According to the British "New Scientist" weekly website reported on January 19, by analyzing high-resolution images, the computer can quickly predict the sequence of amino acids in antibodies. This could reduce the time required to monitor antibody responses during vaccine development by several months.
Andrew Ward of the Scripps Institute in California, USA, said: "This provides a shortcut to a process that typically takes months to complete with existing tools and techniques. ”
Antigens, such as the spike protein of the new coronavirus, are a key component of vaccines. Antigens cause the immune system to produce a series of antibodies against them, but in terms of immune response, some of these antibodies act more than others.
Analyzing the ratio of "targeted" useful antibodies to less useful antibodies "off target" produced by vaccination can help us optimize the vaccine so that the immune response is tilted in the direction of producing more protective antibodies, Ward said.
However, this work takes time. Dna sequencing of individual B cells that produce antibodies is usually sequenced, antibodies are generated based on these sequences, and then the structure of these antibodies is imaged to predict where they bind to the antigen.
Ward and colleagues have now developed a faster approach. They used cryo-electron microscopy to image the structure of the frozen antibody and designed a computer algorithm that can quickly predict the amino acid sequence based on the antibody structure.
The report also pointed out that to test their method, the researchers inoculated rhesus monkeys with HIV antigens, so that the monkeys produced antibodies. They then drew blood from two monkeys and mixed each sample with hive antigen overnight.
The next day, they performed batch imaging of the antibody-bound antigens in each sample to create a detailed map. The map shows the structure of the different antibodies in the sample and how they bind to the antigen.
The researchers then focused on one antibody in each monkey and used computer algorithms to compare the antibody structure to a known library of antibody sequences in monkeys, so they could find the existing sequence that best matched that structure.
They also made antibodies based on predicted sequences and confirmed that the antibody structures matched those in the original images. The synthesized antibody binds to the antigen in the same way as the antibody originally imaged.
Ward said: "This is a transformative tool for vaccine design and antibody-dependent therapies. ”
Source: Reference News Network
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