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 +4 more
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The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to Ca2+
, 2023 ABSTRACTRotaviruses infect cells by delivering into the cytosol a transcriptionally active inner capsid particle (a "double-layer particle": DLP). Delivery is the function of a third, outer layer, which drives uptake from the cell surface into small vesicles from which the DLPs escape.
Marilina De Sautu +3 more
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Ab initio modeling of the herpesvirus VP26 core domain assessed by CryoEM density.
PLoS Computational Biology, 2006 Efforts in structural biology have targeted the systematic determination of all protein structures through experimental determination or modeling.
Matthew L Baker +5 more
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Establishment of Sandwich ELISA for Quality Control in Rotavirus Vaccine Production
Vaccines, 2022 Non-replicating rotavirus vaccines are alternative strategies that may improve the protective efficacy of rotavirus vaccines in low- and middle-income countries.
Cao Li +9 more
doaj +1 more source
A synthetic biology approach for a vaccine platform against known and newly emerging serotypes of bluetongue virus [PDF]
, 2014 Bluetongue is one of the major infectious diseases of ruminants and is caused by Bluetongue virus (BTV), an arbovirus existing in nature in at least 26 distinct serotypes. Here, we describe the development of a vaccine platform for BTV.
Brunet, Silvie +6 more
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Alternative intermolecular contacts underlie the rotavirus VP5* two‐ to three‐fold rearrangement [PDF]
The EMBO Journal, 2006 The spike protein VP4 is a key component of the membrane penetration apparatus of rotavirus, a nonenveloped virus that causes childhood gastroenteritis. Trypsin cleavage of VP4 produces a fragment, VP5*, with a potential membrane interaction region, and primes rotavirus for cell entry.
Joshua D, Yoder, Philip R, Dormitzer
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Bluetongue virus capsid protein VP5 perforates membranes at low endosomal pH during viral entry [PDF]
Nature Microbiology, 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-containing core (VP3 and VP7) into the host cell cytosol after perforation of the endosomal membrane ...
Xian Xia +4 more
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Viruses, 2021 The bluetongue virus (BTV) is transmitted by Culicoides biting midges and causes bluetongue (BT), an OIE-notifiable disease of ruminants. At least 29 BTV serotypes are described as determined by the outer shell proteins VP2 and VP5.
Piet A. van Rijn +2 more
doaj +1 more source
Antigenic and biochemical characterization of bovine rotavirus V1005, a new member of rotavirus serotype 10 [PDF]
, 1990 Bovine rotavirus (BRV) V1005 is serologically distinct from rotavirus serotypes 1, 2, 3, 4, 5, 6, 8 and 9. BRV V1005 showed cross-reactions with BRV B223, the American prototype of serotype 10 rotavirus, and with BRV E4049, a British serotype 10 isolate.
Bruttin, Anne +5 more
core +1 more source
Infectious bursal disease virus VP5 polypeptide: a phosphoinositide-binding protein required for efficient cell-to-cell virus dissemination. [PDF]
PLoS ONE, 2015 Infectious bursal disease virus (IBDV), a member of the Birnaviridae family, is a major avian pathogen responsible for an immunosuppressive disease affecting juvenile chickens. The IBDV genome is formed by two dsRNA segments.
Fernando Méndez +3 more
doaj +1 more source