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Title: Structural basis for human respiratory syncytial virus NS1-mediated modulation of host responses


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Chatterjee, Srirupa, Luthra, Priya, Esaulova, Ekaterina, Agapov, Eugene, Yen, Benjamin C., Borek, Dominika M., Edwards, Megan R., Mittal, Anuradha, Jordan, David S., Ramanan, Parameshwar, Moore, Martin L., Pappu, Rohit V., Holtzman, Michael J., Artyomov, Maxim N., Basler, Christopher F., Amarasinghe, Gaya K., and Leung, Daisy W.. Structural basis for human respiratory syncytial virus NS1-mediated modulation of host responses. United States: N. p., 2017. Web. doi:10.1038/nmicrobiol.2017.101.
Chatterjee, Srirupa, Luthra, Priya, Esaulova, Ekaterina, Agapov, Eugene, Yen, Benjamin C., Borek, Dominika M., Edwards, Megan R., Mittal, Anuradha, Jordan, David S., Ramanan, Parameshwar, Moore, Martin L., Pappu, Rohit V., Holtzman, Michael J., Artyomov, Maxim N., Basler, Christopher F., Amarasinghe, Gaya K., & Leung, Daisy W.. Structural basis for human respiratory syncytial virus NS1-mediated modulation of host responses. United States. doi:10.1038/nmicrobiol.2017.101.
Chatterjee, Srirupa, Luthra, Priya, Esaulova, Ekaterina, Agapov, Eugene, Yen, Benjamin C., Borek, Dominika M., Edwards, Megan R., Mittal, Anuradha, Jordan, David S., Ramanan, Parameshwar, Moore, Martin L., Pappu, Rohit V., Holtzman, Michael J., Artyomov, Maxim N., Basler, Christopher F., Amarasinghe, Gaya K., and Leung, Daisy W.. 2017. "Structural basis for human respiratory syncytial virus NS1-mediated modulation of host responses". United States. doi:10.1038/nmicrobiol.2017.101.
@article{osti_1374614,
title = {Structural basis for human respiratory syncytial virus NS1-mediated modulation of host responses},
author = {Chatterjee, Srirupa and Luthra, Priya and Esaulova, Ekaterina and Agapov, Eugene and Yen, Benjamin C. and Borek, Dominika M. and Edwards, Megan R. and Mittal, Anuradha and Jordan, David S. and Ramanan, Parameshwar and Moore, Martin L. and Pappu, Rohit V. and Holtzman, Michael J. and Artyomov, Maxim N. and Basler, Christopher F. and Amarasinghe, Gaya K. and Leung, Daisy W.},
abstractNote = {},
doi = {10.1038/nmicrobiol.2017.101},
journal = {Nature Microbiology},
number = 06, 2017,
volume = 2,
place = {United States},
year = 2017,
month = 6
}
  • Motavizumab is {approx}tenfold more potent than its predecessor, palivizumab (Synagis), the FDA-approved monoclonal antibody used to prevent respiratory syncytial virus (RSV) infection. The structure of motavizumab in complex with a 24-residue peptide corresponding to its epitope on the RSV fusion (F) glycoprotein reveals the structural basis for this greater potency. Modeling suggests that motavizumab recognizes a different quaternary configuration of the F glycoprotein than that observed in a homologous structure.
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