Primed for Discovery: Atomic-Resolution Cryo-EM Structure of a Reovirus Entry Intermediate [PDF]
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.
Shane D. Trask +2 more
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Molecular Characterization of Outer Capsid Proteins VP5 and VP7 of Grass Carp Reovirus
Aquareovirus, which is a member of the Reoviridae family, was isolated from aquatic animals. A close molecular evolutionary relationship between aquareoviruses and mammalian orthoreoviruses was revealed.
Fuxian Zhang, Diangang Sun, Qin Fang
doaj +3 more sources
Analysis of Conserved, Computationally Predicted Epitope Regions for VP5 and VP7 Across three Orbiviruses [PDF]
Orbiviruses are double-stranded RNA viruses that have profound economic and veterinary significance, 3 of the most important being African horse sickness virus (AHSV), bluetongue virus (BTV), and epizootic hemorrhagic disease virus (EHDV).
Bonnie L Russell +2 more
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Proteomic analysis reveals differential accumulation of small heat shock proteins and late embryogenesis abundant proteins between ABA-deficient mutant vp5 seeds and wild-type Vp5 seeds in maize [PDF]
ABA is a major plant hormone that plays important roles during many phases of plant life cycle, including seed development, maturity and dormancy, and especially the acquisition of desiccation tolerance.
Xiaolin eWu +5 more
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VP5* Rearranges when Rotavirus Uncoats [PDF]
ABSTRACT 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 ...
Joshua D, Yoder +7 more
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Rotavirus Capsid Protein VP5* Permeabilizes Membranes [PDF]
ABSTRACT Proteolytic cleavage of the VP4 outer capsid spike protein into VP8* and VP5* proteins is required for rotavirus infectivity and for rotavirus-induced membrane permeability. In this study we addressed the function of the VP5* cleavage fragment in permeabilizing membranes.
E, Denisova +6 more
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Grass carp hemorrhagic disease caused by grass carp reovirus (GCRV) results in significant economic losses to the global grass carp aquaculture industry. Oral vaccination is an ideal choice for disease precaution in aquaculture. However, oral vaccine can
Chaolin Jiang +6 more
doaj +1 more source
Cypovirus capsid protein VP5 has nucleoside triphosphatase activity [PDF]
As a major protein of cypovirus capsid shell,VP5 performs as the clamp protein to stabilize the capsid shell structure (Yu et al.,2008).And as a part of viral RNA (vRNA) replication machinery,VP5 has been found to possess an ATP-independent RNA chaperoning activity (Yang et al.,2014).Here,we report that VP5 also has the nucleoside triphosphatase ...
Jie Yang +5 more
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The VP5 Domain of VP4 Can Mediate Attachment of Rotaviruses to Cells [PDF]
ABSTRACT Some animal rotaviruses require the presence of sialic acid (SA) on the cell surface to infect the cell. We have isolated variants of rhesus rotavirus (RRV) whose infectivity no longer depends on SA. Both the SA-dependent and -independent interactions of these viruses with the cell are mediated by the virus spike protein
S, Zárate +5 more
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Enhanced and Extended Anti-Hypertensive Effect of VP5 Nanoparticles [PDF]
Hypertension has become a significant global public health concern and is also one of the most common risk factors of cardiovascular disease. Recent studies have shown the promising result of peptides inhibiting angiotensin converting enzyme (ACE) in lowering the blood pressure in both animal models and humans.
Yu, Ting +10 more
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