ArticleJournal of virology2005
pH-induced conformational change of the rotavirus VP4 spike: implications for cell entry and antibody neutralization.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Investigation of the presence of human adenovirus, norovirus, and rotavirus in tap water in Marrakech, Morocco.Applied and environmental microbiology · 2026Article
- Rotavirus Reverse Genetics Systems and Oral Vaccine Delivery Vectors for Mucosal Vaccination.Microorganisms · 2025Review
- Genetic and antigenic characterization of two diarrhoeicdominant rotavirus A genotypes G3P[12] and G14P[12] circulating in the global equine population.The Journal of general virology · 2024Article
- The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to Ca2.PLoS pathogens · 2024Article
- Penetration of non-enveloped viruses.Nature microbiology · 2021Article
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- Article
- Structural Insights into Reovirus σ1 Interactions with Two Neutralizing Antibodies.Journal of virology · 2017Article
- Both Lewis and secretor status mediate susceptibility to rotavirus infections in a rotavirus genotype-dependent manner.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2014Article
- Histo-blood group antigens: a common niche for norovirus and rotavirus.Expert reviews in molecular medicine · 2014Review
- Spike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner.Journal of virology · 2012Article
- Lack of correlation between virus barosensitivity and the presence of a viral envelope during inactivation of human rotavirus, vesicular stomatitis virus, and avian metapneumovirus by high-pressure processing.Applied and environmental microbiology · 2011Article
- Atomic model of an infectious rotavirus particle.The EMBO journal · 2011Article
- Simian rotaviruses possess divergent gene constellations that originated from interspecies transmission and reassortment.Journal of virology · 2010Article
- Rotavirus architecture at subnanometer resolution.Journal of virology · 2009Article
- Sindbis virus conformational changes induced by a neutralizing anti-E1 monoclonal antibody.Journal of virology · 2008Article
- Geometric mismatches within the concentric layers of rotavirus particles: a potential regulatory switch of viral particle transcription activity.Journal of virology · 2008Article
- Assembly of highly infectious rotavirus particles recoated with recombinant outer capsid proteins.Journal of virology · 2006Article
- Alternative intermolecular contacts underlie the rotavirus VP5* two- to three-fold rearrangement.The EMBO journal · 2006Article
- High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain.Journal of virology · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The rotavirus spike protein, VP4, is a major determinant of infectivity and neutralization. Previously, we have shown that trypsin-enhanced infectivity of rotavirus involves a transformation of the VP4 spike from a flexible to a rigid bilobed structure. Here we show that at elevated pH the spike undergoes a drastic, irreversible conformational change and becomes stunted, with a pronounced trilobed appearance. These particles with altered spikes, at a normal pH of 7.5, despite the loss of infectivity and the ability to hemagglutinate, surprisingly exhibit sialic acid (SA)-independent cell binding in contrast to the SA-dependent cell binding exhibited by native virions. Remarkably, a neutralizing monoclonal antibody that remains bound to spikes throughout the pH changes (pH 7 to 11 and back to pH 7) completely prevents this conformational change, preserving the SA-dependent cell binding and hemagglutinating functions of the virion. A hypothesis that emerges from the present study is that high-pH treatment triggers a conformational change that mimics a post-SA-attachment step to expose an epitope recognized by a downstream receptor in the rotavirus cell entry process. This process involves sequential interactions with multiple receptors, and the mechanism by which the antibody neutralizes is by preventing this conformational change.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.