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. 2013 Nov 13:5:ecurrents.outbreaks.22254b58675cdebc256dbe3c5aa6498b.
doi: 10.1371/currents.outbreaks.22254b58675cdebc256dbe3c5aa6498b.

Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission

Gerard Kian-Meng Goh  1 , A Keith Dunker, Vladimir Uversky
Affiliations

Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission

Gerard Kian-Meng Goh et al. PLoS Curr. .

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.

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Figures

Graphical comparison of the PID in MERS-CoV and other coronaviruses.
Graphical comparison of the PID in MERS-CoV and other coronaviruses.
The chart illustrates the pair-wise similarity of disorder contents in M- and N-proteins of MERS-CoV and TGEV belonging to the category C. M- and N-proteins of SARS-CoV and PEDV (both are from the category B) also possess similar PID contents, whereas the proteins of the bat coronavirus are located at the borderline between the categories B and C. Group A (HCoV 229E and IBV) is characterized by the most disordered M- and N-proteins.
Disorder propensities of the coronaviral M-proteins.
Disorder propensities of the coronaviral M-proteins.
Evaluating disorder propensities of the M-proteins from IBV (A), SARS-CoV (B), MHV (C), Bat-HKU4 (D), Bat-HKU5 (E), and MERS-CoV (F) by the PONDR-FIT algorithm. Scores above 0.5 correspond to the disordered residues/regions (shaded in light pink), whereas scores below 0.5 indicate residues/regions predicted to be ordered (shaded in light cyan). Pink shades around the PONDR-FIT curves (dark red) reflect the distributions of errors in evaluating the disorder scores.
Disorder propensities of the coronaviral N-proteins.
Disorder propensities of the coronaviral N-proteins.
Analysis of the disorder propensities of the N-proteins from IBV (A), SARS-CoV (B), MHV (C), Bat-HKU4 (D), Bat-HKU5 (E), and MERS-CoV (F) by the PONDR-FIT algorithm. Scores above 0.5 correspond to the disordered residues/regions (shaded in light pink), whereas scores below 0.5 indicate residues/regions predicted to be ordered (shaded in light cyan). Pink shades around the PONDR-FIT curves (dark red) reflect the distributions of errors in evaluating the disorder scores.
Structures of the ordered domains of the N-proteins.
Structures of the ordered domains of the N-proteins.
3D-structures of the ordered domains of N-proteins of three coronaviruses from different disorder groups, group A: IBV (A), group B: SARS-CoV (B), and group C: MHV (C). In addition to the available 3D-structures of the RNA-binding and dimerization domains, each panel contains the PONDR-FIT profile, where the localization of these domains is shown by blue and dark yellow bars, respectively. For IBV, the shown structures of the RNA-binding and dimerization domains are 2BXX (residues 29-160) and 2CA1 (residues 218-326). For SARS-CoV, structures of the RNA-binding and dimerization domains are 1SSK (residues 45-181) and 2JW8 (residues 248-365). For MHV, the only available structure is the structure of the RNA-binding domain (PDB code: 3HD4, residues 60-197). Structures were drawn using the VMD software.
Structural alignments of the ordered domains of coronaviral N-proteins.
Structural alignments of the ordered domains of coronaviral N-proteins.
Structural alignments of the RNA-binding domains (A) and dimerization domains (B) of the N-proteins from three representative members of the coronavirus family, IBV (blue structures), SARS-CoV (red structures) and MHV (grey structure). The structural alignment was done by MultiProt (http://bioinfo3d.cs.tau.ac.il/MultiProt/). The aligned structures were drawn using the VMD software.
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