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Galectin-1, -2, and -3 Exhibit Differential Recognition of Sialylated Glycans and Blood Group Antigens*
It is demonstrated that each of these galectins mechanistically differ in their binding to glycans on the microarrays and that these differences are reflected in the determinants required for cell binding and signaling.
Glycan microarray analysis of Candida glabrata adhesin ligand specificity
- Margaret L. Zupancic, M. Frieman, David F. Smith, R. Alvarez, R. Cummings, B. Cormack
- BiologyMolecular microbiology
- 1 May 2008
A five‐amino‐acid region within the N‐terminal ligand‐binding domain is mapped that accounts for the difference in specificity of Epa6 and Epa7 and it is shown that these residues contribute to adherence to both epithelial and endothelial cell lines in vitro.
Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen
It is shown that VP8* of a human rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A- type HBGA.
Innate immune lectins kill bacteria expressing blood group antigen
Two innate immune lectins, galectin-4 (Gal-4) and Gal-8, which are expressed in the intestinal tract, recognize and kill human blood group antigen–expressing Escherichia coli while failing to alter the viability of other E. coli strains or other Gram-negative or Gram-positive organisms both in vitro and in vivo.
Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin
It is shown that SubB has a strong preference for glycans terminating in the sialic acid N-glycolylneuraminic acid (Neu5Gc), a monosaccharide not synthesized in humans, which confers susceptibility to the gastrointestinal and systemic toxicities of SubAB.
Receptor binding specificity of recent human H3N2 influenza viruses
- K. Kumari, Shelly Gulati, David F. Smith, Upma Gulati, R. Cummings, G. Air
- BiologyVirology Journal
- 9 May 2007
It is suggested that binding of chicken red cells to cell surface hemagglutinin but not to virions is due to a more favorable hemag GLUTinin density on the cell surface, and the presence of high levels of α2-6 sialic acids on a cell surface does not guarantee productive replication of a virus with α 2-6 receptor specificity.
Human H3N2 Influenza Viruses Isolated from 1968 To 2012 Show Varying Preference for Receptor Substructures with No Apparent Consequences for Disease or Spread
It is concluded that the year-to-year variation in receptor binding specificity is a consequence of amino acid sequence changes driven by antigenic drift, and that viruses with quite different binding specificity and avidity are equally fit to infect and transmit in the human population.
Immunization by Avian H5 Influenza Hemagglutinin Mutants with Altered Receptor Binding Specificity
Structural-based modification of HA specificity can guide the development of preemptive vaccines and therapeutic monoclonal antibodies that can be evaluated before the emergence of human-adapted H5N1 strains.
Dimeric Galectin-8 Induces Phosphatidylserine Exposure in Leukocytes through Polylactosamine Recognition by the C-terminal Domain*
- S. Stowell, C. Arthur, K. Slanina, J. Horton, David F. Smith, R. Cummings
- Biology, ChemistryJournal of Biological Chemistry
- 18 July 2008
Gal-8 dimerization promotes functional bivalency of each CRD, which allows Gal-8 to signal PS exposure in leukocytes entirely through C-terminal domain recognition of polyLacNAc glycans.
Role of Cellular Heparan Sulfate Proteoglycans in Infection of Human Adenovirus Serotype 3 and 35
- S. Tuve, Hongjie Wang, J. Jacobs, Roma C. Yumul, David F. Smith, A. Lieber
- BiologyPLoS pathogens
- 1 October 2008
The findings show that Ad3 and Ad35 directly utilize HSPGs as co-receptors for infection, and suggest that adenoviruses evolved to simulate the presence of physiologic HSPG ligands in order to increase infection.