Protein – Carbohydrate Recognition
Cyanovirin (CVN) like lectins represent a new class of anti-viral agents. Our long-term goal in this research area is to understand the molecular mechanisms and structural basis of high-affinity oligosaccharide recognition and the mode of anti-viral activity of these proteins. Lectins are well known multifaceted carbohydrate-binding proteins that specifically recognize diverse sugar structures and mediate a variety of biological processes such as cell-cell and host-pathogen interactions, serum glycoprotein turnover and innate immune responses. In 1998, our laboratory solved the first solution structure of a cyanobacterial derived protein, CVN, that exhibited potent HIV-inactivating properties. The structure revealed a novel three-dimensional fold, distinct from any known lectin folds. Extensive biochemical and structural characterizations based on our initial results and primarily from our laboratory have now led to the categorization of a new structural class of lectins, with CVN as the class defining member, the so called CVNH family. We have now determined atomic structures of other CVNH family members and are investigating the detailed structure/function relationships for a variety CVNH proteins using structural, biochemical and biophysical approaches. This will lead to a comprehensive molecular understanding of this class of anti-viral lectins.
Angela Gronenborn is a participating investigator in the Consortium for Functional Glycomics.