The 2015 Karl Meyer Award goes to Robert S. Haltiwanger
The Society for Glycobiology is pleased to announce that the recipient of the 2015 Karl Meyer Award is Robert S. Haltiwanger. The Karl Meyer Award was established in 1990 to honor the distinguished career of Karl Meyer and his outstanding contributions to the field of Glycobiology. This international award is presented to well-established scientists with currently active research programs who have made widely recognized major contributions to the field of Glycobiology.
Dr. Robert S. Haltiwanger (GRA Eminent Scholar in Biomedical Glycosciences and Professor of Biochemistry and Molecular Biology at the Complex Carbohydrate Research Center of the University of Georgia) began his scientific career in the laboratory of Dr. Robert Hill at Duke University working on two mammalian lectins: a novel fucose-binding lectin from rat liver and the mannose receptor, which he purified and characterized from rat lung alveolar macrophages. From his PhD research he published 3 first-author papers and a second author paper. His postdoctoral work was with Jerry Hart at Johns Hopkins where his major contribution was development of an in vitro assay for, and the purification of, O-GlcNAc Transferase (OGT), the nucleocytoplasmic glycosyltransferase that adds O-GlcNAc to proteins. He also collaborated with other postdocs and students in the Hart lab and ended up publishing 10 peer reviewed papers and 5 reviews. He was first author on 3 of the peer-reviewed papers. Following his postdoc, Bob was appointed Assistant Professor of Biochemistry and Cell Biology at Stony Brook University in 1992. During the past 21 years Bob progressed through the ranks in a timely manner, and became Interim Chair of the department in 2007. The honor of being chosen for this position reflects Bob's high standing within the department and the university at large. Thus only 2 years later, Bob was appointed Chair. Bob's lab at Stony Brook is highly respected and internationally recognized as the lab that can determine the sites of attachment and structure of the rare O-glycans of Notch receptors, and the lab that has purified, cloned and characterized the glycosyltransferases that generate these O-glycans. Bob's lab was the first to clone mammalian protein O-fucosyltransferase 1 (POFUT1), to determine the structure of the O-fucose glycans attached to Notch EGF repeats, and to determine that the Fringe proteins are glycosyltransferases that add a β3-linked GlcNAc to O-fucose. His lab developed an assay for the first protein O-glucosyltransferase (POGLUT1) and demonstrated that the Drosophila gene, rumi, encodes this activity. They also showed that POGLUT1/Rumi is a dual specificity enzyme that can transfer xylose directly to EGF repeats as well as glucose. His group has mapped the sites of O-glucose modification on several Notch proteins and made contributions to what is known about the xylosyltransferases that elongate O-glucose. His group has also identified and characterized POFUT2, which adds O-fucose to thrombospondin type 1 repeats (TSRs), and showed that modification of TSRs with O-fucose is required for folding of these domains in several proteins. In short, Bob is the world expert on the enzymes that synthesize non-mucin O-glycans in Drosophila and mammals, the structures of these O-glycans, and their influence on Notch signaling or TSRs in cell-based assays.
Bob has been PI or co-PI on several grants from NIH and other public and private agencies. He has also received a number of awards over the years in recognition of his excellent science. Bob is an excellent mentor, well liked by his students and postdocs. He is also a model departmental and university citizen, serving on numerous school-wide committees, and teaching extensively in undergraduate and graduate courses. For the glycobiology community, Bob is also an outstanding contributor and role model. He continues to serve as Editor-In-Chief of Glycobiology, the leading journal devoted to our field, and he is an enthusiastic participant in meetings, gives excellent, clear and logical talks and contributes generously. He has been elected Chair of the Gordon Conference on Glycobiology and President of the Society of Glycobiology, and in those capacities, has organized international meetings that were appreciated by all.
In summary, Bob is a consummate glycobiologist/biochemist, in the mold of Karl Meyer. He has excelled in the isolation, purification and characterization of several lectins and glycosyltransferases. He has developed sensitive mass spec techniques to determine sites of glycosylation and the structures of O-glycans. He is a leader in the field of glycobiology. He is highly deserving of the Karl Meyer Lectureship Award of the Society for Glycobiology.