Research Topics
Species | Jared R PatchSummaryAffiliation: Uniformed Services University of the Health Sciences Country: USA Publications
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Detail Information
Publications
Quantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix proteinJared R Patch
Department of Microbiology and Immunology, Uniformed Services University, Bethesda, Maryland 20814, USA
Virol J 4:1. 2007..Here, we have established recombinant expression systems to study NiV particle assembly and budding through the formation of virus-like particles (VLPs)...
Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor bindingKimberly A Bishop
Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD 20814, USA
J Virol 82:11398-409. 2008..Together, these data suggest the stalk domain of G plays an important role in the conformational stability and receptor binding-triggered changes leading to productive fusion, such as the dissociation of G and F...
Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virusKatharine N Bossart
Department of Microbiology and Immunology, F Edward Hebert School of Medicine, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, MD 20814 4799, USA
J Virol 79:6690-702. 2005..This HeV sG glycoprotein will be exceedingly useful for structural studies, receptor identification strategies, and vaccine development goals for these important emerging viral agents...
The YPLGVG sequence of the Nipah virus matrix protein is required for buddingJared R Patch
Department of Microbiology and Immunology, Uniformed Services University, Bethesda, Maryland 20814, USA
Virol J 5:137. 2008..Here, we have used this system to further explore the budding process by analyzing elements within the M protein that are critical for particle release...
