ArticleVirology2008
Epitope mapping and use of epitope-specific antisera to characterize the VP5* binding site in rotavirus SA11 NSP4.
Article in Virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Viroporin activity is necessary for intercellular calcium signals that contribute to viral pathogenesis.Science advances · 2025Article
- Bile acid-sensitive human norovirus strains are susceptible to sphingosine-1-phosphate receptor 2 inhibition.Journal of virology · 2024Article
- Host IPmBio · 2024Article
- Rotavirus induces intercellular calcium waves through ADP signaling.Science (New York, N.Y.) · 2020Article
- COPII Vesicle Transport Is Required for Rotavirus NSP4 Interaction with the Autophagy Protein LC3 II and Trafficking to Viroplasms.Journal of virology · 2019Article
- Rotavirus Calcium Dysregulation Manifests as Dynamic Calcium Signaling in the Cytoplasm and Endoplasmic Reticulum.Scientific reports · 2019Article
- The Rotavirus NSP4 Viroporin Domain is a Calcium-conducting Ion Channel.Scientific reports · 2017Article
- Higher Expression Level and Lower Toxicity of Genetically Spliced Rotavirus NSP4 in Comparison to the Full-Length Protein inIranian journal of biotechnology · 2016Article
- Structural plasticity of the coiled-coil domain of rotavirus NSP4.Journal of virology · 2014Article
- Activation of the endoplasmic reticulum calcium sensor STIM1 and store-operated calcium entry by rotavirus requires NSP4 viroporin activity.Journal of virology · 2013Article
- Autophagy hijacked through viroporin-activated calcium/calmodulin-dependent kinase kinase-β signaling is required for rotavirus replication.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Rotavirus non-structural proteins: structure and function.Current opinion in virology · 2012Review
- Genetic divergence of rotavirus nonstructural protein 4 results in distinct serogroup-specific viroporin activity and intracellular punctate structure morphologies.Journal of virology · 2012Article
- Rotavirus NSP4 is secreted from infected cells as an oligomeric lipoprotein and binds to glycosaminoglycans on the surface of non-infected cells.Virology journal · 2011Article
- Novel pentameric structure of the diarrhea-inducing region of the rotavirus enterotoxigenic protein NSP4.Journal of virology · 2011Article
- Rotavirus NSP4: Cell type-dependent transport kinetics to the exofacial plasma membrane and release from intact infected cells.Virology journal · 2011Article
- Multiplex reverse transcription PCR Luminex assay for detection and quantitation of viral agents of gastroenteritis.Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology · 2011Article
- Article
- Rotavirus vaccines and pathogenesis: 2008.Current opinion in gastroenterology · 2009Review
- Integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxin.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Rotavirus (RV) is the leading cause of infantile gastroenteritis worldwide. RV nonstructural protein 4 (NSP4), the first characterized viral enterotoxin, is a 28-kDa glycoprotein that has pleiotropic functions in RV infection and pathogenesis. NSP4 has multiple forms enabling it to perform its different functions. Dissecting such functions could be facilitated by use of epitope-specific antibodies. This work mapped the epitopes for the monoclonal antibody B4-2/55 and three polyclonal antisera generated against synthetic SA11 NSP4 peptides corresponding to residues 114-135, 120-147, and 150-175. The epitope for B4-2/55 mapped to residues 100-118, wherein residues E105, R108 and E111 are critical for antibody binding. Antiserum generated to two peptides (aa114-135 and aa120-147) with enterotoxin activity each recognize a single but distinct epitope. The epitope for the peptide antiserum to aa114-135 was mapped to residues 114-125 with highly conserved residues T117/T118, E120, and E122 being critical for antibody binding. The peptide antiserum to aa120-147 binds to NSP4 at residues 130-140 and residues Q137-T138 are critical for this epitope. Finally, the epitope for the antiserum to peptide aa150-175 mapped to residues 155-170, wherein residues E160 and E170 are critical for antibody binding. Knowledge of the binding sites of domain-specific antibodies can aid in further characterizing different functions of NSP4. To demonstrate this, we characterized the interaction between NSP4 and VP5() [K(D)=0.47 microM] and show that binding of NSP4 to VP5* is blocked by antibody to NSP4 aa114-135 and aa120-147, but not aa150-175. The use of single epitope-specific antibodies to differentially block functions of NSP4 is a feasible approach to determine the functional domain structure of this important RV virulence factor.
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Registered trials
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