On August 7, 2020, Chinese scientists published three Science papers in the same period.

!-- ewebeditor:page title"--August 9, 2020 //--- Another issue of the new Science Journal (August 7, 2020) is published this week. Let the little editor come with you.
images from the Science Journal.
1.Science: Revealing that proteases control the cell division mechanisms of ancient bacteria doi: 10.1126/science.aaz2532 eunuclear organisms are most likely produced by a symbiotic partnership between the paleoacteria host and alpha-deformed bacillus, which produces cell bodies and mitochondria, respectively.
is why some of the proteins that control key events in the ethon cell division cycle originate from ancient bacteria.
this includes the ESCRT-III protein, which catalyzes the final step of cell division in many genel organisms, as well as in the ancient bacteria Sulfolobus acidocaldarius.
However, so far, no quascular bacteria have been found to have the same origins as cytocytocytokines such as periodic protein-dependent kinases and periodic proteins, which enable cell cycle events to occur in an orderly manner in all gyrogenes.
Therefore, it remains unclear how key events in the cell cycle of ancient bacteria, including cell division, are regulated, with the exception of the 20S protease, which is conservative between paleontocyms and gyrogens and regulates the cell cycle of ethons by degrading the cycle proteins."
To explore the function of 20S proteases in acidophilic hot vulcanized leaf bacteria, researchers from University College London, the University of Cambridge, the Francis Crick Institute, Lancaster University and Stockholm University in Sweden analyzed its three-dimensional structure using crystallographic methods and biochemically analyzed its activity when it was inhibited and not inhibited outside the body.
study was published in the August 7, 2020 issue of the journal Science, entitled "The proteasome controls ESCRT-III-mediated division cell in an archaeon".
2.Science: New methods can be used faster and cheaper to synthesize nucleoside analogants for viral infections and cancer dooi: 10.1126/science.abb3231; doi:10.1126/science.abd1283 Over the past 50 years, scientists have developed drugs using artificial, synthetic nucleoside analogants for the treatment of diseases involving cell division and/or infection of the virus.
these diseases include hepatitis, herpes simplex, HIV and cancer.
, however, professor Robert Britton, a chemist at Simon Fraser University in Canada, said, "The process is intensive and challenging, limiting and preventing the discovery of new drug therapies."
now, in a new study, Britton and his team can build new nucleoside analogies months ahead of previous methods, paving the way for faster drug discovery.
it would also make it faster and cheaper to discover antiviral and cancer drugs.
the findings, published in the August 7, 2020 issue of science, is entitled "A short de novo synthesis of nucleoside analogs". Professor
Britton said, "The reduction in synthesis time and cost will vary depending on the specific nucleoside analogy, but we have examples of reducing the synthesis step, which typically takes at least a few months to complete, to three or four steps, which will take only about a week."
is clearly a key factor in the treatment of newly evolved viruses such as SARS-CoV-2, a new coronavirus that causes COVID-19 disease.
"3.Science: Using powerful medium and antibodies from COVID-19 patients to identify multiple vulnerable targets of the new coronary virus doi: 10.1126/science.abc5902 In a new study, from the Netherlands Researchers at the University of Amsterdam, Erasmus Medical Center, the Scripps Institute in the United States and Cornell University's Weir School of Medicine isolated 18 medium antibodies (NAbs) from three patients recovering from a stable fusion of pre-sting proteins from SARS-CoV-2.
study was published online June 15, 2020 in the journal Science, entitled "Potent neutralizing antibodies from COVID-19 patients define multiple targets of the company."
these antibodies have low-level somatic hypermutation and show strong abundence in the use of VH1-69, VH3-30-3, and VH1-24 genes.
a small portion of these antibodies are effective in suppressing real SARS-CoV-2 infections as low as 0.007 ?g/mL.
competition and electroscopic studies show that the SARS-CoV-2 S protein contains several different antigen sites, including multiple recepor binding domain (RBD) and non-RBD positions.
as guidance for vaccine design, these antibodies are promising candidates for COVID-19 treatment and prevention.
these 18 targeted S proteins have different antigen bits, two of which have skin molar-intrinsic activity (IC50 is 0.007 and 0.009 ?g/mL, or 47 and 60pM, respectively) for real SARS-CoV-2 viruses.
4.Science: Our scientists have found that the N-end domain doi: 10.1126/science.abc6952 trinity tyrogens (S proteins) that bind to SARS-CoV-2 tyrogens in human and antibodies play a key role in the virus's entry.
,S(TMPRSS2)NS1CS2,。
S1 and S2 consist of an extracellulate domain (ECD, 1-1208 amino acids) and a single trans-membrane spiral, respectively, mediated receptacle binding and membrane fusion.
S1 consists of an N-side domain (NTD) and a receptor-combined domain (RBD), which is critical to determining the organization's addiction and hosting range.
RBD is responsible for combining with ACE2, and the function of NTD is not yet clear.
in some coronaviruses, NTD may identify specific glyco groups at initial attachment and may play an important role in the transition of S proteins from pre-fusion to post-fusion states.
