Richard Cummings, PhD

Dr. Cummings' laboratory is interested in the fundamental biological processes regulating cell adhesion and signaling with particular emphasis on the functions of glycans in glycoproteins and other glycoconjugates. Cell adhesion/signaling is essential for animal cell development, differentiation, tumor metastasis, inflammation and microbial pathogenesis and is mediated by glycoconjugates and glycan-binding proteins (GBPs) and antibodies that recognize these glycans.

Cummings' laboratory has projects in multiple areas including cancer biology and the roles of glycoconjugates in cancer initiation and metastasis, developmental biology, parasitology, e.g. schistosomiasis and helminth infections, microbial and viral pathogenesis, as well as the general development of glycomics and techniques in the glycoscience area. The laboratory studies a wide variety of GBPs, such as C-type lectins and galectins, which are expressed by all cells and their roles in specific cellular functions. The laboratory utilizes mouse and human genetics and a host of biochemical strategies to define molecular pathways of developmental and disease importance in which specific glycan expression is implicated.

Dr. Cummings is the Director of the National Center for Functional Glycomics (NCFG) and Chair of the Consortium for Functional Glycomics, both supported by the NIH/NIGMS. Cummings is also the Director of the newly designated Harvard Medical School Center for Glycoscience (along with Co-Director Dr. Robert Sackstein). The Center makes available 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. Some key techniques in the Center are sequence analysis of glycans in glycoproteins, serum or plasma, and cells, the development of shotgun glycomics to sequence the glycans in the human glycome, and the screening of GBPs and antibodies on glycan microarrays of defined glycans, glycopeptides, and glycopeptides, as well as on microarrays of natural glycans derived from human, animal, and microbial sources.