ArticleJournal of virology2002
Membrane association and dimerization of a cysteine-rich, 16-kilodalton polypeptide released from the C-terminal region of the coronavirus infectious bronchitis virus 1a polyprotein.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Structural view and substrate specificity of papain-like protease from avian infectious bronchitis virus.The Journal of biological chemistry · 2015Article
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- Binding of the 5'-untranslated region of coronavirus RNA to zinc finger CCHC-type and RNA-binding motif 1 enhances viral replication and transcription.Nucleic acids research · 2012Article
- The cellular RNA helicase DDX1 interacts with coronavirus nonstructural protein 14 and enhances viral replication.Journal of virology · 2010Article
- Functional and genetic studies of the substrate specificity of coronavirus infectious bronchitis virus 3C-like proteinase.Journal of virology · 2010Article
- Inhibition of protein kinase R activation and upregulation of GADD34 expression play a synergistic role in facilitating coronavirus replication by maintaining de novo protein synthesis in virus-infected cells.Journal of virology · 2009Article
- Towards construction of viral vectors based on avian coronavirus infectious bronchitis virus for gene delivery and vaccine development.Journal of virological methods · 2009Article
- Article
- Article
- Identification of sequence changes responsible for the attenuation of avian infectious bronchitis virus strain Arkansas DPI.Archives of virology · 2009Article
- Article
- Analysis of murine hepatitis virus strain A59 temperature-sensitive mutant TS-LA6 suggests that nsp10 plays a critical role in polyprotein processing.Journal of virology · 2007Article
- Murine hepatitis virus replicase protein nsp10 is a critical regulator of viral RNA synthesis.Journal of virology · 2007Article
- Article
- The non-structural protein Nsp10 of mouse hepatitis virus binds zinc ions and nucleic acids.FEBS letters · 2006Article
- Mutational analysis of MHV-A59 replicase protein-nsp10.Advances in experimental medicine and biology · 2006Article
- Infectious bronchitis virus 3a protein localizes to a novel domain of the smooth endoplasmic reticulum.Journal of virology · 2005Article
- The coronavirus replicase.Current topics in microbiology and immunology · 2005Review
- Development of mouse hepatitis virus and SARS-CoV infectious cDNA constructs.Current topics in microbiology and immunology · 2005Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
More than 10 mature proteins processed from coronavirus gene 1-encoded polyproteins have been identified in virus-infected cells. Here, we report the identification of the most C-terminal cleavage product of the 1a polyprotein as a 16-kDa protein in infectious bronchitis virus-infected Vero cells. Indirect immunofluorescence demonstrated that the protein exhibits a distinct perinuclear punctate staining pattern, suggesting that it is associated with cellular membranes. Positive staining observed on nonpermeabilized cells indicates that the protein may get transported to the cell surface, but no secretion of the protein out of the cells was observed. Treatment of the membrane fraction prepared from cells expressing the 16-kDa protein with Triton X-100, a high pH, and a high concentration of salts showed that the protein may be tightly associated with intracellular membranes. Dual-labeling experiments demonstrated that the 16-kDa protein colocalized with the 5'-bromouridine 5'-triphosphate-labeled viral RNA, suggesting that it may be associated with the viral replication machinery. Sequence comparison of the 16-kDa protein with the equivalent products of other coronaviruses showed multiple conserved cysteine residues, and site-directed mutagenesis studies revealed that these conserved residues may contribute to dimerization of the 16-kDa protein. Furthermore, increased accumulation of the 16-kDa protein upon stimulation with epidermal growth factor was observed, providing preliminary evidence that the protein might be involved in the growth factor signaling pathway.
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