Ghalib Alkhatib, Ph.D.
Professor, Department of Biomedical Sciences and Center of Excellence for Infectious Diseases
Department of Biomedical Sciences
Center of Excellence for Infectious Diseases
Texas Tech University Health Sciences Center
5001 El Paso Drive, El Paso TX, Zip Code 79905
Phone: (915) 783-1241 x.301
Education and Training
- B.Sc., 1979: Pahlavi (Shiraz) University, Shiraz, Iran
- Ph.D., 1989: McGill University, Montreal, Quebec
- PostDoctoral, 1988-1990 Mammalian Cell Genetics Group, Genetic Engineering Section, Biotechnology Research Institute, National Research Council Canada, MontrÃ©al, QuÃ©bec, Canada
- PostDoctoral, 1990-1993 Department of Molecular Immunology & Neurobiology, Mount Sinai Hospital Research Institute, Toronto, Canada
- Visiting Fellow, 1995-1998 Laboratory of Viral Diseases, NIAID, National Institutes of Health, Bethesda, Maryland
1997-2002 Assistant Professor, Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, Indiana
2003-2010 Associate Professor, Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, Indiana
2010-Present Professor, Department of Biomedical Sciences and Center of Excellence for Infectious Diseases, Paul L. Foster School of Medicine, Texas Tech University Health Sciences Center, El Paso, Texas
Summary of the focus of the research of Dr. Alkhatib
Studies in this laboratory are focused on the molecular determinants involved in retrovirus infection. Our research is directed at understanding how interactions of HIV-1 (AIDS virus) and HTLV-1 (human T cell leukemia virus) envelope glycoproteins with host cell receptors lead to membrane fusion and viral entry. Analyzing the mechanisms of retroviral entry is a key step in the development of anti-viral agents (please see video clip for detailed mechanism of entry).
Description and summary of research focus of the laboratory
The AIDS project focuses on the mechanisms of genetic resistance to HIV-1 infection. HIV-1 requires CD4 and a coreceptor (CCR5 or CXCR4) for entry into susceptible host cells. CCR5 and CXCR4 belong to the family of seven transmebrane spanner proteins. A naturally occurring frame-shift mutation caused by a 32 base pair deletion (Î”32) in the human CCR5 gene is highly associated with protection against HIV-1. CCR5Î”32 is a loss-of-function mutation that abolishes cell surface expression of the HIV coreceptor CCR5 and provides resistance to HIV-1 infection. Our results suggest that at least two distinct mechanisms may account for genetic resistance to HIV-1 conferred by CCR5Î”32; loss of wild type CCR5 surface expression, and generation of CCR5Î”32 truncated protein, which functions as a scavenger of both CCR5 and CXCR4. Understanding how CCR5Î”32 interacts with the HIV coreceptors will lead to novel findings concerning coreceptor structure-function that may be utilized for the design of drugs that mimic the CCR5Î”32 activity.
It has been previously determined that the erythrocyte glucose transporter protein (GLUT-1) as a cellular receptor for HTLV-1. Studies are underway to analyze the molecular determinants involved in HTLV-1 tropism and infection. The GLUT-1 receptor is a multi-spanner membrane protein that crosses the plasma membrane 12 times. The common use by HIV-1 and HTLV-1 of these multi-spanning membrane proteins may lead to the identification of common retroviral entry mechanisms and may lead to design of drugs that inhibit retroviral entry.