Journal
JOURNAL OF VIROLOGY
Volume 83, Issue 21, Pages 11372-11377Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01228-09
Keywords
-
Categories
Funding
- NIH [AI-053174]
- Ellison Medical Foundation New Scholars in Global Infectious Diseases Award
- VA Merit Awar [R01 AI021362-24, P30DK56339]
- Investigator in the Howard Hughes Medical Institute
Ask authors/readers for more resources
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*.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available