David F. Smith

Publications164
h-index52
Citations7,046
Highly Influential Citations253
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Galectin-1, -2, and -3 Exhibit Differential Recognition of Sialylated Glycans and Blood Group Antigens*
TLDR
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.
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Glycan microarray analysis of Candida glabrata adhesin ligand specificity
TLDR
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.
View on Wiley
Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen
TLDR
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.
View on Nature
Innate immune lectins kill bacteria expressing blood group antigen
TLDR
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.
View on Nature
Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin
TLDR
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.
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Human H3N2 Influenza Viruses Isolated from 1968 To 2012 Show Varying Preference for Receptor Substructures with No Apparent Consequences for Disease or Spread
TLDR
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.
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Receptor binding specificity of recent human H3N2 influenza viruses
TLDR
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.
View on Springer
A Novel Mechanism for LSECtin Binding to Ebola Virus Surface Glycoprotein through Truncated Glycans*
TLDR
Glycan analysis of the surface glycoprotein of Ebola virus reveals the presence of such truncated glycans, explaining the ability of LSECtin to facilitate infection by Ebola virus.
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Immunization by Avian H5 Influenza Hemagglutinin Mutants with Altered Receptor Binding Specificity
TLDR
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.
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Dimeric Galectin-8 Induces Phosphatidylserine Exposure in Leukocytes through Polylactosamine Recognition by the C-terminal Domain*
TLDR
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.
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