Daved H. Fremont

Last updated
Daved H. Fremont
Born(1964-01-13)January 13, 1964
Alma mater University of California, San Diego
Scientific career
Institutions Washington University School of Medicine in St. Louis
Doctoral advisor Ian Wilson

Daved H. Fremont (born January 13, 1964) is a professor at the Washington University School of Medicine in St. Louis with dual appointments in the Departments of Pathology and Immunology/Biochemistry and Molecular Biophysics. He is currently director of the Computational and Molecular Biophysics Program. [1] Fremont is also a principal investigator in the Center for Structural Genomics of Infectious Disease and his laboratory has deposited structures of proteins from several major human pathogens to the protein data bank (PDB). [2]

In 1993, Fremont received his Ph.D. in chemistry working in Ian Wilson's laboratory at The Scripps Research Institute while a student at the University of California, San Diego.

In 1998, he joined Washington University in St. Louis as an assistant professor where his research expanded to include viral immune evasion and antibody-mediated neutralization. His laboratory has since established the structural basis for interactions between host cytokines and poxviruses [3] and herpesviruses [4] decoy receptors and neutralization of West Nile virus by therapeutic antibodies. [5] Fremont is now best known for his research on how the immune system recognizes viruses and the subversion mechanisms they deploy to avoid detection and clearance.

On the personal side, Fremont is married and has a daughter. He enjoys playing Go and poker; in the latter, he is partial to seven card stud, especially the Chesterfield version, and does not prefer wild card games.[ citation needed ]

Related Research Articles

<span class="mw-page-title-main">HIV vaccine development</span> In-progress vaccinations that may prevent or treat HIV infections

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<span class="mw-page-title-main">Hemagglutinin (influenza)</span> Hemagglutinin of influenza virus

Influenza hemagglutinin (HA) or haemagglutinin[p] is a homotrimeric glycoprotein found on the surface of influenza viruses and is integral to its infectivity.

<i>Dengue virus</i> Species of virus

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<span class="mw-page-title-main">CCR5</span> Immune system protein

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Viral pathogenesis is the study of the process and mechanisms by which viruses cause diseases in their target hosts, often at the cellular or molecular level. It is a specialized field of study in virology.

<span class="mw-page-title-main">Single-domain antibody</span> Antibody fragment

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<span class="mw-page-title-main">Envelope glycoprotein GP120</span> Glycoprotein exposed on the surface of the HIV virus

Envelope glycoprotein GP120 is a glycoprotein exposed on the surface of the HIV envelope. It was discovered by Professors Tun-Hou Lee and Myron "Max" Essex of the Harvard School of Public Health in 1984. The 120 in its name comes from its molecular weight of 120 kDa. Gp120 is essential for virus entry into cells as it plays a vital role in attachment to specific cell surface receptors. These receptors are DC-SIGN, Heparan Sulfate Proteoglycan and a specific interaction with the CD4 receptor, particularly on helper T-cells. Binding to CD4 induces the start of a cascade of conformational changes in gp120 and gp41 that lead to the fusion of the viral membrane with the host cell membrane. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.

<span class="mw-page-title-main">Innate immune system</span> Immunity strategy in living beings

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<span class="mw-page-title-main">Antibody-dependent cellular cytotoxicity</span> Cell-mediated killing of other cells mediated by antibodies

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<span class="mw-page-title-main">C-C chemokine receptor type 7</span> Protein-coding gene in the species Homo sapiens

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A bispecific monoclonal antibody is an artificial protein that can simultaneously bind to two different types of antigen or two different epitopes on the same antigen. Naturally occurring antibodies typically only target one antigen. BsAbs can be manufactured in several structural formats. BsAbs can be designed to recruit and activate immune cells, to interfere with receptor signaling and inactivate signaling ligands, and to force association of protein complexes. BsAbs have been explored for cancer immunotherapy, drug delivery, and Alzeimer's disease.

<span class="mw-page-title-main">Vaccine Research Center</span>

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A neutralizing antibody (NAb) is an antibody that defends a cell from a pathogen or infectious particle by neutralizing any effect it has biologically. Neutralization renders the particle no longer infectious or pathogenic. Neutralizing antibodies are part of the humoral response of the adaptive immune system against viruses, intracellular bacteria and microbial toxin. By binding specifically to surface structures (antigen) on an infectious particle, neutralizing antibodies prevent the particle from interacting with its host cells it might infect and destroy.

<span class="mw-page-title-main">K. Christopher Garcia</span>

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References

  1. "The Division of Biology & Biomedical Sciences". Dbbs.wustl.edu. 2012-11-05. Retrieved 2013-09-28.
  2. "Center for Structural Genomics of Infectious Diseases - Investigators". Csgid.org. Retrieved 2013-09-28.
  3. Phoebe L. Arnold, et al. "Structural determinants of chemokine binding by an Ectromelia virus-encoded decoy receptor.", Journal of Virology, 2006
  4. Jennifer M. Alexander, et al. "Structural basis of chemokine sequestration by a herpesvirus decoy receptor.", Cell, 2002
  5. Grant E. Nybakken, et al. "Structural basis of West Nile virus neutralization by a therapeutic antibody", Nature, 2005