Brian WardSummaryAffiliation: University of Rochester Country: USA Publications
Research Grants
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Detail Information
Publications
The taking of the cytoskeleton one two three: how viruses utilize the cytoskeleton during egressBrian M Ward
Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, NY 14642, USA
Virology 411:244-50. 2011..This review will look at recent findings that relate to the transport of virions to the cell periphery and out of the cell...- The longest micron; transporting poxviruses out of the cellBrian M Ward
Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, New York 14642, USA
Cell Microbiol 7:1531-8. 2005..This review looks at recent reports of poxvirus intracellular transport for virion egress and their interaction with the microtubule network... - Visualization and characterization of the intracellular movement of vaccinia virus intracellular mature virionsBrian M Ward
Department of Microbiology and Immunology, Rochester, NY 14642, USA
J Virol 79:4755-63. 2005.... - The vaccinia virus B5 protein requires A34 for efficient intracellular trafficking from the endoplasmic reticulum to the site of wrapping and incorporation into progeny virionsAmalia K Earley
Department of Microbiology and Immunology, University of Rochester Medical Center, 601 Elmwood Ave, Box 672, Rochester, NY 14642, USA
J Virol 82:2161-9. 2008..Coimmunoprecipitation studies confirmed that B5 and A34 interact through their luminal domains, and further analysis revealed that in the absence of A34, B5 is not efficiently incorporated into virions released from the cell... - The inability of vaccinia virus A33R protein to form intermolecular disulfide-bonded homodimers does not affect the production of infectious extracellular virusWinnie M Chan
Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, NY 14642, USA
Virology 408:109-18. 2010..The recombinant viruses had growth characteristics similar to their parental viruses, indicating that intermolecular disulfide-bonded homodimerization of A33 is not required for its function... - There is an A33-dependent mechanism for the incorporation of B5-GFP into vaccinia virus extracellular enveloped virionsWinnie M Chan
Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, New York 14642, USA
Virology 402:83-93. 2010..These results suggest that in the absence of A33, the cytoplasmic tail of B5 contributes to its incorporation into the envelope of progeny virions... - Using fluorescent proteins to study poxvirus morphogenesisBrian M Ward
Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA
Methods Mol Biol 515:1-11. 2009..The methods presented here describe how to infect and transfect cells for trans-complementation for the purpose of functional domain mapping. The imaging and analysis of these cells is described... - Vaccinia virus protein F12 associates with intracellular enveloped virions through an interaction with A36Sara C Johnston
Department of Microbiology and Immunology, University of Rochester Medical Center, New York 14642, USA
J Virol 83:1708-17. 2009..These results suggest that F12 associates with IEV through an interaction with A36 and that this interaction is critical for the function of F12 during viral egress... - Vaccinia virus entry into cells is dependent on a virion surface protein encoded by the A28L geneTatiana G Senkevich
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
J Virol 78:2357-66. 2004..Furthermore, since A28 is conserved, all poxviruses are likely to penetrate cells in a similar way... - Mutations in the vaccinia virus A33R and B5R envelope proteins that enhance release of extracellular virions and eliminate formation of actin-containing microvilli without preventing tyrosine phosphorylation of the A36R proteinEhud Katz
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0445, USA
J Virol 77:12266-75. 2003..Enhanced virus release, therefore, did not compensate for the loss of actin tails and specialized microvilli... - Vaccinia virus A28L gene encodes an essential protein component of the virion membrane with intramolecular disulfide bonds formed by the viral cytoplasmic redox pathwayTatiana G Senkevich
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0445, USA
J Virol 78:2348-56. 2004..In another paper (T. Senkevich, B. M. Ward, and B. Moss, J. Virol. 78:2357-2366, 2004), we have demonstrated that virions assembled without A28 cannot carry out a second round of infection because they are defective in cell penetration... - Vaccinia virus A36R membrane protein provides a direct link between intracellular enveloped virions and the microtubule motor kinesinBrian M Ward
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0445, USA
J Virol 78:2486-93. 2004..Collectively, these results demonstrated that the viral A36R protein interacts directly with the microtubule motor protein kinesin and that the viral protein A33R may regulate this interaction... - Pox, dyes, and videotape: making movies of GFP-labeled vaccinia virusBrian M Ward
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA
Methods Mol Biol 269:205-18. 2004..Details are also provided for analyzing the images obtained and converting them into QuickTime movies suitable for presentation... - Mapping and functional analysis of interaction sites within the cytoplasmic domains of the vaccinia virus A33R and A36R envelope proteinsBrian M Ward
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0445, USA
J Virol 77:4113-26. 2003..The A33R interaction site of the A36R protein is highly conserved among orthopoxviruses and may overlap binding sites for cellular proteins needed for microtubular movement and actin tail formation...
Research Grants
- Protein Interactions Involved in Poxvirus EnvelopmentBrian Ward; Fiscal Year: 2005....
- Protein Interactions Involved in Orthopoxvirus EnvelopmentBrian Ward; Fiscal Year: 2007..We will investigate how this important protein is incorporated into and coordinates the formation of newly made viruses. A better understanding of this process will provide new targets for antivirals directed against poxviruses. ..
- Protein Interactions Involved in Orthopoxvirus EnvelopmentBrian M Ward; Fiscal Year: 2010..We will investigate how this important protein is incorporated into and coordinates the formation of newly made viruses. A better understanding of this process will provide new targets for antivirals directed against poxviruses. ..