High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains

Umesh Katpally; Neil R. Voss; Tommaso Cavazza; Stefan Taube; John R. Rubin; Vivienne L. Young; Jeanne Stuckey; Vernon K. Ward; Herbert W. Virgin IV; Christiane E. Wobus; Thomas J. Smith

doi:10.1128/JVI.00314-10

High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains

Umesh Katpally, Neil R. Voss, Tommaso Cavazza, Stefan Taube, John R. Rubin, Vivienne L. Young, Jeanne Stuckey, Vernon K. Ward, Herbert W. Virgin IV, Christiane E. Wobus, Thomas J. Smith

Institute of Virology and Cell Biology

37 Citations (Scopus)

Abstract

Our previous structural studies on intact, infectious murine norovirus 1 (MNV-1) virions demonstrated that the receptor binding protruding (P) domains are lifted off the inner shell of the virus. Here, the threedimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to ∼8-Å resolution. rRHDV also has a raised P domain, and therefore, this conformation is independent of infectivity and genus. The atomic structure of the MNV-1 P domain was used to interpret the MNV-1 reconstruction. Connections between the P and shell domains and between the floating P domains were modeled. This observed P-domain flexibility likely facilitates virus-host receptor interactions.

Original language	English
Journal	Journal of Virology
Volume	84
Issue number	11
Pages (from-to)	5836-5841
Number of pages	6
ISSN	0022-538X
DOIs	https://doi.org/10.1128/JVI.00314-10
Publication status	Published - 01.06.2010

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1128/JVI.00314-10

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Katpally, U., Voss, N. R., Cavazza, T., Taube, S., Rubin, J. R., Young, V. L., Stuckey, J., Ward, V. K., Virgin IV, H. W., Wobus, C. E., & Smith, T. J. (2010). High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains. Journal of Virology, 84(11), 5836-5841. https://doi.org/10.1128/JVI.00314-10

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title = "High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains",

abstract = "Our previous structural studies on intact, infectious murine norovirus 1 (MNV-1) virions demonstrated that the receptor binding protruding (P) domains are lifted off the inner shell of the virus. Here, the threedimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to ∼8-{\AA} resolution. rRHDV also has a raised P domain, and therefore, this conformation is independent of infectivity and genus. The atomic structure of the MNV-1 P domain was used to interpret the MNV-1 reconstruction. Connections between the P and shell domains and between the floating P domains were modeled. This observed P-domain flexibility likely facilitates virus-host receptor interactions.",

author = "Umesh Katpally and Voss, {Neil R.} and Tommaso Cavazza and Stefan Taube and Rubin, {John R.} and Young, {Vivienne L.} and Jeanne Stuckey and Ward, {Vernon K.} and {Virgin IV}, {Herbert W.} and Wobus, {Christiane E.} and Smith, {Thomas J.}",

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doi = "10.1128/JVI.00314-10",

language = "English",

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Katpally, U, Voss, NR, Cavazza, T, Taube, S, Rubin, JR, Young, VL, Stuckey, J, Ward, VK, Virgin IV, HW, Wobus, CE & Smith, TJ 2010, 'High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains', Journal of Virology, vol. 84, no. 11, pp. 5836-5841. https://doi.org/10.1128/JVI.00314-10

High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains. / Katpally, Umesh; Voss, Neil R.; Cavazza, Tommaso et al.
In: Journal of Virology, Vol. 84, No. 11, 01.06.2010, p. 5836-5841.

Research output: Journal Articles › Journal articles › Research › peer-review

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T1 - High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains

AU - Katpally, Umesh

AU - Voss, Neil R.

AU - Cavazza, Tommaso

AU - Taube, Stefan

AU - Rubin, John R.

AU - Young, Vivienne L.

AU - Stuckey, Jeanne

AU - Ward, Vernon K.

AU - Virgin IV, Herbert W.

AU - Wobus, Christiane E.

AU - Smith, Thomas J.

PY - 2010/6/1

Y1 - 2010/6/1

N2 - Our previous structural studies on intact, infectious murine norovirus 1 (MNV-1) virions demonstrated that the receptor binding protruding (P) domains are lifted off the inner shell of the virus. Here, the threedimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to ∼8-Å resolution. rRHDV also has a raised P domain, and therefore, this conformation is independent of infectivity and genus. The atomic structure of the MNV-1 P domain was used to interpret the MNV-1 reconstruction. Connections between the P and shell domains and between the floating P domains were modeled. This observed P-domain flexibility likely facilitates virus-host receptor interactions.

AB - Our previous structural studies on intact, infectious murine norovirus 1 (MNV-1) virions demonstrated that the receptor binding protruding (P) domains are lifted off the inner shell of the virus. Here, the threedimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to ∼8-Å resolution. rRHDV also has a raised P domain, and therefore, this conformation is independent of infectivity and genus. The atomic structure of the MNV-1 P domain was used to interpret the MNV-1 reconstruction. Connections between the P and shell domains and between the floating P domains were modeled. This observed P-domain flexibility likely facilitates virus-host receptor interactions.

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SN - 0022-538X

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JF - Journal of Virology

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High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains

Abstract

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