VP5* rearranges when rotavirus uncoats.
Trypsin primes rotavirus for efficient infectivity by cleaving the spike protein, VP4, into VP8* and VP5*. A recombinant VP5* fragment has a trimeric, folded-back structure. Comparison of this structure with virion spikes suggests that a rearrangement, analogous to those of enveloped virus fusion proteins, may mediate membrane penetration by rotavirus during entry. To detect this inferred rearrangement of virion-associated authentic VP5*, we raised conformation-specific monoclonal antibodies against the recombinant VP5* fragment in its putative post-membrane penetration conformation. Using one of these antibodies, we demonstrate that rotavirus uncoating triggers a conformational change in the cleaved VP4 spike to yield rearranged VP5*.
Yoder
Joshua D
JD
Laboratory of Molecular Medicine, Children's Hospital, Boston, Massachusetts 02115, USA.
Trask
Shane D
SD
Vo
T Phuoc
TP
Binka
Mawuena
M
Feng
Ningguo
N
Harrison
Stephen C
SC
Greenberg
Harry B
HB
Dormitzer
Philip R
PR
D000595:Amino Acid Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D012401:Rotavirus / Q000378:metabolism* / Q000648:ultrastructure; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014771:Virion / Q000378:metabolism / Q000648:ultrastructure; D053586:Virus Internalization
D017361:Viral Nonstructural Proteins; C104282:nsp1 protein, Rotavirus
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