NTD of the MERS-CoV S protein can be used as a key ethon for the medium antibody.
!--/ewebeditor:page-!--ewebeditor:page title"--monoclonal antibodies (mAbs) with strong and active target SARS-CoV-2 S proteins are a focus of the development of COVID-19 therapeutic interventions.
many studies have reported on the function and structure of SARS-CoV-2, which targets RBD and inhibits the binding of S proteins to ACE2.
use of a single RBD-targeted antibody may induce coronaviruses to produce resistant mutations.
targeting non-RBD ethnotes may be added to antibody combination therapy for SARS-CoV-2.
not only is the ethnopedic distribution on the RBD of the S protein, but also the ethnopedic distribution on the entire S protein can be used to guide the development of therapeutic drugs that target SARS-CoV-2.
a new study, researchers from the Chinese Academy of Military Medical Sciences, Westlake University and Tsinghua University isolated and described mAb from 10 patients with COVID-19 during rehabilitation.
study was published online June 22, 2020 in the journal Science under the title "A neutralizing human antibody binds to the N-terminal domain of the Spike of SARS-CoV-2".
the three mAbs they separated showed a medium activity to the real SARS-CoV-2.
a type of mAb called 4A8 has higher mid-level effects on real SARS-CoV-2 and SARS-CoV-2 fake viruses, but does not bind to RBD.
They analyzed the low-temperature electromirn structure with an overall resolution of 3.1 E when combined with the S protein and a low-temperature electron mirror structure with a local resolution of 3.3 E for the 4A8-NTD interface, thus determining that the eplugency of 4A8 was NTD of the S protein.
this suggests that NTD is a promising target for therapeutic mAb of COVID-19.
5.Science: Human monoclonal antibodies from recovering SRAS patients can be cross-neutralated and SARS-like coronavirus doi: 10.1126/science.abc7424 There is an urgent need for a broad protective vaccine against known and unseated human coronavirus (HCoV).
To gain a deeper understanding of cross-neutral and antibody responses, in a new study, U.S. researchers analyzed the memory B cell bank of a recovering SRAS provider and found 200 SARS-CoV-2 binding antibodies that targeted multiple conservative sites on the surface of the S protein.
study was published online June 15, 2020 in the journal Science, entitled "Broad Neutralization SARS-Relatedes by Human Monoclonal Antibodies".
A large proportion of these non-mediated antibodies show high levels of high-frequency mutations in sotic cells and cross-react with HCoV, which is transmitted in humans, reminiscent of the prior presence of memory B cells caused by HCoV infections.
several antibodies effectively cross-centar SARS-CoV, SARS-CoV-2, and BAT SARS-like coronavirus WIVE1 by blocking receptor attachment and inducing S1 sub-base shedding.
these antibodies provide promising drug candidates for therapeutic interventions and provide a target for the rational design of a pan-sarbecovirus virus vaccine.
These powerful cross-centring and antibody binding conservative ethos overlap with the hACE2 binding bit, which reveals that this antigen surface is a promising target for the rational design of a pan-sarbecovirus virus vaccine.
, for example, the RBD ethes determined by these antibodies can be presented on a stable protein stent, thus concentrating the antibody response at this point.
Moremore, these human antibodies, whether used alone or in combination, represent promising candidate drugs that can be used to prevent or treat SARS, COVID-19, and potential future diseases of the emerging SARS-like coronavirus.
6.Science: Is interferon IFN-19 beneficial or harmful? New research has found that it destroys the surface barrier of the lungs after identifying the virus: 10.1126/science.abc3545; doi:10.1126/science.abd2208 Interferon and other cytokines produced by the immune system are important defenses against viral infections, but as we have seen in COVID-19, they can also cause damaging, potentially life-threatening lung inflammation.
recent evidence suggests that an interferon called type III interferon, or interferon xenon (IFN-xenon), can fight viral infections while limiting this inflammatory damage.
lead to clinical trials to test whether type III interferon can be used to treat COVID-19.
, however, in a new study, researchers from Italy and the United States provide evidence that type III interferon increases the risk of life-threatening bacterial "super-infection" in the lungs.
can occur in both influenza and COVID-19.
the researchers warned that giving type III interferon later in the COVID-19 course could do more harm than good.
study was published online June 11, 2020 in the journal Science, with the headline "Type III interferons disrupt the lung epithelial barrier upon viral recognition".
"Our data suggest that SARS-CoV-2 inhibits the production of interferon in the upper respiratory tract, weakens the immune response, and helps the coronavirus survive," said Dr. Ivan Zanoni, an immunologist at Boston Children's Hospital and author of the paper.
, however, when the coronavirus reaches the lower respiratory tract, there is a strong immune response, including an increase in type III interferon, which we consider harmful.
" !--/ewebeditor:page-!--ewebeditor:page title"-Science: Interferon-assisting in the fight against viral infections can also hinder the repair of lung damage doi: 10.1126/science.abc2061; doi:10.1126/scienc.