allow for a better understanding of the function of these six proteins and how they coordinate viral envelopment but will also lay the foundation for further studies into the mechanism of viral envelopment. Specific domains will be identified using an in vivo trans-complementation assay in which the specific protein or domains of the protein being tested will be provided in-trans and complementation will be assessed visually using live fluorescent microscopy. ? ?
Ward, Brian M (2009) Using fluorescent proteins to study poxvirus morphogenesis. Methods Mol Biol 515:1-11 |
Earley, Amalia K; Chan, Winnie M; Ward, Brian M (2008) The vaccinia virus B5 protein requires A34 for efficient intracellular trafficking from the endoplasmic reticulum to the site of wrapping and incorporation into progeny virions. J Virol 82:2161-9 |
Ward, Brian M (2005) Visualization and characterization of the intracellular movement of vaccinia virus intracellular mature virions. J Virol 79:4755-63 |
Ward, Brian M (2005) The longest micron; transporting poxviruses out of the cell. Cell Microbiol 7:1531-8 |