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The goal of the Laboratory of Structural Virology (LSV) is to provide insights into viral latency and the biological processes that modulate the effects on human health. To accomplish this, we investigate the following topics:

  • The relationship between the atomic level structures of macromolecules and their biochemical properties
  • The abilities of viral macromolecules to interact with substrates and other molecules, including those that impact on human health.

 

The research performed by our laboratory requires an integrated approach wherein techniques such as X-ray crystallography, protein interaction analysis, including Isothermal Titration Calorimetry are used to understand the components of viral modulation.

Find out about our Research and Opportunities to Work
on Herpesvirus first hand 
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Recent Publications

LANA E3 Ubiquitin-Ligase Activity Impacts Gammaherpesvirus-Driven Germinal Center B Cell
Proliferation. J Virol. 2016 Jun 15. pii: JVI.00813-16. [Epub ahead of print]PubMed PMID: 27307564.

Stochastic Detection of MPSA-Gold Nanoparticles Using a α-Hemolysin Nanopore Equipped with a Noncovalent Molecular Adaptor. Anal
Chem. 2016 Jun 21;88(12):6214-22. doi: 10.1021/acs.analchem.5b03558. Epub 2016 Jun 8. PubMed PMID: 27238076.

KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res. 2015 Sep 30. pii: gkv987. [Epub ahead of print].

The Kaposi's sarcoma herpesvirus latency-associated nuclear antigen DNA binding domain dorsal positive electrostatic patch facilitates DNA replication and episome persistence. J Biol Chem. 2015 Sep 29. pii: jbc.M115.674622.

Sensing Single Mixed-Monolayer Protected Gold Nanoparticles by the α-Hemolysin Nanopore. Analytical Chemistry Just Accepted Publication Date (Web): September 23, 2013 (Article) DOI: 10.1021/ac4014836.

Crystal structure of the gamma-2 herpesvirus LANA DNA binding domain identifies charged surface residues which impact viral latency. PLoS Pathogens 2013, 9(10): e1003673. doi:10.1371/journal.ppat.1003673 (online or pdf).

Role of Src-homology domain binding in signaling complexes assembled by the murid gammaherpesvirus M2 protein. J. Biol. Chem. 2013 vol. 288 (6) p. 3858-3870.

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Kaye LabSimas Lab

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