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
doaj +3 more sources
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
doaj +3 more sources
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
openaire +5 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +4 more sources
Infectious Pancreatic Necrosis Virus VP5 Is Dispensable for Virulence and Persistence [PDF]
ABSTRACT Infectious pancreatic necrosis virus (IPNV) is the causative agent of infectious pancreatic necrosis (IPN) disease in salmonid fish. Recent studies have revealed variation in virulence between isolates of the Sp serotype, associated with certain residues of the structural protein VP2.
Nina, Santi +3 more
openaire +2 more sources
Effect of Mutations in VP5* Hydrophobic Loops on Rotavirus Cell Entry [PDF]
ABSTRACT 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.
Irene S, Kim +4 more
openaire +2 more sources
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
openaire +2 more sources
Ab initio modeling of the herpesvirus VP26 core domain assessed by CryoEM density.
Efforts in structural biology have targeted the systematic determination of all protein structures through experimental determination or modeling.
Matthew L Baker +5 more
doaj +1 more source

