Carbohydrate-Binding Proteins Fill in Gaps in Immune Defenses

Faculty member in BCDB and IMP, Dr. Richard D. Cummings, published an article entitled, "Microbial glycan microarrays define key features of host-microbial interactions," in Nature Chemical Biology. The Cummings Lab research group made the discovery that our bodies produce a family of proteins that recognize and kill bacteria whose carbohydrate coatings resemble those of our own cells too closely.

"Many microbes cover themselves with glycans that somewhat resemble our own cells," says Dr. Cummings. "That limits how well the immune system can use antibodies to respond to those microbes."

To prevent auto-immune attack, our bodies usually don’t make antibodies against molecules found on our own cells. That leaves gaps in our defenses that bacteria could exploit. Several of those gaps are filled by galectins, the researchers found.

The Cummings resarch group collaborated with the laboratory of James C. Paulson, PhD, at the Scripps Research Institute (TSRI). Co-first authors of the paper are Sean Stowell, MD/PhD (a resident in in laboratory and transfusion medicine at Emory), Connie Arthur, PhD (postdoctoral fellow at Emory with Stowell), and research assistant Ryan McBride at TSRI.

The research was supported by the National Institute of Allergy and Infectious Diseases (AI050143), the National Heart Lung and Blood Institute (HL107151, HL085607), the National Institute for General Medical Sciences (GM103694, GM098791, GM62116), the US National Blood Foundation, the Swiss National Science Foundation, CSL Behring AG, and the Brazilian Ministry of Education.

Reference:
S.R. Stowell et al. Microbial glycan microarrays define key features of host-microbial interactions. Nat. Chem. Bio doi:10.1038/nchembio.1525 (2014).

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