Signal Transduct Target Ther: A team of professors at Shandong University has clarified the subcellular positioning of 28 new coronavirus proteins

New Coronary Pneumonia (COVID-19), caused by SARS-CoV-2 infection, remains a global pandemic, infecting more than 55.62 million people as of November 18, 2020, with a cumulative death toll of more than 1.33 million, seriously endangering human health and creating an unprecedented threat to public health safety and economic development.
the new coronavirus genome encodes about 29 proteins, and understanding the subcellular positioning of these proteins is not only an important inspiration for understanding the interaction between the new coronavirus and host cells, but also provides clues to the development of antiviral drugs.
November 17, 2020, Professor Wang Pei association of Shandong University's Institute of Advanced Medicine and Professor Tang Qiyi of Howard University School of Medicine in the United States, co-authored a research paper entitled: A systemic and molecular research of the journal Signal Transduction and Targeted Therapy in the journal Nature.
the study used methods such as immunofluorescence to elucidate the subcellular positioning of 28 new coronavirus proteins in addition to NSP11 proteins (only 14 amino acids).
results show that most of the new coronavirus proteins are located in the cytokine, some of the new coronavirus proteins have both cytokine and nucleal positioning, and 4 new coronavirus proteins M, NSP15, ORF6, ORF7a detected in Golgi appara ORF3a is located in endosome and lysosome, NSP6, ORF7b, ORF8, and ORF10 are located in endoplasmic reticulum.
considering that M proteins are not the only Golki body-based proteins, other viral proteins other than M proteins such as NSP15, ORF6, and ORF7a may also be involved in the maturation of structural proteins E and S.
ORF3a is co-located with endosome protein Rab5, recycled endosome Rab11, protein Rab7 involved in early endosome transport to late endosomes, and lysosome protein Lamp1, indicating that ORF3a is involved in the endosome and lysosome fusion endosome fusion, so ORF3a may be involved in the self-removal of toxic substances in cells and promote SARS-CoV-2 replication.
this study provides an important basis for understanding the function of the new coronavirus protein and the development of antiviral drugs.
Wang Pei, of Shandong University's Institute of Advanced Medicine, and Tang Qiyi, of Howard University School of Medicine in the United States, co-authored the paper.
Jing Zhang, a 2020 doctoral student at the Institute of Advanced Medicine, and Ruth Cruz-cosme of Howard University School of Medicine were co-authors of the paper, with Shandong University as the first completion unit.
the study was supported by Shandong University's New Crown Pneumonia Emergency Research Project (2020XGB03, P.-H.W) and NIH R01 (Q.T.) in the United States.