Engineered Anti-Inflammatory Antibodies may Treat Autoimmune Disease
Enzyme treatment converts autoantibodies into anti-inflammatory antibodies in animal models of two autoimmune diseases
A team of Massachusetts General Hospital (MGH) investigators have developed a method to engineer antibodies within an organism, converting autoantibodies to attack self-tissues into anti-inflammatory antibodies in animal models of two autoimmune diseases by sugar attaching to antibodies. According to the Autoimmune Disease Diagnostics Market report published by Coherent Market Insights, The autoimmune disease causes abnormal organ growth and changes in organ function. The genes of an individual with environmental exposure might be the major reason for autoimmune disease development.
“While more work is required, we hope that this approach of anti-inflammatory antibody conversion will have a beneficial effect on patients suffering from autoimmune and inflammatory diseases,” said Robert Anthony, PhD, researcher at Center for Immunology and Inflammatory Diseases.
The MGH team set out to determine whether administration of a transferase enzyme moves chemical groups such as glycans from one molecule to another that could convert inflammatory antibodies to anti-inflammatory forms within a living animal. While glycans are usually attached to the proteins making up antibodies they are assembled within cells recent evidence suggests they could be modified outside of the cellular environment
Although intravenous administration of either enzyme did not reduce inflammation in a mouse model of rheumatoid arthritis, simultaneous administration of both in a form called B4ST6Fc had anti-inflammatory effects similar to those of high-dose IVIG. B4ST6Fcadministration also reduced kidney damage in a mouse model of lupus-related kidney inflammation. Additional experiments found little evidence that enzyme administration affected antibodies not involved with the specific autoimmune condition and also showed that platelets, which become activated at the site of antibody-driven inflammation, provided the sialic acid and galactose attached to the Fc region by the B4ST6Fc enzyme.
Anthony explains that, while IVIG can be effective against many inflammatory and autoimmune diseases, it is in short supply, the treatment is expensive, and administration is time consuming. “We found that our enzymes were effective at a 400-fold lower dose than high-dose IVIG and by manipulating the enzymes already in an organism, our method eliminates the need for a lengthy IVIG infusion.” Researchers are working on appropriate dosage, optimal administration, and treatments required for this method.
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