Journal
JOURNAL OF VIROLOGICAL METHODS
Volume 181, Issue 1, Pages 1-5Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jviromet.2012.01.001
Keywords
Noroviruses; RNase; Binding; RT-PCR; Heat inactivation
Funding
- Ghent University
- China Scholarship Council
- Research Foundation-Flanders (Fonds voor Wetenschappelijk Onderzoek [FWO] Vlaanderen)
- USDA of USA
Ask authors/readers for more resources
Attempts were made to evaluate methods measuring the capsid integrity and/or functions of noroviruses (NoVs) following heat treatment. Intact viruses (Murine Norovirus-1 [MNV-1] and human NoV GII.4), virus like particles (VLPs) and P particles (expressed in vitro from the protruding domain of the viral capsid) of NoVs were used in this study. Following heat treatment, no significant difference of viral titer of MNV-1 versus NoV GII.4 was observed by RNase One RT-PCR or cell-binding RT-PCR, although cell-binding RT-PCR (to measure the capsid functions) revealed higher reductions than RNase One RT-PCR (to measure the capsid integrity). These results indicate that the function assay for receptor binding is more sensitive than the capsid integrity assay to measure the protected viral RNA. MNV-1 could be used as a surrogate for human NoVs by heat inactivation from the perspective of capsid integrity and/or functions. The heat resistance varied among different Gland GII NoV strains when their P particles were studied. (C) 2012 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available