AIDS and Cancer Virus Program

Biography

Dr. Elena Chertova received her Master’s Degree in Biochemistry from Moscow State University, Moscow, Russia; and PhD from Shemyakin Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia. Her area of expertise is in studying protein structure, function, and topography. In 1993-1994 she was a visiting scientist at the Department of Biochemistry and Biophysics at Chalmers University of Technology in Gothenburg, Sweden. In 1994, Dr. Chertova joined the AIDS Vaccine Program (now AIDS and Cancer Virus Program) and has been the Head of the Retroviral Protein Chemistry Core since 2004.

Core Description

The Retroviral Protein Chemistry Core (RPCC) provides unique state-of-the-art preparative and analytic protein chemistry expertise, applied to the characterization of retroviral virions and related samples. The laboratory has pioneered the development of techniques for the use of HPLC methods for the separation of retroviral virions into their constituent proteins. The evolution of these methods to include microbore HPLC approaches allows analyses to be performed using much smaller amounts of virus than had been possible previously, including amounts achievable using transfection methods, without a requirement for intervening amplification in culture that can introduce mutations. Analytical techniques available include gel analysis, immunoblots, protein microsequencing and amino acid analysis, and mass spectrometry. The RPCC also performs studies and provides analytical support for studies of various approaches to the inactivation of retroviruses, including chemical confirmation of relevant modifications by different inactivation approaches and detailed analyses of mechanisms of inactivation. With the Retroviral Mutagenesis Section of the AIDS and Cancer Virus Program, the RPCC makes available to AIDS researchers purified wild type and selected mutant recombinant retroviral nucleocapsid proteins, to facilitate further research on this important viral protein. Where feasible, the protein purification and characterization capabilities of the RPCC are also made available to non-ACVP investigators within the NCI, NIH and the extramural community.

Recent Publications

1. Waheed AA, Ablan SD, Sowder RC, Roser JD, Schaffner CP, Chertova E, Freed EO: Effect of mutations in the HIV-1 protease on cleavage of the gp41 cytoplasmic tail. J Virol 84(6)3121-3126, 2010. Epud 2009 Dec 30. PMID: 20042499.
2. Minang JT, Trivett MT, Coren LV, Barsov EV, Piatak MJr, Chertov O, Chertova E, Ott DE, Ohlen C: The Mamu B 17-restricted SIV Nef IW9 to TW9 mutation abrogates correct epitope processing and presentation without loss of replicative fitness. Virology 375:307-314, 2008.
3. Xu H, Chertova E, Chen J, Ott DE, Roser JD, Hu W-S, Pathak VK: Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions. Virology 360:247-256, 2007.
4. Waheed AA, Ablan SD, Roser JD, Sowder RC, Schaffner CP, Chertova E, Freed EO: HIV-1 escape from the entry-inhibiting effects of a cholesterol-binding compound via cleavage of gp41 by the viral protease. PNAS 104:8467-8471, 2007.
5. Coren LV, Thomas JA, Chertova EN, Sowder RC, II, Gagliardi TD, Gorelick RJ, Ott DE: Mutational analysis of the C-terminal gag cleavage sites in human immunodeficiency virus type 1. J Virol 81:10047-10054, 2007.
6. Zhu P, Liu J, Bess J, Chertova E, Lifson JD, Grise H, Ofek GA, Taylor KA, Roux KH. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 441:847-852, 2006.
7. Chertova E, Chertov O, Coren LV, Roser JD, Trubey CM, Bess JW, Sowder RC, Barsov E, Hood BL, Fisher RJ, Nagashima K, Conrads TP, Veenstra TD, Lifson JD, Ott DE: Proteomic and biochemical analysis of purified HIV-1 produced from infected monocyte-derived macrophages. J Virol 80:9039-9052, 2006.
8. Morcock DR, Thomas JA, Gagliardi TD, Gorelick RJ, Roser D, Chertova EN, Bess JWJr, Ott DE, Sattentau QJ, Frank I, Pope M, Lifson JD, Henderson LE, Crise BJ: Elimination of retroviral infectivity by N-ethylmaleimide with preservation of functional envelope glycoproteins. J Virol 79:1533-1542, 2005.
9. Louder MK, Sambor A, Chertova E, Hunte T, Barrett S, Ojong F, Sanders-Buell E, Zolla-Pazner S, McCutchan FD, Roser JD, Gabuzda D, Lifson JD, Mascola JR: HIV-1 envelope pseudotyped viral vectors and infectious molecular clones expressing the same envelope glycoprotein have a similar neutralization phenotype, but culture in peripheral blood mononuclear cells is associated with decreased neutralization sensitivity. Virology 339:226-238, 2005.
10. Raviv Y, Viard M, Bess JW, Chertova E, Blumenthal R: Inactivation of retrovirus with preservation of structural integrity by targeting the hydrophobic domain of the viral envelope. J Virol 79:12394-12400, 2005.

Staffing

• Raymond C. Sowder, II, Associate Scientist
• J. David Roser, Research Associate I