Dr. Kenneth Samuel
Program Director, MBRS-SCORE
Professor
Department of Biology
Dixon Science Research Center, Room 205
School of Computer, Mathematical and Natural Sciences
Morgan State University
1700 E. Coldspring Lane
Baltimore, Maryland 21251

Dixon 206
(tel) 443-885-4005
(lab) 443-885-1361
(fax) 443-885-8285
ksamuel@moac.morgan.edu

Biographical Sketch (cv)

Dr. Samuel was a Postdoctoral Research Fellow in Professor Paul Marks’ laboratory in the Department of Human Genetics and Development at Columbia University in New York, from 1978-1980. He later trained at the National Cancer Institute, National Institutes of Health in Bethesda, Maryland, from 1980-1985 in the laboratory of the late Dr. Takis S. Papas under a Fogarty International Fellowship. He became a Scientist with the Program Resources, Incorporated, at the Frederick Cancer Research and Development Center in Frederick, Maryland, from 1985-1990, and Senior Scientist and Head of the Biotechnology Working Group at SAIC at the Frederick Cancer Research and Development Center, Frederick, Maryland, from 1990-1995. Dr. Samuel joined the Department of Biology in 1995, served as the Acting Department Chair from 1998-2000, and became Program Director of the MBRS SCORE Program in June, 2002.

Dr. Samuel is the recipient of both a United States and Canadian patents for a diagnostic test for the human T-Lymphotropic Virus Type 1 (HTLV-1).

Research Interest

The major focus of our research has been centered on investigating structure-function relationships of conserved sequence motifs within two relatively small HIV-1 accessory gene products, the Nef and Vpu proteins, with the goal of understanding molecular mechanisms and defining function. It is well established that Nef protein is involved in modulating cellular signaling events and in maintaining high virus load that leads to disease pathogenesis in vivo. Similarly, Vpu is necessary for virus maturation and release, and for degradation of CD4 in the endoplasmic reticulum. Despite significant progress made in understanding structure-function relationships of Nef and Vpu, major challenges still remain in defining molecular mechanisms.

Thematically, current research interests and projects in the laboratory are directed toward understanding structure-function relationships of two conserved sequence motifs: one involves the role of a carboxyl-terminal sequence in mediating subcellular localization and distribution of Vpu in the cell; and the other is a conserved carboxyl-terminal tyrosine-based motif that could potentially serve as a docking site for interaction of Nef with cellular signaling partners. Understanding mechanisms of Vpu’s retention in the endoplasmic reticulum and role of retention for function, and interference of Nef with cellular signaling dysfunction, could provide insights for novel drug intervention to block their function.

The group is utilizing a variety of standard molecular, cellular, and biochemical techniques, as well as proteomic and computational applications and tools in its research.

Recent Publications

1. Hodge, D. R., Chen, Y.-M.A., and Samuel, K. P.:Oligomerication Of The HIV Type 2 Nef Protein: Mutational Analysis Of The Heptad Leucine Repeat Motif And Cysteine Residues. AIDS Research And Human Retroviruses 11: 65-79, 1995.
2. Kondoh,N., Noda,M., Fisher, R.J., Schweinfest, C.W., Papas, T.S., Kondoh, A., Samuel, K. P., and Oikawa, T. : The S29 ribosomal protein increases tumor suppressor activity of K rev-1 gene on v-K ras-transformed NIH3T3 cells. Biochimica et Biophysica Acta 1313: 41-46, 1996.
3. Hodge, D.R., Dunn, K.J., Pei, G.K., Chakrabarty, M.K., Heidecker, G., Lautenberger, J.A., and Samuel, K.P.: Binding of c-Raf1 Kinase to a Conserved Acidic Sequence within the Carboxy-Terminal Region of the HIV-1 Nef Protein. J. Biol. Chem., 273: 15727-15733, 1998.
4. Hartz, P.A., McMiller, T., Scott-Wright, D., and Samuel, K.P.: Low Level Expression of the HIV-1 Nef Protein In Transiently Transfected COS-1 Cells In Culture. Cellular And Molecular Biology, 49: 1101-1107, 2003.