Viral membrane fusion figure, from the Peter S. Kim Lab

Welcome to the Peter S. Kim Lab

We are studying the mechanism of viral membrane fusion and its inhibition by drugs and antibodies. We use the HIV envelope protein (gp120/gp41) as a model system. Some of our studies are aimed at creating an HIV vaccine that elicits antibodies against a transient, but vulnerable, intermediate in the membrane-fusion process, called the pre-hairpin intermediate.

We are also interested in protein surfaces that are referred to as "non-druggable". These surfaces are defined empirically based on failure to identify small, drug-like molecules that bind to them with high affinity and specificity. Some of our efforts are aimed at characterizing select non-druggable targets. We are also interested in developing methods to identify ligands for non-druggable protein surfaces.

Publication Highlights

  1. Vaccination with peptide mimetics of the gp41 prehairpin fusion intermediate yields neutralizing antisera against HIV-1 isolates.
    Elisabetta Bianchi, Joseph G. Joyce, Michael D. Miller, Adam C. Finnefrock, Xiaoping Liang, Marco Finotto, Paolo Ingallinella, Philip McKenna, Michael Citron, Elizabeth Ottinger, Robert W. Hepler, Renee Hrin, Deborah Nahas, Chengwei Wu, David Montefiori, John W. Shiver, Antonella Pessi, and Peter S. Kim Proc. Natl. Acad. Sci. USA (2010) 107: 10655-10660. (PDF)
  2. A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope
    Michael D. Miller, Romas Geleziunas, Elisabetta Bianchi, Simon Lennard, Renee Hrin, Hangchun Zhang, Meiqing Lu, Zhiqiang An, Paolo Ingallinella, Marco Finotto, Marco Mattu, Adam C. Finnefrock, David Bramhill, James Cook, Debra M. Eckert, Richard Hampton, Mayuri Patel, Stephen Jarantow, Joseph Joyce, Gennaro Ciliberto, Riccardo Cortese, Ping Lu, William Strohl, William Schleif, Michael McElhaugh, Steven Lane, Christopher Lloyd, David Lowe, Jane Osbourn, Tristan Vaughan, Emilio Emini, Gaetano Barbato, Peter S. Kim, Daria J. Hazuda, John W. Shiver, and Antonello Pessi Proc. Natl. Acad. Sci. (2005) 102: 14759-14764. (PDF)
  3. Mechanisms of Viral Membrane Fusion and Its Inhibition.
    Debra M. Eckert and Peter S. Kim Annu. Rev. Biochem. (2001) 70: 777-810. (PDF)
  4. Protein Design of an HIV-1 Entry Inhibitor
    Michael J. Root, Michael S. Kay, Peter S. Kim Science (2001) 291: 884-888. (PDF)
  5. Inhibiting HIV-1 Entry: Discovery of D-Peptide Inhibitors that Target the gp41 Coiled-Coil Pocket.
    Debra M. Eckert, Vladimir N. Malashkevich, Lily H. Hong, Peter A. Carr and Peter S. Kim Cell (1999) 99: 103-115. (PDF)
  6. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    David S. Chan, Christine T. Chutkowski, Peter S. Kim Proc. Natl. Acad. Sci. (1998) 95: 15613-15617. (PDF)
  7. Influenza hemagglutinin is spring-loaded by a metastable native conformation
    Chavela M. Carr, Charu Chaudhry, Peter S. Kim Proc. Natl. Acad. Sci. (1997) 94:14306-14313. (PDF)