Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission
Open Access
- 1 January 2013
- journal article
- Published by Public Library of Science (PLoS) in PLoS Currents
Abstract
A novel coronavirus, MERS-CoV (NCoV, HCoV-EMC/2012), originating from the Middle-East, has been discovered. Incoming data reveal that the virus is highly virulent to humans. A model that categorizes coronaviuses according to the hardness of their shells was developed before the discovery of MERS-CoV. Using protein intrinsic disorder prediction, coronaviruses were categorized into three groups that can be linked to the levels of oral-fecal and respiratory transmission regardless of genetic proximity. Using this model, MERS-CoV is placed into disorder group C, which consists of coronaviruses that have relatively hard inner and outer shells. The members of this group are likely to persist in the environment for a longer period of time and possess the highest oral-fecal components but relatively low respiratory transmission components. Oral-urine and saliva transmission are also highly possible since both require harder protective shells. Results show that disorder prediction can be used as a tool that suggests clues to look for in further epidemiological investigations.Keywords
This publication has 77 references indexed in Scilit:
- The Emergence of Human Coronavirus EMC: How Scared Should We Be?mBio, 2013
- Differential Cell Line Susceptibility to the Emerging Novel Human Betacoronavirus 2c EMC/2012: Implications for Disease Pathogenesis and Clinical ManifestationThe Journal of Infectious Diseases, 2013
- A novel coronavirus capable of lethal human infections: an emerging pictureVirology Journal, 2013
- Understanding Viral Transmission Behavior via Protein Intrinsic Disorder Prediction: CoronavirusesJournal of Pathogens, 2012
- Intrinsically unstructured proteinsTrends in Biochemical Sciences, 2002
- What does it mean to be natively unfolded?European Journal of Biochemistry, 2002
- The protein trinity—linking function and disorderNature Biotechnology, 2001
- Intrinsically disordered proteinPublished by Elsevier ,2001
- Why are ?natively unfolded? proteins unstructured under physiologic conditions?Proteins-Structure Function and Bioinformatics, 2000
- Intrinsically unstructured proteins: re-assessing the protein structure-function paradigmJournal of Molecular Biology, 1999