The President of the Society is honoured to announce that the 2008 Karl Meyer awardee is:

Richard D. Cummings, Ph.D. William Patterson Timmie Professor and Chair Department of Biochemistry, Emory University School of Medicine Web site

    The breadth of accomplishments of Dr. Cummings in animal glycobiology span nearly 30 years and a publication list of over 175 peer-reviewed manuscripts.  Early studies by Dr. Cummings focused on the binding specificity of plant lectins and their use in purifying glycoproteins that contain specific carbohydrate structures. Subsequent studies used Griffonia simplicifolia lectin IB4 that binds α1,3-galactose residue for the expression cloning of the cDNA encoding α1,3-galactosyltransferase, in collaboration with John Lowe. This was the first report of expression cloning of a glycosyltransferase. Dr. Cummings extended his studies to the animal lectins, including galectins and P-selectin and their corresponding ligands. In collaborative studies with Roger McEver, Dr. Cummings showed that PSGL-1was the major P-selectin counter-receptor and identified sialyl Lewis X on core 2 O-glycans in combination with tyrosine sulfates as the essential structural elements on P-selectin ligands. The Cummings lab expanded these studies by synthesizing the peptide backbone of PSGL-1 and adding a sulfate group and sialyl Lewis X core 2 O-glycans and determining ligand activity for the carbohydrate-binding protein.

   In extended studies on mucin-type O-glycan synthesis, the Cummings lab purified and cloned the β1,3-galactosyltransferase  (core 1 synthase) that forms the Galβ1,3GalNAc structure. He showed that expression of this galactosyltransferase requires a molecular chaperone, termed Cosmc. This was the first report on a chaperone for a glycosyltransferase and represents a landmark discovery in glycobiology. The Cummings lab then showed that Tn syndrome is caused by somatic mutations in Cosmc rather than in the galactosyltransferase gene itself and that the overexpression of sialyl Tn and Tn in tumor cells is also due to somatic mutations in the Cosmc gene. Thus the Cummings lab has made a series of major findings concerning the structure, biosynthesis, and function of mammalian glycoconjugates.

   Dr. Cumming’s versatility is evident by his work with multiple species, ranging from C. elegans to human parasites to mice and humans.  In a series of elegant studies he has applied his broad knowledge of glycobiology to the parasitic organism that causes schistosomiasis and has defined novel oligosaccharide structures and biosynthetic pathways that are helping to explain the immunologic reactions to this infectious agent.

   Beyond his scientific contributions, Dr. Cummings has been a mentor to many students and post-doctorate trainees.  He has served as President of the Society for Glycobiology as well as chair of the Gordon Conference on Glycobiology.  He has been a member of a number of NIH study sections, editor for a number of scientific journals, co-editor of the key reference text in the field, Essentials of Glycobiology, and is well regarded as one of the top spokesmen for the field of glycobiology.  Most recently his leadership skills along with his scientific expertise were recognized by his appointment as Chair of Biochemistry at Emory. The span of the fundamental work and outstanding contributions to glycobiology by Dr. Richard Cummings is being recognized through his selection as the recipient of the 2008 Karl Meyer Award by the Society for Glycobiology. 

The President of the Society is honoured to announce that the 2008 Rosalind Kornfeld Lifetime Achievement Awardees are:

Dr. Nathan Sharon and Dr. Robert G. Spiro  (the text of Dr. Sharon's and Dr. Spiro's remarks upon receiving the Rosalind Kornfeld Award) 

