Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Shane D. Trask"'
Publikováno v:
Viruses, Vol 2, Iss 6, Pp 1340-1346 (2010)
A recently solved structure of the aquareovirus virion (Zhang, X; Jin, L.; Fang, Q; Hui, W.H.; Zhou Z.H. 3.3 Å Cryo-EM Structure of a Nonenveloped Virus Reveals a Priming Mechanism for Cell Entry. Cell 2010, 141, 472-482 [1]) provides new insights i
Externí odkaz:
https://doaj.org/article/3dc32b635bf9430bb97b35b8a4e53e57
Publikováno v:
Methods. 59:199-206
Effective methods to engineer the segmented, double-stranded RNA genomes of Reoviridae viruses have only recently been developed. Mammalian orthoreoviruses (MRV) and bluetongue virus (BTV) can be recovered from entirely recombinant reagents, signific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ee8ecee863ae83de4aee2aef9854f63
https://doi.org/10.1016/j.ymeth.2012.05.012
https://doi.org/10.1016/j.ymeth.2012.05.012
Publikováno v:
Current Opinion in Virology. 2:373-379
Rotaviruses are members of the Reoviridae family of non-enveloped viruses and important etiologic agents of acute gastroenteritis in infants and young children. In recent years, high-resolution structures of triple-layered rotavirus virions and the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e5302c2f8c6d2ebd5999b09bc59afa8
https://doi.org/10.1016/j.coviro.2012.04.005
https://doi.org/10.1016/j.coviro.2012.04.005
Cross-Linking of Rotavirus Outer Capsid Protein VP7 by Antibodies or Disulfides Inhibits Viral Entry
Autor:
Philip R. Dormitzer, Barbara S. Coulson, Harry B. Greenberg, Shane D. Trask, Stephen C. Harrison, Scott T. Aoki
Publikováno v:
Journal of Virology. 85:10509-10517
Antibodies that neutralize rotavirus infection target outer coat proteins VP4 and VP7 and inhibit viral entry. The structure of a VP7-Fab complex (S. T. Aoki, et al., Science 324:1444-1447, 2009) led us to reclassify epitopes into two binding regions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::630106e9b21117cdf8e388cf4040386f
https://doi.org/10.1128/jvi.00234-11
https://doi.org/10.1128/jvi.00234-11
Publikováno v:
Journal of Virology. 84:1764-1770
During rotavirus entry, a virion penetrates a host cell membrane, sheds its outer capsid proteins, and releases a transcriptionally active subviral particle into the cytoplasm. VP5*, the rotavirus protein believed to interact with the membrane bilaye
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2895812e4886e38a1b4e888f7520aa01
https://doi.org/10.1128/jvi.01682-09
https://doi.org/10.1128/jvi.01682-09
Infectious entry of the nonenveloped rotavirus virion requires proteolysis of the spike protein VP4 to mediate conformational changes associated with membrane penetration. We sequenced and characterized an isolate that was cultured in the absence of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8291f33c72623d6cd518a1df0a971b87
https://europepmc.org/articles/PMC3709623/
https://europepmc.org/articles/PMC3709623/
Publikováno v:
Journal of virology. 87(11)
The rotavirus (RV) genome consists of 11 segments of double-stranded RNA (dsRNA). Typically, each segment contains 5′ and 3′ untranslated regions (UTRs) that flank an open reading frame (ORF) encoding a single protein. RV variants with segments o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6831fbc543ac40e8e5a73e5baaefaea3
https://pubmed.ncbi.nlm.nih.gov/23536662
https://pubmed.ncbi.nlm.nih.gov/23536662
Viral replication is rapid and robust, but it is far from a chaotic process. Instead, successful production of infectious progeny requires that events occur in the correct place and at the correct time. Rotaviruses (segmented double-stranded RNA viru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17a177a6a62109c1c730050978e72f12
https://europepmc.org/articles/PMC3771686/
https://europepmc.org/articles/PMC3771686/
Experiments in cell-free systems have demonstrated that the VP5* cleavage fragment of the rotavirus spike protein, VP4, undergoes a foldback rearrangement that translocates three clustered hydrophobic loops from one end of the molecule to the other.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a336a4ace923759b7bc6392853fbbd30
https://europepmc.org/articles/PMC2876642/
https://europepmc.org/articles/PMC2876642/
Autor:
Philip R. Dormitzer, Ningguo Feng, Phuoc T. Vo, Mawuena Binka, Joshua D. Yoder, Harry B. Greenberg, Shane D. Trask, Stephen C. Harrison
Publikováno v:
Journal of virology. 83(21)
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 rearrangemen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bf34653d3826818710ac197942aa458
https://pubmed.ncbi.nlm.nih.gov/19692464
https://pubmed.ncbi.nlm.nih.gov/19692464