Journal
VACCINE
Volume 26, Issue 24, Pages 3026-3035Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.vaccine.2007.12.026
Keywords
HIV; membrane fusion; membrane rafts; FRAP; lateral mobility; CD4; chemokine receptors; HIV gp120; HIV gp41; cholesterol; sphingomyelin; glycosphingolipids; six-helix bundle
Categories
Funding
- Intramural NIH HHS [Z01 BC008303-35, Z01 BC010652-03, Z99 CA999999] Funding Source: Medline
- NCI NIH HHS [N01CO12400, N01-CO-12400] Funding Source: Medline
Ask authors/readers for more resources
Our overall goal is to understand how viral envelope proteins mediate membrane fusion and pathogenesis. Membrane fusion is a crucial step in the delivery of the viral genome into the cell resulting in infection. On the other hand, fusion activity of viral envelope glycoproteins expressed in infected cells may cause the demise of uninfected bystander cells by apoptosis. Our general approach is to kinetically resolve steps in the pathway of viral. envelope glycoprotein-mediated membrane fusion and to uncover physical parameters undertying those steps using a variety of biochemical, biophysical, virological, and molecular and cell biotogical. techniques. Since HIV fusion involves a comptex cascade of interactions of the envelope glycoprotein with two receptors, membrane organization plays an important rote and interfering with it may modulate entry. To study this phenomenon, we have either examined cell, lines with differential expression of sphingolipids (such as GM3), or altered membrane organization by modifying levels of cholesterol, ceramides, or gtycosphingolipids. We show that the localized plasma membrane lipid microenvironment (and not the specific membrane lipids) in the vicinity of CD4 controls receptor mobitity and HIV-1 fusion. The complex cascade of
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available