	Nathan Sharon (Professor Emeritus, Weizmann Inst. Science) pioneered studies on glycoconjugates and lectins and made seminal contributions to glycobiology. Dr. Sharon, in collaboration with Roger Jeanloz, first reported the isolation of an unusual bacterial diamino sugar (2,4-diamino-2,4,6-trideoxy-D-glucose) which he named bacillosamine. This sugar is not made by humans and may therefore be a target for anti-bacterial drugs.
He demonstrated that carbohydrates serve as markers for immune cells, demonstrating the use of lectins in fractionation of these cells into biologically distinct cell subpopulations, thus providing immunologists access to the immature thymocytes of mouse and man. His work served as the basis for the routine application of soybean lectin for the purging bone marrow of human donors prior to transplantation into children born with combined immune deficiency ('bubble children'), a procedure that has saved the lives of hundreds of them. In his studies of plant lectins, he demonstrated that plants can glycosylate proteins by a pathway similar to that in animals, and was the first to show that legume lectins are members of a large family of homologous proteins. Dr. Sharon also made important contributions to the field of bacterial lectins, their roles in pathogenesis, and the use of sugars in anti-adhesion therapy of microbial diseases.  His studies provided insights into interactions between lectins and their sugar ligands at the atomic level. Dr. Sharon's achievements are not only of fundamental importance, but also of broad significance for human health. They serve as an excellent example of the convergence between basic and applied research.  In addition to some 300 primary papers, Dr. Sharon has also published numerous widely cited and influential review articles (e.g., 3 in Ann. Rev. Biochem., 3 in Science, 5 in Scientific American). Seven of his publications have been selected as Citation Classics. He was listed among the 1000 most cited scientists in the years between 1965 and 1978 (Current Contents, Oct. 12, 1990) and was ranked 260th among "Citation Superstars 1973-1984" (The Scientist, July 6, 1990). In addition he has recently published, together with his long time colleague Halina Lis, a second and widely expanded edition of the book Lectins, originally published in 1989. Sharon's 'Complex Carbohydrates: their Chemistry, Biosynthesis and Functions' that appeared in 1975 was the first modern text on the subject; the three books were all translated into Japanese. His work continues to be widely quoted, and several of his publications are on top of the citation list of all lectin papers published since 1965. Finally, Dr. Sharon’s contributions are not only to the scientific literature, but also to the often neglected but important area of communicating the importance of science to the lay public and politicians who fund our research.  For his long-lasting contributions to understanding glycoconjugates and the functions of lectins in biological systems, the Society for Glycobiology has awarded Dr. Sharon the 2008 Rosalind Kornfeld Award for Lifetime Achievement in Glycobiology.
	Dr. Robert G. Spiro’s (Professor Emeritus Harvard Med. School and Senior Investigator Emeritus, Joslin Diabetes Center) accomplishments include broad-based fundamental studies on glycoprotein structure, function, and biosynthesis that have had profound and long-lasting impact to the field of glycobiology. Publications from the Spiro lab include over 130 primary
research papers and 32 reviews providing seminal contributions to glycobiology, including synthesis and catabolism of N-glycans, O-glycan, proteoglycans, and collagen glycosylation. Groundbreaking studies in the Spiro lab began with work on the basic structural features of N‐linked carbohydrate units, moving on to their biosynthesis and finally to their role in protein quality control. Key advances in methods development include original papers and review articles that have been widely adopted by other investigators. Numerous review articles, including those in Annual Review of Biochemistry, Advances in Protein Chemistry, New England Journal of Medicine, Journal of Biological Chemistry, and Glycobiology have proved to be a wonderful resource for established glycobiologists as well as generating widespread interest to new investigators in the field.  A recent (2002) review in Glycobiology has been high on the “most‐read list” for several years and was in first place several times in 2007. Highlights of research in the Spiro lab include the first studies on the glyco portion of serum proteins, including groundbreaking studies on fetuin and thyroglobulin, demonstrating both high mannose and complex glycans on the same protein. Studies on these proteins, and microheterogeneity of glycan structures on alpha2-macroglobulin, led to major insights in the assembly and processing of N‐glycans. Characterization of collagen glycosylation and basement membrane proteoglycans were also major areas of research in the Spiro lab. In addition to mature glycan structure determination, the Spiro lab also focused on studies of dolichol-oligosaccharide precursor biosynthesis, transfer to nascent polypeptides via oligosaccharyltransferase, and early glycan trimming events in the ER as a basis for studies on ER glucosidases, exo-mannosidases, and the first identification and characterization of an endo-mannosidase involved in glycan maturation. Among other areas of research include the characterization of released free oligosaccharides in the ER and cytosol leading to a new field of studies of glycan catabolism resulting from ER associated degradation. Sulfation of proteoglycans and N-linked glycans of thyroglobulin was also the subject of numerous publications.The span of fundamental studies in glycobiology and groundbreaking contributions from over four decades of work clearly defines a lifetime of achievement for Dr. Spiro that has been recognized by the Society for Glycobiology with the 2008 Rosalind Kornfeld Award for Lifetime Achievement in Glycobiology.