ating the molecular determinants of attachment protein (G)-receptor specificity4,6,9-13
- Identifying the parameters that modulate fusion (F) protein activity14-16
- Dissecting the receptor binding triggered membrane fusion cascade16-20
- Developing quantitative and immunological tools to shed light on the kinetics and stoichiometry of the fusion process12,16,18,21
- Characterizing the prevalence of cross-reactive neutralizing antibodies from wild-life (mostly bats) and humans at high-risk for exposure in various locales (West Africa, South America) that have now reported the presence of henipavirus-related viruses
In the longer term, we are developing highly efficient reverse genetics rescue systems for single-stranded negative-sense RNA viruses (Mononegavirales) that are more robust (easy to optimize) and do not required the use of vaccinia-driven T7 polymerase (a standard method in the field). Protocols will be published on our lab's web-site, as and when they are published in the peer reviewed literature.
- Drexler, J. F. et al. Bats host major mammalian paramyxoviruses. Nature communications 3, 796, doi:10.1038/ncomms1796 (2012).
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- Lloyd-Smith, J. O. et al. Epidemic dynamics at the human-animal interface. Science 326, 1362-1367, doi:10.1126/science.1177345 (2009).
- Negrete, O. A. et al. EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus. Nature 436, 401-405, doi:10.1038/nature03838 (2005).
- Bonaparte, M. I. et al. Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus. Proc Natl Acad Sci U S A 102, 10652-10657, doi:10.1073/pnas.0504887102 (2005).
- Negrete, O. A. et al. Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus. PLoS Pathog 2, e7, doi:10.1371/journal.ppat.0020007 (2006).
- Pasquale, E. B. Eph-ephrin bidirectional signaling in physiology and disease. Cell 133, 38-52, doi:10.1016/j.cell.2008.03.011 (2008).
- Lee, B. & Ataman, Z. A. Modes of paramyxovirus fusion: a Henipavirus perspective. Trends Microbiol, doi:S0966-842X(11)00053-9 [pii]
- Lee, B. Envelope-receptor interactions in Nipah virus pathobiology. Ann N Y Acad Sci 1102, 51-65, doi:1102/1/51 [pii]
- Negrete, O. A., Chu, D., Aguilar, H. C. & Lee, B. Single amino acid changes in the Nipah and Hendra virus attachment glycoproteins distinguish ephrinB2 from ephrinB3 usage. J Virol 81, 10804-10814, doi:JVI.00999-07 [pii]
- Lee, B., Ataman, Z. A. & Jin, L. Evil versus 'eph-ective' use of ephrin-B2. Nat Struct Mol Biol 15, 540-542, doi:nsmb0608-540 [pii]
- Wolf, M. C. et al. A catalytically and genetically optimized beta-lactamase-matrix based assay for sensitive, specific, and higher throughput analysis of native henipavirus entry characteristics. Virol J 6, 119, doi:10.1186/1743-422x-6-119 (2009).
- Pernet, O., Wang, Y. E. & Lee, B. Henipavirus Receptor Usage and Tropism. Current topics in microbiology and immunology, doi:10.1007/82_2012_222 (2012).
- Aguilar, H. C. et al. N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry. J Virol 80, 4878-4889, doi:10.1128/jvi.80.10.4878-4889.2006 (2006).
- Aguilar, H. C. et al. Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling. J Virol 81, 4520-4532, doi:10.1128/jvi.02205-06 (2007).
- Aguilar, H. C., Aspericueta, V., Robinson, L. R., Aanensen, K. E. & Lee, B. A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the nipah virus membrane fusion cascade. J Virol 84, 8033-8041, doi:10.1128/jvi.00469-10 (2010).
- Aguilar, H. C. et al. A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F). J Biol Chem 284, 1628-1635, doi:M807469200 [pii]
- Garner, O. B. et al. Endothelial galectin-1 binds to specific glycans on nipah virus fusion protein