<div class="csl-bib-body">
<div class="csl-entry">Allmaier, G., Weiss, V., & Blaas, D. (2022, June 14). <i>Intact human rhinovirus: Purification by monolithic chromatography followed by sizing/molecular mass determination by nano electrospray differential mobility analysis</i> [Conference Presentation]. 9th Monolith Summer Symposium, Portoroz, Slovenia.</div>
</div>
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dc.identifier.uri
http://hdl.handle.net/20.500.12708/152644
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dc.description.abstract
For structural characterization from the primary to the 3D structure, direct fluorescent labeling, vaccine development, and numerous other studies, homogeneous and intact virus preparations of high purity are essential. Working with human rhinoviruses (HRVs), members of the picornavirus family and the main cause of generally mild respiratory infections, we noticed that our routine laboratory preparations of HRVs appeared highly homogeneous on analysis by means of sodium dodecyl sulfate polyacrylamide gel electrophoresis, exclusively showing the four viral capsid proteins (VPs) which are only partly sequenced on the protein level. However, the preparations turned out to contain substantial amounts of contaminating material when analyzed by orthogonal analytical techniques including nano electrospray differential mobility analysis (nES DMA), capillary zone electrophoresis (UV fluorescence), and negative stain transmission electron microscopy. Because these latter analyses are not routine to many particularly biochemical/virology-oriented laboratories, the above contaminations might remain unnoticed and skew experimental and particularly functional results. By using HRV serotype A2 as example prepared by HeLa A1 cell culture and centrifugation we report monolithic anion-exchange chromatography as a last polishing step in the isolation/purification and demonstrate that it yields infective, highly pure, virus (was confirmed by peptide mass fingerprinting) devoid of foreign material as judged by the mentioned criteria. Exact size determination (29.5 nm) and the unsurpassed narrow width of the virus size distribution determined by nES DMA was achieved.
en
dc.language.iso
en
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dc.subject
Human Rhinovirus
en
dc.subject
nES GEMMA
en
dc.subject
Differential Mobility Analysis
en
dc.title
Intact human rhinovirus: Purification by monolithic chromatography followed by sizing/molecular mass determination by nano electrospray differential mobility analysis
en
dc.type
Presentation
en
dc.type
Vortrag
de
dc.type.category
Conference Presentation
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tuw.researchTopic.id
M2
-
tuw.researchTopic.id
M6
-
tuw.researchTopic.id
M4
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tuw.researchTopic.name
Materials Characterization
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tuw.researchTopic.name
Biological and Bioactive Materials
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tuw.researchTopic.name
Non-metallic Materials
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tuw.researchTopic.value
30
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tuw.researchTopic.value
40
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tuw.researchTopic.value
30
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tuw.linking
https://www.monolith-events.com/
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tuw.publication.orgunit
E164-01-1 - Forschungsgruppe Massenspektrometrische Bio- und Polymeranalytik
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tuw.author.orcid
0000-0002-1438-9462
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tuw.author.orcid
0000-0002-0056-6819
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tuw.event.name
9th Monolith Summer Symposium
en
tuw.event.startdate
13-06-2022
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tuw.event.enddate
17-06-2022
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tuw.event.online
Hybrid
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tuw.event.type
Event for scientific audience
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tuw.event.place
Portoroz
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tuw.event.country
SI
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tuw.event.presenter
Allmaier, Günter
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wb.sciencebranch
Chemie
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wb.sciencebranch.oefos
1040
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wb.sciencebranch.value
100
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item.languageiso639-1
en
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item.openairetype
conference paper not in proceedings
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item.grantfulltext
none
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item.fulltext
no Fulltext
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item.cerifentitytype
Publications
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item.openairecristype
http://purl.org/coar/resource_type/c_18cp
-
crisitem.author.dept
E164-01-1 - Forschungsgruppe Massenspektrometrische Bio- und Polymeranalytik
-
crisitem.author.dept
E164-01-1 - Forschungsgruppe Massenspektrometrische Bio- und Polymeranalytik
-
crisitem.author.orcid
0000-0002-1438-9462
-
crisitem.author.orcid
0000-0002-0056-6819
-
crisitem.author.parentorg
E164-01 - Forschungsbereich Imaging und Instrumentelle Analytische Chemie
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crisitem.author.parentorg
E164-01 - Forschungsbereich Imaging und Instrumentelle Analytische Chemie
