Modular glycosphere assays for high-throughput functional characterization of influenza viruses
Identifieur interne : 001633 ( Ncbi/Checkpoint ); précédent : 001632; suivant : 001634Modular glycosphere assays for high-throughput functional characterization of influenza viruses
Auteurs : Sven N. Hobbie [Singapour] ; Karthik Viswanathan [États-Unis] ; Ido Bachelet [États-Unis] ; Udayanath Aich [États-Unis] ; Zachary Shriver [États-Unis] ; Vidya Subramanian [États-Unis] ; Rahul Raman [États-Unis] ; Ram Sasisekharan [Singapour, États-Unis]Source :
- BMC Biotechnology [ 1472-6750 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antiviraux (), Anticorps antiviraux (analyse), Attachement viral, Biotine (), Humains, Hémagglutinines (métabolisme), Microsphères, Oiseaux, Orthomyxoviridae (isolement et purification), Orthomyxoviridae (métabolisme), Polyosides (analyse), Polyosides (métabolisme), Sous-type H1N1 du virus de la grippe A (isolement et purification), Sous-type H1N1 du virus de la grippe A (métabolisme), Sous-type H5N1 du virus de la grippe A (isolement et purification), Sous-type H5N1 du virus de la grippe A (métabolisme), Streptavidine (), Tests de criblage à haut débit ().
- MESH :
- analyse : Anticorps antiviraux, Polyosides.
- isolement et purification : Orthomyxoviridae, Sous-type H1N1 du virus de la grippe A, Sous-type H5N1 du virus de la grippe A.
- métabolisme : Hémagglutinines, Orthomyxoviridae, Polyosides, Sous-type H1N1 du virus de la grippe A, Sous-type H5N1 du virus de la grippe A.
- Animaux, Anticorps antiviraux, Attachement viral, Biotine, Humains, Microsphères, Oiseaux, Streptavidine, Tests de criblage à haut débit.
English descriptors
- KwdEn :
- Animals, Antibodies, Viral (analysis), Antibodies, Viral (chemistry), Biotin (chemistry), Birds, Hemagglutinins (metabolism), High-Throughput Screening Assays (methods), Humans, Influenza A Virus, H1N1 Subtype (isolation & purification), Influenza A Virus, H1N1 Subtype (metabolism), Influenza A Virus, H5N1 Subtype (isolation & purification), Influenza A Virus, H5N1 Subtype (metabolism), Microspheres, Orthomyxoviridae (isolation & purification), Orthomyxoviridae (metabolism), Polysaccharides (analysis), Polysaccharides (metabolism), Streptavidin (chemistry), Virus Attachment.
- MESH :
- chemical , analysis : Antibodies, Viral, Polysaccharides.
- chemical , chemistry : Antibodies, Viral, Biotin, Streptavidin.
- chemical , metabolism : Hemagglutinins, Polysaccharides.
- isolation & purification : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H5N1 Subtype, Orthomyxoviridae.
- metabolism : Influenza A Virus, H1N1 Subtype, Influenza A Virus, H5N1 Subtype, Orthomyxoviridae.
- methods : High-Throughput Screening Assays.
- Animals, Birds, Humans, Microspheres, Virus Attachment.
Abstract
The ongoing global efforts to control influenza epidemics and pandemics require high-throughput technologies to detect, quantify, and functionally characterize viral isolates. The 2009 influenza pandemic as well as the recent in-vitro selection of highly transmissible H5N1 variants have only increased existing concerns about emerging influenza strains with significantly enhanced human-to-human transmissibility. High-affinity binding of the virus hemagglutinin to human receptor glycans is a highly sensitive and stringent indicator of host adaptation and virus transmissibility. The surveillance of receptor-binding characteristics can therefore provide a strong additional indicator for the relative hazard imposed by circulating and newly emerging influenza strains.
Streptavidin-coated microspheres were coated with selected biotinylated glycans to mimic either human or avian influenza host-cell receptors. Such glycospheres were used to selectively capture influenza virus of diverse subtypes from a variety of samples. Bound virus was then detected by fluorescently labelled antibodies and analyzed by quantitative flow cytometry. Recombinant hemagglutinin, inactivated virus, and influenza virions were captured and analyzed with regards to receptor specificity over a wide range of analyte concentration. High-throughput analyses of influenza virus produced dose–response curves that allow for functional assessment of relative receptor affinity and thus transmissibility.
Modular glycosphere assays for high-throughput functional characterization of influenza viruses introduce an important tool to augment the surveillance of clinical and veterinarian influenza isolates with regards to receptor specificity, host adaptation, and virus transmissibility.
Url:
DOI: 10.1186/1472-6750-13-34
PubMed: 23587408
PubMed Central: 3751502
Affiliations:
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>The ongoing global efforts to control influenza epidemics and pandemics require high-throughput technologies to detect, quantify, and functionally characterize viral isolates. The 2009 influenza pandemic as well as the recent in-vitro selection of highly transmissible H5N1 variants have only increased existing concerns about emerging influenza strains with significantly enhanced human-to-human transmissibility. High-affinity binding of the virus hemagglutinin to human receptor glycans is a highly sensitive and stringent indicator of host adaptation and virus transmissibility. The surveillance of receptor-binding characteristics can therefore provide a strong additional indicator for the relative hazard imposed by circulating and newly emerging influenza strains.</p>
</sec>
<sec><title>Results</title>
<p>Streptavidin-coated microspheres were coated with selected biotinylated glycans to mimic either human or avian influenza host-cell receptors. Such glycospheres were used to selectively capture influenza virus of diverse subtypes from a variety of samples. Bound virus was then detected by fluorescently labelled antibodies and analyzed by quantitative flow cytometry. Recombinant hemagglutinin, inactivated virus, and influenza virions were captured and analyzed with regards to receptor specificity over a wide range of analyte concentration. High-throughput analyses of influenza virus produced dose–response curves that allow for functional assessment of relative receptor affinity and thus transmissibility.</p>
</sec>
<sec><title>Conclusions</title>
<p>Modular glycosphere assays for high-throughput functional characterization of influenza viruses introduce an important tool to augment the surveillance of clinical and veterinarian influenza isolates with regards to receptor specificity, host adaptation, and virus transmissibility.</p>
</sec>
</div>
</front>
<back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Miller, Ma" uniqKey="Miller M">MA Miller</name>
</author>
<author><name sortKey="Viboud, C" uniqKey="Viboud C">C Viboud</name>
</author>
<author><name sortKey="Balinska, M" uniqKey="Balinska M">M Balinska</name>
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<author><name sortKey="Simonsen, L" uniqKey="Simonsen L">L Simonsen</name>
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<author><name sortKey="Taubenberger, Jk" uniqKey="Taubenberger J">JK Taubenberger</name>
</author>
<author><name sortKey="Fauci, As" uniqKey="Fauci A">AS Fauci</name>
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