End of 2020: SARS-CoV-2 important research results interpretation!

uses the SARS-CoV-2 strain Wuhan-1 (GenBank: MN908947) as a template, and the authors selected three sets of natural variants and glycosylated mutants to build the prosthetic virus.
as shown in Figure 1, Group A represents all high-frequency variants of the entire S gene (29 strains) except the subject binding domain (RBD) region and a combination variant with D614G.
group B includes variants (51 strains) that appear in RBD.
although the eight single-point mutations in Group A and Group B, namely Q239K, V341I, A435S, K458R, I472V, H519P, A831V and S943T, do not exist, they are found to be combined with D614G.
, fake viruses were constructed for these eight single-point mutations to compare them with those built for their two-bit combination mutation with D614G.
C group consists of 26 mutants with amino acid changes at presumed glycosylation points (22 bits), including variants (N74K, N149H, and T719A) and experimental mutants constructed by these authors to analyze the effects on glycosylation.
specifically, 22 single-point mutants were constructed in the lab for all 22 bits (N to Q);
, they have built 106 fake viruses, 80 natural variants and 26 glycosylated mutants.
: Building a more stable SARS-CoV-2 hedgehog protein to help accelerate COVID-19 vaccine development doi:10.1126/science.abd0826 for rapid development In a new study, researchers at the University of Texas at Austin have successfully redesigned a key protein in the new coronavirus SARS-CoV-2, a makeover that could allow the world to produce vaccines faster and more steadily.
study was published in the journal Science.
most coronavirus candidates train the human immune system to recognize a key protein on the surface of the SARS-CoV-2 virus, the prickly protein (S), to fight infection.
the authors designed a new version of the protein, which, when expressed in cells, produces 10 times as many proteins as the synthetic prickly proteins previously used in a variety of COVID-19 vaccines.
also worked with colleagues at the National Institutes of Health to design earlier versions of the python protein found in at least two COVID-19 candidate vaccines currently in clinical trials in the United States.
image Source: The Francis Crick Institute 6 Nature: Revealing the structural mechanism of SARS-CoV-2 hedgehog protein binding human ACE2 receptor doi:10.1038/s41586-020-2772-0 In a new study, researchers from the Francis-Crick Institute in the United Kingdom found that the prickly protein (S protein) on the surface of the SARS-CoV-2 coronavirus can take at least ten different structural states when in contact with the human virus subject ACE2.
new insights into the mechanisms of infection lay the foundation for the development of vaccines and treatments.
the findings were published in the journal Nature.
as a coronavirus that causes covid-19, SARS-CoV-2 has an surface covered with S protein, which allows the virus to infect human cells.
infection begins when the S protein binds to the cell surface bind, ACE2, and the virus genome is released into the cell at a later stage.
, the exact nature of the S protein binding between ACE2 and SARS-CoV-2 is still unknown.
the first study to examine the binding mechanism between ACE2 and S proteins, the researchers characterization of 10 different structures associated with the different stages of S protein binding and infection.
first incubated a mixture of S protein and ACE2, and then captured different forms of S protein by quickly freezing in liquid ethane.
used cryogenic electroscopy to examine the protein samples and obtained tens of thousands of high-resolution images of different binding stages.
: The Lancet: New Discoveries! The loss of 382 nucleotides may make SARS-CoV-2 infections milder! doi:10.1016/S0140-6736 (20) 31757-8 In a recent study published in the international journal The Lancet, scientists from the Singapore Science and Technology Research Agency (A-STAR) and others found genetic mutations that make the SARS-CoV-2 virus mild.
Like any other living thing on Earth, SARS-CoV-2 tends to be prone to natural genetic diversity because of mutations that have been a source of concern since the SARS-CoV-2-induced COVID-19 outbreak swept the world. Contagious and lethal, however, the researchers found the opposite results in this study, in which they analyzed a particular mutation that makes SARS-CoV-2 less pathogenic, resulting in a lower immune response, less infectious infection, and better clinical outcomes for infected people.
Previously, researchers have found mutations in the SARS-CoV-2 genome because such genetic mutations can be translated into different characteristics that affect viruses in different ways, so researchers are interested in studying these mutations and their effects; for example, mutations in areas where immune targets or viruses can be diagnosed for testing may have some serious effects on human hosts against viruses, and genetic mutations can also cause concern about the spread and toxicity of viruses.
study, researchers focused on a specific genetic mutation that researchers found during routine sequencing of the genome of SARS-CoV-2 isolated from cases in Singapore between January and February this year.
-8 Cell: Analysis of the structure and function of the SARS-CoV-2 hedgehog protein variant D614G doi:10.1016/j.cell.2020.20. 09.032 In a new study, researchers from the University of Massachusetts School of Medicine and others in the United States found that D614G is more infectious than its ancestor virus in human lung cells, colon cells, and ACE2 ogenesis that express human ACE2 through heterogeneity or from a variety of mammals, including Chinese chrysanthemum bats and Malay armor.
study was published in the Cell journal.