points (1) and (2) below: general context. points (3)-(6) show role of recombinant viral S protein that is sold online, a subtle but crucial (I believe) contrast to role of naturally occurring viral S protein. point (7) is a new study. -r, mt. shasta
(1) 4-3-20 Between Dec. 27, 2019, and Jan. 5, 2020, five firms and institutions detected a SARS-like coronavirus that caused pneumonia among people in Wuhan….on Jan. 1, Hubei province health authorities oddly ordered the company that first sequenced the virus to stop testing, destroy all samples and keep information secret. Two days later central health authorities issued a similar official order to testing facilities across the country. https://thehill.com/opinion/international/490258-what-did-chinas-xi-jinping-know-and-when-did-he-know-it
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(2) 3-26-20 Another variant of the flu is H5N1. It is an avian flu with a human mortality rate of 60 percent. To understand this flu variant, researchers went to work to decode its secrets. They then produced their own variant by passing the flu from mammal to mammal—ferrets to be exact—by adjusting the virus’s ability to attach to a ferret lung cell receptor. This altered the variant to make it airborne. In fear of it falling into the wrong hands, the U.S. government shut down the study and testing. As journalist Carl Zimmer explained, the Frankenstein test-tube H5N1 “could make the deadly 1918 pandemic look like a pesky cold.”…
In 2015 the University of North Carolina reported that it had manipulated the original sars virus protein gene to attach more readily and infect human cells through mice….This new test-tube coronavirus was a more intelligent, mutated version of Sars with a greater potential for infection due to certain design features in the “spokes” of the virus to bind to human cells. As Nature explained in November 2015, this new variant was “made up of a surface protein of shc014 and the backbone of a Sars virus that had been adapted to grow in mice and to mimic human disease. The chimaera infected human airway cells—proving that the surface protein of shc014 has the necessary structure to bind to a key receptor on the cells and to infect them” (emphasis added)….One of the prime researchers involved in the University of North Carolina “breakthrough” was Zheng-li Shi, who works at the Wuhan Institute of Virology….Zheng-li’s colleague, Xing-Yi Ge, also works at the Wuhan Institute of Virology. In 2013, he isolated the Sars virus in bats and adjusted it to make it more receptive to human transmission through a certain human cell receptor. https://www.thetrumpet.com/22131-chinas-test-tube-pandemic
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(3) Virol Sin. 2018 Feb; 33(1): 104–107.
Published online 2018 Mar 2 -team included Peter Daszak,4 and Zheng-Li Shi1
We conducted a virus neutralization test for the six positive samples targeting two SARSr-CoVs, WIV1 and WIV16 (Ge et al. 2013; Yang et al. 2016). None of them were able to neutralize either virus. These sera also failed to react by Western blot with any of the recombinant RBD proteins from SARS-CoV or the three bat SARSr-CoVs Rp3, WIV1, and SHC014. We also performed viral nucleic acid detection in oral and fecal swabs and blood cells, and none of these were positive….
Our study provides the first serological evidence of likely human infection by bat SARSr-CoVs or, potentially, related viruses. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6178078/
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(4) Cellular & Molecular Immunology (2020) A coronavirus contains four structural proteins, including spike (S), envelope (E), membrane (M), and nucleocapsid (N) proteins.2,10,11 Among them, S protein plays the most important roles in viral attachment, fusion and entry, and it serves as a target for development of antibodies, entry inhibitors and vaccines.1,12,13,14,15,16,17
The S protein mediates viral entry into host cells by first binding to a host receptor through the receptor-binding domain (RBD) in the S1 subunit and then fusing the viral and host membranes through the S2 subunit.16,18,19 SARS-CoV and MERS-CoV RBDs recognize different receptors. SARS-CoV recognizes angiotensin-converting enzyme 2 (ACE2) as its receptor, whereas MERS-CoV recognizes dipeptidyl peptidase 4 (DPP4) as its receptor.20,21 Similar to SARS-CoV, SARS-CoV-2 also recognizes ACE2 as its host receptor binding to viral S protein.22 Therefore it is critical to define the RBD in SARS-CoV-2 S protein as the most likely target for the development of virus attachment inhibitors, neutralizing antibodies, and vaccines. https://www.nature.com/articles/s41423-020-0400-4
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(5) The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. It's been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD) which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity. https://www.abeomics.com/recombinant-2019-ncov-s-protein-rbd-sd1-c-mfc-active
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(6) Virology Journal, 2010: Expression of recombinant RBD proteins
The RBD-His (RBD sequence with a His-tag) and RBD-Fc (RBD fused with human IgG-Fc) proteins were respectively expressed and purified as described previously [16, 23]. In brief, the plasmid encoding RBD-His or RBD-Fc was transfected into HEK293T cells using Lipofectamine 2000 (Invitrogen, Carlsbad, CA) according to the manufacturer's protocols. Culture medium was replaced by fresh OPTI-MEM I Reduced-Serum Medium 12 h post-transfection and the supernatants containing expressing RBD proteins were collected 72 h later. RBD-His was purified by Nickel affinity column (Qiagen), while RBD-Fc was purified by protein A-Sepharose 4 Fast Flow (Amersham Biosciences, Piscataway, NJ).
https://virologyj.biomedcentral.com/articles/10.1186/1743-422X-7-299
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(7) 5-8-20 We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the “up” conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2. https://science.sciencemag.org/content/368/6491/630
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November 10, 2015 Source: University of North Carolina at Chapel Hill
Summary: A new bat SARS-like virus has been discovered that can jump directly from its bat hosts to humans without mutation.
reference: team included Xing-Yi Ge, Zhengli-Li Shi, Ralph S Baric. A SARS-like cluster of circulating bat coronaviruses shows potential for human emergence. Nature Medicine, 2015 https://www.sciencedaily.com/releases/2015/11/151110115711.htm
……………………………………more importantly: https://www.naturalnews.com/2020-05-08-virologists-lying-origins-coronavirus-contains-gain-of-function-gene-sequences.html
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