Dr. Cummings's laboratory is interested in the fundamental biological process by which cells adhere to each other and interact with the extracellular matrix or basement membrane. This research area also relates to processes by which animal pathogens, such as viruses, bacteria, and parasites stick to animal cells and initiate disease. Cell adhesion is an essential prelude to animal cell development, differentiation, tumor metastasis, inflammation and microbial pathogenesis.
Many recent studies indicate that carbohydrate residues within glycoconjugates on the surfaces of cells and in the extracellular matrices are critically involved in cell "stickiness" or cell adhesion phenomena. The overall hypothesis is that these glycoconjugates are recognized and bound by a class of proteins called lectins expressed by a wide variety of cells. There are likely to be many different lectins and many different glycoconjugates involved in cell adhesion. Dr. Cummings's laboratory is currently studying lectins and glycoconjugates important in a wide variety of cell adhesion phenomena. These include leukocyte recruitment to sites of inflammation in human tissues, adhesion of human rotaviruses to human intestinal cells, structure and immunogenicity of glycoproteins on the surfaces of the human parasitic blood fluke Schistosoma mansoni, binding of lectins to glycoproteins of the extracellular matrix, and the cloning and identification of genes encoding lectins and enzymes (glycosyl transferases) responsible for synthesizing glycoconjugates.
Dr. Cummings is the Coordinator of Core Facility H at Emory University, part of the Consortium for Functional Glycomics (CFG), a large research initiative funded by the National Institute of General Medical Sciences (NIGMS). The consortium is comprised of Scientific Core Facilities located at prestigious research institutions in the United States and Europe. The Core Facilities (designated A through H) are producing a variety of resources and services to investigators for use in performing experiments that contribute to our understanding the roles of carbohydrate-protein interactions at the cell surfaces in cell-cell adhesion and cellular signaling. Dr. David Smith, newly appointed Professor in the Biochemistry, is the Director of Core Facility H.
Core Facility H is the central resource for conducting glycan binding specificity and affinity studies for a wide range of projects initiated by Participating Investigators. The central technique of Core H is the screening of Glycan Binding Proteins (GBP) on microarrays of defined oligosaccharides, glycopeptides, and glycoproteins. The Core has developed a process for receiving samples and reporting data that encompasses communication, sample handling, glycan array manufacture, standardized assays, data processing, data upload, and data dissemination. The data generated by Core H are made available to Participating Investigators and deposited in the database where it also become available to the public according to Consortium policy. In the last few years Core H, which is one of the most popular technology resources developed by the Consortium, has seen dramatic growth in the number of resource requests from researchers to screen samples on the glycan array. The unique aspect of the glycan array is that dedicated funding supports the level of resources needed to build and grow an array of glycans on an unprecedented scale and is freely available to researchers world-wide. The future aim of Core H is to extend and improve novel technologies to aid Participating Investigators in a broad range of disciplines to explore how protein-glycan interactions influence cell communication and adhesion in many biological systems, including roles of glycoconjugates in innate and acquired immunity and host-pathogen interactions.
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