The Society for Glycobiology is pleased to announce that the recipient of the 2012 Karl Meyer Award is Kurt Drickamer. 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. Kurt Drickamer Imperial College London
Dr. Drickamer is most recognized for his discoveries on cloning the genes encoding lectins or glycan-binding proteins, including the C-type lectin family, for which he coined the term, and characterizing the topological arrangements, expression and functions of such lectins. Dr. Drickamer also was the first to recognize that these lectins, along with other families of lectins, including galectins, contain a carbohydrate-recognition domain (CRD). His work has been most insightful into the expression and functions of the C-type lectins, which occur in both soluble forms and on cell-surfaces, and how these lectins recognize and distinguish the spectrum of glycans that is attached to macromolecules, cells and pathogen surfaces. The succession of field-leading discoveries that Dr. Drickamer has made during the last thirty years and through his over 100 publications, and the insights they afford, has had incomparable influence on the forefront of research in several disciplines, including biochemistry, structural biology, immunology and microbiology. Another of Dr. Drickamer's famous insights was recognition of the unprecedented orientation of the hepatic glycoprotein C-type lectin receptor in the plasma membrane, with its N-terminus inside the cell and its C-terminus outside. He went on to demonstrate that the type II proteins (unlike type I) do not need cleavable N-terminal signal sequences for membrane insertion, as their hydrophobic transmembrane anchor serves double-duty as the signal sequence.
In his outstanding work on the modular nature of CRDs, he demonstrated that the soluble mannose-binding protein of blood and lymph also contains CRDs. He showed that the CRDs are linked to collagen-like sequences, as is also the case for pulmonary surfactants. Collagen-like stalks are also a feature of C1q, the complement component that initiates the classical pathway of complement activation, leading Dr. Drickamer to see the functional parallel between mannose-binding protein and C1q: the former detecting pathogens to initiate innate immunity, the latter initiating adaptive immunity through detection of pathogen-specific antibody bound to the pathogen. These were major contributions to our early understanding of the role of glycan recognition in regulating immune responses.
Extending these studies to cell-surface C-type lectins, he found that DC-SIGN, a pathogen receptor on dendritic cells that initiates immune responses to viral infection, employs an alternative strategy in which display of carbohydrate-binding sites restricts their engagement to the geometry of the more complex glycans that characterize viruses. Dr. Drickamer also determined that several related proteins, which were not known to bind carbohydrates, had CRDs with carbohydrate-binding activity based on Western blotting. In extending the approach, he pioneered genome scanning to identify novel, uncharacterized proteins as candidates for having glycan-binding function. Complementing this approach, Dr. Drickamer emerged as a leader in applying glycan array technology to test these candidates and determine their sugar specificities. Examples are his studies on endothelial cell scavenger receptor C-type lectin, LSECtin, a glycan-binding receptor on liver and lymph node sinusoidal endothelial cells, and prolectin, which has specificity for terminal fucose or mannose and is expressed in rapidly dividing B cells of germinal centers.
Besides his scientific contributions, Dr. Drickamer has been a world leader in education and the promotion of glycobiology. The identification of lectin families and modular CRDs provided important organizing principles in the development of the field over the past 25 years, as is clearly and concisely laid out in the recently published third edition of the 2011 textbook "Introduction to Glycobiology", which he co-authored with his colleague and collaborator Maureen Taylor. In addition, Dr. Drickamer has been a major leader in supporting international glycobiology, and served as deputy chair of the Steering Committee for the Consortium for Functional Glycomics for a decade.
From his seminal contributions to the field both in high impact research and service, as well as his pioneering work in defining glycan-binding proteins, Kurt Drickamer represents the very best in the field and thus has been awarded the 2012 Karl Meyer award from the Society for Glycobiology.