Steven Foung
Academic Appointments
- Professor, Pathology
Contact Information
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Clinical Offices
Stanford Blood Center 3373 Hillview Ave MC 5556 Palo Alto, CA 94304 Tel Work (650) 723-6481 Fax (650) 725-6610Practices at Stanford Hospital and Clinics and Lucile Packard Children's Hospital
- Academic Offices
Personal Information Email Tel (650) 723-6481Administrative Contact Paochen Zhang Administrative Associate for Steven Foung Email Tel Work 650-723-6481Not for medical emergencies or patient use
Professional Snapshot
Clinical Focus
- Pathology
- Pathology and Laboratory Medicine
Administrative Appointments
- Associate Chair for Academic Affairs, Stanford University School of Medicine - Pathology (2004 - present)
Professional Education
| Residency: | SUMC - Graduate Medical Education, CA (1980) |
| Residency: | UCSF Medical Center, CA (1977) |
| Internship: | San Francisco General Hospital, CA (1976) |
| Medical Education: | UCSD Medical Center, CA (1975) |
Postdoctoral Advisees
Scientific Focus
Current Research Interests
The Foung laboratory is focused on the early events of hepatitis C virus infection- virus attachment and entry to susceptible cells. The approach is through the generation of human monoclonal antibodies (HMAbs) to the virus envelope proteins with an emphasis on antibodies to conformational epitopes. A large panel of HMAbs has been produced with many broadly reactive to different HCV isolates common in the US and elsewhere. Functional studies showed that the HCV envelope E2 glycoprotein is organized in distinct immunological and functional clusters with epitopes within each cluster or domain sharing similar functional and structural properties. At least three domains mediate virus neutralization and antibodies to epitopes within two domains inhibit virus binding to the virus receptor, CD81. Interestingly, some of these antibodies also block a second step in virus entry by inhibiting the low pH induced virus envelope conformational rearrangement that is necessary to trigger virus fusion with the endosomal membrane. These findings support the view that virus entry is mediated by only specific determinants on the virus surface and appear to be restricted to distinct immunogenic domains. This is in contrast for other viruses where the convention is that neutralization is the result of a critical number of any binding sites being occupied and preventing virus entry through steric hindrance. Studies are underway on expanding this model of the virus envelope glycoproteins, which will be important in linking structure and function.
Publications
- CD81 is dispensable for hepatitis C virus cell-to-cell transmission in hepatoma cells. J Gen Virol. 2009; (Pt 1): 48-58
- Antigen-specific proteolysis by hybrid antibodies containing promiscuous proteolytic light chains paired with an antigen-binding heavy chain. J Biol Chem. 2009; (36): 24622-33
- Antibody-dependent enhancement of hepatitis C virus infection. J Virol. 2008; (5): 2140-9
- In vitro selection of a neutralization-resistant hepatitis C virus escape mutant. Proc Natl Acad Sci U S A. 2008; (49): 19450-5
- Hepatitis C virus (HCV)-induced immunoglobulin hypermutation reduces the affinity and neutralizing activities of antibodies against HCV envelope protein. J Virol. 2008; (13): 6711-20
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