The unusual structure of certain antibodies found in cattle could add to understanding of the diversity of antibodies and their specific functions in the immune systems of human and cattle.
In research to presented at the 58th Annual Biophysical Society Meeting this week, Dr. Damian Ekiert, from University of California, San Francisco, described research conducted at the Scripps Research Institute in La Jolla, Calif. His presentation abstract, titled “Reshaping Antibody Diversity.” is available online.
The researchers used used x-ray crystallography to determine the unusually long "ball and chain" structure of the bovine antibodies, while deep sequencing helped them study the function and generation of these antibodies.
Quoted in a news release, Ekiert says antibody diversity is particularly important because an animal’s ability to recognize and neutralize a wide range of pathogens directly depends on the diversity of its antibody repertoire. “The more different kinds of antibodies we have in our bodies, the more different kinds of targets we can block."
Studying the immune systems of cows and other animals, he adds, helps scientists understand how human immune systems function. “The unique structure of these cow antibodies may be particularly well-suited for recognizing certain kinds of antigens and may be useful for antibody based therapies or diagnostics.”
The next steps in realizing the potential of this research, according to the release, are to determine how these antibodies recognize their target molecules and bind to them.