Results 21 to 30 of about 10,250 (201)

The VP5 Domain of VP4 Can Mediate Attachment of Rotaviruses to Cells [PDF]

Journal of Virology, 2000
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, R, Espinosa, P, Romero, E, Méndez, C F, Arias, S, López   +5 more
openaire   +5 more sources

VP5* Rearranges when Rotavirus Uncoats [PDF]

Journal of Virology, 2009
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, Shane D, Trask, T Phuoc, Vo, Mawuena, Binka, Ningguo, Feng, Stephen C, Harrison, Harry B, Greenberg, Philip R, Dormitzer   +7 more
openaire   +2 more sources

Bluetongue virus capsid protein VP5 perforates membranes at low endosomal pH during viral entry. [PDF]

, 2021
Bluetongue virus (BTV) is a non-enveloped virus and causes substantial morbidity and mortality in ruminants such as sheep. Fashioning a receptor-binding protein (VP2) and a membrane penetration protein (VP5) on the surface, BTV releases its genome ...
Cui, Yanxiang, Roy, Polly, Zhou, Z. Hong, Wu, Weining, Xia, Xian, Zhou, Z Hong, Z. Hong Zhou, Xian Xia, Weining Wu, Polly Roy, Yanxiang Cui   +10 more
core   +1 more source

Rotavirus Capsid Protein VP5* Permeabilizes Membranes [PDF]

Journal of Virology, 1999
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, W, Dowling, R, LaMonica, R, Shaw, S, Scarlata, F, Ruggeri, E R, Mackow   +6 more
openaire   +2 more sources

Enhanced and Extended Anti-Hypertensive Effect of VP5 Nanoparticles [PDF]

International Journal of Molecular Sciences, 2016
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, Zhao, Shengnan, Li, Ziqiang, Xu, Bei, Fang, Dailong, Wang, Fazhan, Zhang, Zhi, He, Lili, Song, Xiangrong, Yang, Jian, Wang, Yi   +10 more
openaire   +4 more sources

Infectious Pancreatic Necrosis Virus VP5 Is Dispensable for Virulence and Persistence [PDF]

Journal of Virology, 2005
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, Haichen, Song, Vikram N, Vakharia, Øystein, Evensen   +3 more
openaire   +2 more sources

Cypovirus capsid protein VP5 has nucleoside triphosphatase activity [PDF]

Virologica Sinica, 2017
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, Qi Qian, Teng-Feng Li, Xueli Yang, Sok Jin Won, Xi Zhou   +5 more
openaire   +2 more sources

Cross‐Neutralizing and Broadly Neutralizing Human Antibodies Against Nonenveloped Viruses [PDF]

Eur J Immunol
In this review article, Marchand et al. compare cross ‐ and broadly ‐neutralizing human antibodies against non ‐ enveloped viruses from several major families, discussing their structural characteristics, neutralization mechanisms and relevance for the development of antiviral vaccines and therapeutics.
Marchand S, Taouli S, McIlroy D.
europepmc   +2 more sources

Effect of Mutations in VP5* Hydrophobic Loops on Rotavirus Cell Entry [PDF]

Journal of Virology, 2010
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, Shane D, Trask, Marina, Babyonyshev, Philip R, Dormitzer, Stephen C, Harrison   +4 more
openaire   +2 more sources

Proteolysis of Monomeric Recombinant Rotavirus VP4 Yields an Oligomeric VP5* Core [PDF]

Journal of Virology, 2001
ABSTRACT Rotavirus particles are activated for cell entry by trypsin cleavage of the outer capsid spike protein, VP4, into a hemagglutinin, VP8*, and a membrane penetration protein, VP5*. We have purified rhesus rotavirus VP4, expressed in baculovirus-infected insect cells.
Dormitzer, Philip R., Greenberg, Harry B., Harrison, Stephen C.   +2 more
openaire   +4 more sources