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....like a live animal, perhaps? Cheap, self-replicating with just enough variability to be a useful test, and a very good model of a live animal.
Something safe for tardigrades may not be safe for humans.
Quote from: hamdani yusuf on 05/08/2021 11:10:01Something safe for tardigrades may not be safe for humans.Yes, and of course.Something safe for organoids may not be safe for humans.So, as Alan said, there's not much point testing vaccines on them, is there?
When the uncertainty is high, such as in early stages, simpler systems can be used for test. If it's promising, then increase the complexity step by step to resemble a more complete human body.
No point in putting your head in the sand like the Kiwis and Aussies are doing!!
Isolation can not work in the long term..
Preferably those with similar physiology as humans.
We were slow in issuing the vaccine
Quote from: hamdani yusuf on 05/08/2021 11:10:01Preferably those with similar physiology as humans.Like a human, for instance? There wouldn't be much point in testing an anti-zoonotic vaccine on a mammal that tolerates the zoonosis. Thalidomide was deemed safe after testing on rabbits.
Quote from: hamdani yusuf on 05/08/2021 13:09:06When the uncertainty is high, such as in early stages, simpler systems can be used for test. If it's promising, then increase the complexity step by step to resemble a more complete human body.What do you think they currently do?Do you not think they worked that out already?
there's not much point testing vaccines on them, is there?
By Max Planck Institute August 4, 2021Coronavirus Nanobodies AlpacasThe figure shows how two of the newly developed nanobodies (blue and magenta) bind to the receptor-binding domain (green) of the coronavirus spike protein (grey), thus preventing infection with Sars-CoV-2 and its variants. The nanobodies originate from alpacas and are smaller and simpler than conventional antibodies. Credit: Max Planck Institute for Biophysical ChemistryGöttingen researchers have developed mini-antibodies that efficiently block the coronavirus SARS-CoV-2 and its dangerous new variants. These so-called nanobodies bind and neutralize the virus up to 1000 times better than previously developed mini-antibodies. In addition, the scientists optimized their mini-antibodies for stability and resistance to extreme heat. This unique combination makes them promising agents to treat COVID-19. Since nanobodies can be produced at low costs in large quantities, they could meet the global demand for COVID-19 therapeutics. The new nanobodies are currently in preparation for clinical trials.Antibodies help our immune system to fend off pathogens. For example, the molecules attach to viruses and neutralize them so that they can no longer infect cells. Antibodies can also be produced industrially and administered to acutely ill patients. They then act like drugs, relieving symptoms and shortening recovery from the disease. This is established practice for treating hepatitis B and rabies. Antibodies are also used for treating COVID-19 patients. However, producing these molecules on an industrial scale is too complex and expensive to meet worldwide demand. Nanobodies could solve this problem.Scientists at the Max Planck Institute (MPI) for Biophysical Chemistry in Göttingen (Germany) and the University Medical Center Göttingen (UMG) have now developed mini-antibodies (also known as VHH antibodies or nanobodies) that unite all the properties required for a potent drug against COVID-19. “For the first time, they combine extreme stability and outstanding efficacy against the virus and its Alpha, Beta, Gamma, and Delta mutants,” emphasizes Dirk Görlich, director at the MPI for Biophysical Chemistry.At first glance, the new nanobodies hardly differ from anti-SARS-CoV-2 nanobodies developed by other labs. They are all directed against a crucial part of the coronavirus spikes, the receptor-binding domain that the virus deploys for invading host cells. The nanobodies block this binding domain and thereby prevent the virus from infecting cells.“Our nanobodies can withstand temperatures of up to 95 °C without losing their function or forming aggregates,” explains Matthias Dobbelstein, professor and director of the UMG’s Institute of Molecular Oncology. “For one thing, this tells us that they might remain active in the body long enough to be effective. For another, heat-resistant nanobodies are easier to produce, process, and store.”Single, double, and triple nanobodiesThe simplest mini-antibodies developed by the Göttingen team already bind up to 1000 times more strongly to the spike protein than previously reported nanobodies. They also bind very well to the mutated receptor-binding domains of the Alpha, Beta, Gamma, and Delta strains. “Our single nanobodies are potentially suitable for inhalation and thus for direct virus neutralization in the respiratory tract,” Dobbelstein says. “In addition, because they are very small, they could readily penetrate tissues and prevent the virus from spreading further at the site of infection.”A ‘nanobody triad’ further improves binding: The researchers bundled three identical nanobodies according to the symmetry of the spike protein, which is comprised of three identical building blocks with three binding domains. “With the nanobody triad, we literally join forces: In an ideal scenario, each of the three nanobodies attaches to one of the three binding domains,” reports Thomas Güttler, a scientist in Görlich’s team. “This creates a virtually irreversible bond. The triple will not let release the spike protein and neutralizes the virus even up to 30,000-fold better than the single nanobodies.” Another advantage: The larger size of the nanobody triad expectedly delays renal excretion. This keeps them in the body for longer and promises a longer-lasting therapeutic effect.As a third design, the scientists produced tandems. These combine two nanobodies that target different parts of the receptor-binding domain and together can bind the spike protein. “Such tandems are extremely resistant to virus mutations and the resulting ‘immune escape’ because they bind the viral spike so strongly”, explains Metin Aksu, a researcher in Görlich’s team.For all nanobody variants – monomeric, double as well as triple – the researchers found that very small amounts are sufficient to stop the pathogen. If used as a drug, this would allow for a low dosage and thus for fewer side effects and lower production costs.
we are already 90% vaccinated and herd immune to Covid
What's gone wrong with the world in the face of COVID?
This is causing many sportsmen in particular to miss fixtures unnecessarily.
everyone is infectious anyway and is carrying the virus