Q&A With Robert Anthony, FARE Investigator in Food Allergy
Robert M. Anthony, PhD, is an associate professor at Harvard Medical School and a principal investigator in the Center for Immunology and Inflammatory Diseases at Massachusetts General Hospital. He received a mid-career FARE Investigator in Food Allergy award in 2017. Here he discusses his research on how the glycosylation of allergy-associated IgE antibodies – that is, the addition of sugars molecules to IgE proteins – might influence food allergy.
Robert M. Anthony, PhD, is an associate professor at Harvard Medical School and a principal investigator in the Center for Immunology and Inflammatory Diseases at Massachusetts General Hospital. He received a mid-career FARE Investigator in Food Allergy award in 2017. Here he discusses his research on how the glycosylation of allergy-associated IgE antibodies – that is, the addition of sugars molecules to IgE proteins – might influence food allergy. Dr. Anthony will be presenting an update on his work at the 2019 FARE Research Retreat, to be held April 13 in McLean, VA.
What first attracted you to food allergy research?
Our start in food allergy was a practical one. During my postdoctoral fellowship I worked on IgG antibodies (the most abundant type of antibodies in blood, best known for fighting infection). When I started my own lab, I started working on IgE (the antibody that causes allergy). Our lab neighbors the lab of [FARE's medical advisor for Research] Wayne Shreffler, and Wayne’s interest in food allergy has rubbed off. Plus, we believe there is a gap in what we know about the role and regulation of antibody glycosylation in food allergy.
What has sustained your interest?
In addition to food allergy being a serious clinical condition, the complexity of the disease and its treatment are fascinating. So many components of the immune system are involved. Also, it is unclear how some individuals can have food-specific IgE and never experience food allergy, while others have life-threatening allergic reactions. There is a lot of work to be done.
What experimental finding has surprised you the most, and why?
The importance of IgE glycosylation has been a surprise to us, and also very rewarding. Glycosylation is a modification that occurs after proteins are made, in which glycans (sugars) are added to the proteins. These glycans have been shown to be important for IgG antibodies, but little was known about the importance of glycosylation to the IgE antibodies that cause food allergy. Our work has shown that these glycans are important.
How might your FARE-supported research affect patient care in the future?
We hope that targeting the glycans on IgE might offer a new therapeutic approach for food allergy. The differences in the glycans on IgE may hold the answer to why individuals with food-specific IgE can have such distinct clinical presentations. The glycans may be a biomarker for food allergy.
What unresolved question relating to food allergies would you most like to see answered?
I am intrigued to learn how and why oral immunotherapy works. It is fascinating that feeding increasing doses of peanut flour to peanut allergic-patients results in sustained peanut tolerance in some patients, but not others. The reason is probably multifactorial, but we would be thrilled if IgE glycosylation was a contributing factor!