Mutational Asymmetries in the SARS-CoV-2 Genome May Lead to Increased Hydrophobicity of Virus Proteins
Laboratory of Molecular Epigenetics, Institute of Biophysics, Academy of Sciences of the Czech Republic, Královopolská 135, 61265 Brno, Czech Republic
*
Author to whom correspondence should be addressed.
Academic Editors: Giuseppe Novelli and Michela Biancolella
Genes 2021, 12(6), 826; https://doi.org/10.3390/genes12060826
Received: 25 March 2021
/
Revised: 21 May 2021
/
Accepted: 25 May 2021
/
Published: 27 May 2021
(This article belongs to the Special Issue COVID-19 and Molecular Genetics)
The genomic diversity of SARS-CoV-2 has been a focus during the ongoing COVID-19 pandemic. Here, we analyzed the distribution and character of emerging mutations in a data set comprising more than 95,000 virus genomes covering eight major SARS-CoV-2 lineages in the GISAID database, including genotypes arising during COVID-19 therapy. Globally, the C>U transitions and G>U transversions were the most represented mutations, accounting for the majority of single-nucleotide variations. Mutational spectra were not influenced by the time the virus had been circulating in its host or medical treatment. At the amino acid level, we observed about a 2-fold excess of substitutions in favor of hydrophobic amino acids over the reverse. However, most mutations constituting variants of interests of the S-protein (spike) lead to hydrophilic amino acids, counteracting the global trend. The C>U and G>U substitutions altered codons towards increased amino acid hydrophobicity values in more than 80% of cases. The bias is explained by the existing differences in the codon composition for amino acids bearing contrasting biochemical properties. Mutation asymmetries apparently influence the biochemical features of SARS CoV-2 proteins, which may impact protein–protein interactions, fusion of viral and cellular membranes, and virion assembly.
View Full-Text
Keywords:
SARS-CoV-2; coronavirus; mutability; evolution; genetic variation; apolipoprotein B mRNA editing enzyme (APOBEC); amino acid hydrophobicity
▼
Show Figures
Figure 1
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited
- Supplementary File 1:
ZIP-Document (ZIP, 2286 KiB)
MDPI and ACS Style
Matyášek, R.; Řehůřková, K.; Berta Marošiová, K.; Kovařík, A. Mutational Asymmetries in the SARS-CoV-2 Genome May Lead to Increased Hydrophobicity of Virus Proteins. Genes 2021, 12, 826. https://doi.org/10.3390/genes12060826
AMA Style
Matyášek R, Řehůřková K, Berta Marošiová K, Kovařík A. Mutational Asymmetries in the SARS-CoV-2 Genome May Lead to Increased Hydrophobicity of Virus Proteins. Genes. 2021; 12(6):826. https://doi.org/10.3390/genes12060826
Chicago/Turabian StyleMatyášek, Roman, Kateřina Řehůřková, Kristýna Berta Marošiová, and Aleš Kovařík. 2021. "Mutational Asymmetries in the SARS-CoV-2 Genome May Lead to Increased Hydrophobicity of Virus Proteins" Genes 12, no. 6: 826. https://doi.org/10.3390/genes12060826
Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.
