Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C1175175 (SARS)
 19,188 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The open reading frame 3 (ORF3) of the severe acute respiratory syndrome coronavirus (SARS-CoV) genome encodes a predicted 154-amino acid protein, which lacks similarities to any known protein, and is named 3b. In this study, it was shown that 3b protein was predominately localized to nucleus with EGFP tag at its N- or C-terminus. The localization patterns were similar in different transfected cells. Immuno-fluorescence assay revealed that 3b protein was co-localized well with C23 in nucleolus. C23, B23 and fibrillarin all are important nucleolar proteins, which localize in the region of the nucleolus. Co-transfection of p3b-EGFP with pC23-DsRed, pB23-DsRed and pfibrillarin-DsRed further confirmed 3b's nucleolus localization. With construction of serial truncated mutants of 3b, a region (residues 134-154 aa) responsible for nucleolar localization was determinated in 3b protein. These results provide a new insight for further functional studies of SARS-CoV 3b protein.
 ...
PMID:Nucleolar localization of non-structural protein 3b, a protein specifically encoded by the severe acute respiratory syndrome coronavirus. 1604 44

Severe acute respiratory syndrome coronavirus nonstructural protein 1 (nsp1) is a key factor in virus-induced down-regulation of host gene expression. In infected cells, nsp1 engages in a multipronged mechanism to inhibit host gene expression by binding to the 40S ribosome to block the assembly of translationally competent ribosome, and then inducing endonucleolytic cleavage and the degradation of host mRNAs. Here, we report a previously undetected mechanism by which nsp1 exploits the nuclear pore complex and disrupts the nuclear-cytoplasmic transport of biomolecules. We identified members of the nuclear pore complex from the nsp1-associated protein assembly and found that the expression of nsp1 in HEK cells disrupts Nup93 localization around the nuclear envelope without triggering proteolytic degradation, while the nuclear lamina remains unperturbed. Consistent with its role in host shutoff, nsp1 alters the nuclear-cytoplasmic distribution of an RNA binding protein, nucleolin. Our results suggest that nsp1, alone, can regulate multiple steps of gene expression including nuclear-cytoplasmic transport.
 ...
PMID:SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex. 3094 71