Chaoping Chen

Chaoping ChenAssociate Professor
Office: MRB 233
Phone: 970-491-0726
Education: Ph.D., Purdue University
Research Title: HIV-1 protease autoprocessing mechanism and drug discovery

Retroviruses are enveloped RNA viruses, which comprise a large and diverse family including human immunodeficiency virus 1 (HIV-1), the causative agent of AIDS. During the late stage of virus replication, specific and highly concerted interactions among viral components and host cofactors are required for progeny virion assembly and release. An exciting possibility is that these specific virus-host interfaces might represent novel targets for the development of therapeutic strategies against HIV-1 infection. We are interested in characterization of the molecular and cellular mechanisms underlying this late stage of HIV-1 replication using a combination of biological imaging, cellular and molecular virology approaches. The ongoing study includes:

  • Understanding the mechanism of HIV-1 protease autoprocessing, a highly regulated reaction responsible for production of the mature protease;
  • Identification and characterization of novel autoprocessing inhibitors. We have established a functional assay that enable an unprecedented screening campaign for small molecule inhibitors that suppress autoprocessing via novel action mechanisms.

Selected Publications

Huang L, Li Y, Chen C. Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions.  Retrovirology 8:79, 2011.

Huang LQ, Sayer JM, Swinford M, Louis JM, Chen C. Modulation of Human Immunodeficiency Virus Type 1 Protease Autoprocessing by Charge Properties of Surface Residue 69. J Virol 83:7789, 2009.

Huang LQ, Hall Al, Chen C. Cysteine 95 and other residues influence the regulatory effects of Histidine 69 mutations on Human Immunodeficiency Virus Type 1 protease autoprocessing. Retrovirology 7:24, 2010.

Chen C, Jin J, Rubin M, Huang L, Sturgeon T, Weixel KM, Stolz DB, Watkins SC, Bamburg JR, Weisz OA, Montelaro RC. Association of Gag multimers with Filamentous Actin during Equine Infectious Anemia Virus Assembly. Curr HIV Res. 5:315-23, 2007 (cover of the issue).

Chen C, Vincent O, Jin J, Weisz OA, Montelaro RC. Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding. J Biol Chem 280:40474, 2005.

Chen C, Weisz OA, Stolz DB, Watkin SC, Montelaro RC. Differential effects of actin cytoskeleton dynamics on equine infectious anemia virus particle production. J Virol 78:882, 2004.

Chen C and Montelaro RC. Characterization of RNA elements that regulate Gag-Pol ribosomal frameshifting in equine infectious anemia virus. J Virol 77:10280, 2003.

Li F, Chen C, Puffer BA, Montelaro RC. Functional replacement and positional dependence of homologous and heterologous L-domains in equine infectious virus budding and infection. J Virol 76:1569, 2002.

Chen C, Li F, Montelaro RC. Functional role of equine infectious anemia virus Gag p9 in viral budding and infection. J Virol 75:9762, 2001.

Chen C, Sheng S, Shao Z, Guo P. A dimer as a building block in assembling RNA, A hexamer that gears bacterial virus phi29 DNA-translocating machinery. J Biol Chem 275:17510, 2000.

Guo P, Zhang C, Chen C, Garver K, Trottier M. Inter-RNA interaction of phage phi29 pRNA to form a hexameric complex for viral DNA translocation. Mol Cell 2:149, 1998.

Chen C and Guo P. Sequential action of six DNA-packaging pRNAs during phage phi29 genomic DNA translocation. J Virol 71:3864, 1997.

NIH PubMed Publications List