Mutation detail:
| Mutation site | R13A |
| Virus | MERS-CoV |
Mutation level  |
Amino acid level |
| Gene/protein/region type | ORF1ab(nsp1) |
| Gene ID | 14254602 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | JX869059.2 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
decrease |
| Pathogenicity mechanism | Therefore, as shown in Fig. 5D, we used Mfold software to predict the MERS-CoV RNA structure from 1 to 460 nt containing the nsp1-coding region (Zuker, 2003). The predicted structure revealed that the R13A mutation in nsp1 affected the secondary structure |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | 1AB polyprotein |
| Uniprot protein ID | K9N7C7 |
| Protein length | 7078 amino acids |
| Protein description | ORF1ab, the largest gene, contains overlapping open reading frames that encode polyproteins PP1ab and PP1a. The polyproteins are cleaved to yield 16 nonstructural proteins, NSP1-16. Production of the longer (PP1ab) or shorter protein (PP1a) depends on a -1 ribosomal frameshifting event. The proteins, based on similarity to other coronaviruses, include the papain-like proteinase protein (NSP3), 3C-like proteinase (NSP5), RNA-dependent RNA polymerase (NSP12, RdRp), helicase (NSP13, HEL), endoRNAse (NSP15), 2'-O-Ribose-Methyltransferase (NSP16) and other nonstructural proteins.MERS-CoV nonstructural proteins are responsible for viral transcription, replication, proteolytic processing, suppression of host immune responses and suppression of host gene expression. The RNA-dependent RNA polymerase is a target of antiviral therapies. |
Literature information:
| Pubmed ID | 28843094 |
| Clinical information | No |
| Disease | - |
| Published year | 2017 |
| Journal | Virology |
| Title | MERS coronavirus nsp1 participates in an efficient propagation through a specific interaction with viral RNA |
| Author | Yutaka Terada,Kengo Kawachi,Yoshiharu Matsuura,Wataru Kamitani |
| Evidence | Although the activity of translational shutoff of nsp1-R13A mutant was a little weaker than that of nsp1-wt (Fig. 4E), these data indicated that R13A mutation made nsp1 critically lost its activity to bind with 5-UTR but retained translational shutoff act |