Steven Foung
Academic Appointments
- Professor, Pathology
Key Documents
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) 723-6481Alternate Contact Paochen Zhang Administrative Associate for Steven Foung Email Tel Work 650-723-6481Not for medical emergencies or patient use
Professional Overview
Clinical Focus
- Pathology
- Transfusion Medicine
Administrative Appointments
- Associate Chair for Academic Affairs, Stanford University School of Medicine - Pathology (2004 - present)
Professional Education
| Residency: | Stanford University School of Medicine CA (1980) |
| Residency: | UCSF Medical Center CA (1977) |
| Internship: | San Francisco General Hospital CA (1976) |
| Medical Education: | UCSD Medical Center CA (1975) |
Industry Relationships
Stanford is committed to ethical and transparent interactions with our industrial and other commercial partners. It is our policy to disclose payments (exclusive of travel support) from, and/or equity in, companies or other commercial entities to Stanford faculty of $5,000 or more in total value, as well as any equity in a privately held company, when the faculty member also has institutional responsibilities related to his or her interactions with the company. View Full Information
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
- Characterization of hepatitis C virus recombinants with chimeric E1/E2 envelope proteins and identification of single amino acids in the E2 stem region important for entry. J Virol. 2013; (3): 1385-99
- Contrasting roles of mitogen-activated protein kinases in cellular entry and replication of hepatitis C virus: MKNK1 facilitates cell entry. J Virol. 2013; (8): 4214-24
- Cooperativity in virus neutralization by human monoclonal antibodies to two adjacent regions located at the amino terminus of hepatitis C virus E2 glycoprotein. J Virol. 2013; (1): 37-51
- Human monoclonal antibodies to a novel cluster of conformational epitopes on HCV E2 with resistance to neutralization escape in a genotype 2a isolate. PLoS Pathog. 2012; (4): e1002653
- Mutations that alter use of hepatitis C virus cell entry factors mediate escape from neutralizing antibodies. Gastroenterology. 2012; (1): 223-233.e9
- Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody. J Virol. 2012; (23): 12923-32
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