TY - JOUR
T1 - Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3
AU - Liemann, Susanne
AU - Chandran, Kartik
AU - Baker, Timothy S.
AU - Nibert, Max L.
AU - Harrison, Stephen C.
N1 - Funding Information:
We thank Sophia Rits-Volloch for expression of the SeMet-labeled protein; David King at HHMI, Berkeley, and John Rush at the Biopolymers Facility, Harvard Medical School, for mass spectrometry; L. Berman, M. Becker, and H. Lewis at beamline X25 at NSLS BNL and W. Schildkamp, R. Pahl, and the staff of beamline 14-C at BioCARS (APS) for assistance with data collection; and members of the Harrison and Wiley research groups, especially Andrea Carfı́ and Jens Hennecke, for discussions. This work has been supported by grants from the NIH (CA-13202 to S.C.H., AI-46440 to M.L.N., and GM-33050 to T.S.B.). S.L. was supported by a postdoctoral BASF research fellowship of the Studienstiftung des deutschen Volkes and is now an HHMI associate. K.C. was supported by a pre-doctoral fellowship from the Howard Hughes Medical Institute. S.C.H. is an investigator in the Howard Hughes Medical Institute.
PY - 2002/1/25
Y1 - 2002/1/25
N2 - Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, μ1. The structure of μ1, complexed with its "protector" protein, σ3, and the fit of this μ13σ33 heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides μ1 into myristoylated μ1N and μ1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of μ1N, linked to a major conformational change of the entire μ1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of μ1N, and long-range molecular rearrangement of μ1C, thus appears to be part of the penetration mechanism.
AB - Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, μ1. The structure of μ1, complexed with its "protector" protein, σ3, and the fit of this μ13σ33 heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides μ1 into myristoylated μ1N and μ1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of μ1N, linked to a major conformational change of the entire μ1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of μ1N, and long-range molecular rearrangement of μ1C, thus appears to be part of the penetration mechanism.
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U2 - 10.1016/S0092-8674(02)00612-8
DO - 10.1016/S0092-8674(02)00612-8
M3 - Article
C2 - 11832217
AN - SCOPUS:0037169362
SN - 0092-8674
VL - 108
SP - 283
EP - 295
JO - Cell
JF - Cell
IS - 2
ER -