Danso Ako-Adjei, Ph.D.

Viral Genome Curator

Computercraft (contractor for NIH), Washington, DC



Education

B.S., Biology/Biotechnology, Carleton University, Ottawa, ON, Canada, 2001
Ph.D., Molecular Biology and Genetics, Cornell University, Ithaca, NY, 2007
FIRST Postdoctoral Fellow,
Emory School of Medicine, Department of Pediatrics, 2007-2009


Research Statement

The nuclear export of most cellular mRNAs is mediated by the NXF1 complex. As with most cellular mRNAs, efficient export is heavily dependent on the presence of intronic sequences. This poses a problem for retroviruses as they must export intron-containing genomic RNA as well as spliced transcripts that express the full complement of their viral proteins. In order to overcome this problem, many retroviruses rely on stem-loop structures which directly recruit NXF1 nuclear export machinery. In the case of HIV-1, the viral protein Rev facilitates export of unspliced RNAs by interacting with a cis-acting viral sequence known as the Rev response element (RRE) and recruiting the cellular Crm1 nuclear export machinery.

As with most infectious diseases, an animal model is critical to understanding the lifecycle of the infectious agent. It has recently been suggested that the inefficient expression and release of HIV-1 virions from mouse cells is a consequence of utilizing the Crm1 nuclear export mechanism. I am interested in elucidating the nature of HIV-1 RNA export as well as understanding the differences between the human and murine nuclear export machinery.

 

Publications

Dalton, A.K., Ako-Adjei, D., Murray, P.S., Murray, D., Vogt, V.M. (2007) Electrostatic interactions drive membrane association of the human immunodeficiency virus type 1 Gag MA domain. J Virol. 81(12):6434-45.

Ako-Adjei, D., Johnson, M.C., Vogt, V.M. (2005) The retroviral capsid domain dictates virion size, morphology, and coassembly of gag into virus-like particles. J Virol.79(21):13463-72.

Johnson, M.C., Spidel, J.L., Ako-Adjei, D., Wills, J.W., Vogt, V.M. (2005) The C-terminal half of TSG101 blocks Rous sarcoma virus budding and sequesters Gag into unique nonendosomal structures. J Virol. 79(6):3775-86.

 

Computercraft
Washington, DC

Email: dansoako@gmail.com


Emory University School of Medicine
Department of Physiology
Atlanta, GA 30322-3110
(404) 727-7410 Office ~ (404) 727-2648 FAX

For questions or comments, contact the webmaster at FIRST@emory.edu.