Following major achievements in the study of the mechanism of cross-species transmission of influenza virus, and after the publication of "Science" and "The Lancet", Gao Fu's research group of the Institute of Microbiology, Chinese Academy of Sciences has made important progress in the study of the mechanism of new coronavirus invasion into host cells .

The new coronavirus, also known as the Middle East Respiratory Syndrome coronavirus (MERS-CoV), is another highly pathogenic coronavirus after SARS-CoV. Similar to SARS, patients with MERS-CoV infection may develop fever, cough, and acute respiratory distress syndrome, sometimes with renal failure, and the mortality rate is very high. Since the first report in September 2012, as of July 5, 2013, a total of 79 cases of MERS-CoV virus infection laboratory-confirmed cases have been notified to WHO worldwide, of which 42 have died. To date, laboratory confirmed cases have been reported in Jordan, Qatar, Saudi Arabia, the United Arab Emirates, France, Germany, Italy, Tunisia and the United Kingdom; limited local transmission has also occurred in France, Italy, Tunisia and the United Kingdom. For a time, MERS-CoV's high case fatality rate, human-to-human ability, and the trend of spreading to other countries have attracted attention and concern from all parties. Therefore, it is very important to understand the mechanism of MERS-CoV invasion into host cells.

MERS-CoV and SARS-CoV belong to the Coronaviridae family, Beta Coronavirus is a positive-strand RNA virus with a capsule. The viral envelope contains spike proteins (sp, S), which mediate the binding of the virus to host-specific receptor molecules, and are the most important molecule to initiate viral infection. Recent studies have shown that dipeptidyl peptidase-4 (DPPeptidyl peptidase 4, DPPIV / CD26) is the receptor for MERS-CoV in host cells. Identifying the binding mode of MERS-CoV S protein and CD26 is of great significance for the study of the MERS-CoV virus invasion mechanism and the discovery of effective drug targets. The Gaofu research group has long been devoted to the study of the transspecies transmission mechanism and immune molecular recognition of enveloped viruses. For the newly discovered virus receptor molecules, it has rapidly carried out functional studies on the structure and interaction of the complex.

Researchers Lu Guangwen, Hu Yawei, Wang Qihui, Qi Jianxun, Gao Feng and other researchers first identified the part of the S protein responsible for binding to CD26, that is, the receptor binding domain of MERS (MERS-RBD); MERS-RBD and protein complexes with CD26, and obtained high-quality crystals; finally resolved the molecular structure of MERS-RBD monomers and ligand / receptor complexes. MERS-RBD is composed of a core region and an external receptor recognition region (see Figure a). The core region structure is homologous to the spike molecules of SARS-CoV, while the external receptor recognition region appears as a unique composition of β-sheet The structural unit recognizes the IV and V paddles in the “β-propeller” -like structure of the CD26 molecule. CD26 belongs to type II transmembrane protein, which exists on the cell membrane as a dimer. MERS-RBD binds to the distal membrane end of CD26, forming a U-shaped molecular structure (Figure b). In the process of recognition of receptors by viral ligands, the hydrogen bonds formed by side chain groups interact with hydrophilic interactions such as salt bridges. The details of these interactions at the molecular level provide an important reference for the design of small molecule drugs that target viral invasion.

The potential threat of MERS-CoV to public health security urgently needs specific and highly effective anti-MERS-CoV virus drugs. It is one of the most effective anti-virus means to block the combination and intrusion of viruses and prevent them from happening. The research team's research results on the combination mode of MERS-RBD and CD26 have important guiding significance for the design of drugs against MERS-CoV virus.

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