scholarly journals Prevention of Human Immunodeficiency Virus Type 1 Transmission by Pharmaceuticals Targeted to Host Proteins Required for Virus Infection? Consideration of Farnesyl Thiosalicylic Acid, a Ras Inhibitor

2010 ◽  
Vol 01 (02) ◽  
Author(s):  
A Robert Neurath ◽  
Carol Lackman-Smith
Keyword(s):  
Human Immunodeficiency Virus ◽  
Virus Infection ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Host Proteins ◽  
Thiosalicylic Acid ◽  
Immunodeficiency Virus ◽  
Farnesyl Thiosalicylic Acid

scholarly journals Cholesterol Depletion of Human Immunodeficiency Virus Type 1 and Simian Immunodeficiency Virus with β-Cyclodextrin Inactivates and Permeabilizes the Virions: Evidence for Virion-Associated Lipid Rafts

2003 ◽  
Vol 77 (15) ◽  
pp. 8237-8248 ◽  
Author(s):  
David R. M. Graham ◽  
Elena Chertova ◽  
Joanne M. Hilburn ◽  
Larry O. Arthur ◽  
James E. K. Hildreth
Keyword(s):  
Human Immunodeficiency Virus ◽  
Lipid Rafts ◽  
Simian Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Viral Rna ◽  
Host Proteins ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT Recent evidence suggests that human immunodeficiency virus type 1 (HIV-1) particles assemble and bud selectively through areas in the plasma membrane of cells that are highly enriched with glycosylphosphatidylinositol-anchored proteins and cholesterol, called lipid rafts. Since cholesterol is required to maintain lipid raft structure and function, we proposed that virion-associated cholesterol removal with the compound 2-hydroxy-propyl-β-cyclodextrin (β-CD) might be disruptive to HIV-1 and simian immunodeficiency virus (SIV). We examined the effect of β-CD on the structure and infectivity of cell-free virions. We found that β-CD inactivated HIV-1 and SIV in a dose-dependent manner and permeabilized the viral membranes, resulting in the loss of mature Gag proteins (capsid, matrix, nucleocapsid, p1, and p6) without loss of the envelope glycoproteins. SIV also lost reverse transcriptase (RT), integrase (IN), and viral RNA. IN appeared to be only slightly diminished in HIV-1, and viral RNA, RT, matrix, and nucleocapsid proteins were retained in HIV-1 but to a much lesser degree. Host proteins located internally in the virus (actin, moesin, and ezrin) and membrane-associated host proteins (major histocompatibility complex classes I and II) remained associated with the treated virions. Electron microscopy revealed that under conditions that permeabilized the viruses, holes were present in the viral membranes and the viral core structure was perturbed. These data provide evidence that an intact viral membrane is required to maintain mature virion core integrity. Since the viruses were not fixed before β-CD treatment and intact virion particles were recovered, the data suggest that virions may possess a protein scaffold that can maintain overall structure despite disruptions in membrane integrity.

scholarly journals Inhibitory role of CXCR4 glycan in CD4-independent X4-tropic human immunodeficiency virus type 1 infection and its abrogation in CD4-dependent infection

2007 ◽  
Vol 88 (11) ◽  
pp. 3139-3144 ◽  
Author(s):  
Yoshinao Kubo ◽  
Masaru Yokoyama ◽  
Hiroaki Yoshii ◽  
Chiho Mitani ◽  
Chika Tominaga ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Virus Infection ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Viral Envelope ◽  
Extracellular Region ◽  
Immunodeficiency Virus ◽  
Env Protein ◽  
Hiv 1

CXCR4 functions as an infection receptor of X4 human immunodeficiency virus type 1 (HIV-1) . CXCR4 is glycosylated at the N-terminal extracellular region, which is important for viral envelope (Env) protein binding. We compared the effects of CXCR4 glycan on the CD4-dependent and –independent infections in human cells by X4 viruses. We found that transduction mediated by Env proteins of CD4-independent HIV-1 strains increased up to 5.5-fold in cells expressing unglycosylated CXCR4, suggesting that the CXCR4 glycan inhibits CD4-independent X4 virus infection. Co-expression of CD4 on the target cell surface or pre-incubation of virus particles with soluble CD4 abrogates the glycan-mediated inhibition of X4 virus infection, suggesting that interaction of Env protein with CD4 counteracts the inhibition. These findings indicate that it will be advantageous for X4 HIV-1 to remain CD4-dependent. A structural model that explains the glycan-mediated inhibition is discussed.

scholarly journals Hepatitis G Virus Infection in Human Immunodeficiency Virus Type 1‐Infected Mothers and Their Children

1998 ◽  
Vol 178 (3) ◽  
pp. 862-865 ◽  
Author(s):  
Maurizio de Martino ◽  
Chiara Azzari ◽  
Massimo Resti ◽  
Maria Moriondo ◽  
Maria Elisabetta Rossi ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Virus Infection ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Hepatitis G Virus ◽  
Immunodeficiency Virus ◽  
Hepatitis G

TT virus infection in human immunodeficiency virus type 1 infected mothers and their infants

2000 ◽  
Vol 61 (3) ◽  
pp. 347-351 ◽  
Author(s):  
Maurizio de Martino ◽  
Maria Moriondo ◽  
Chiara Azzari ◽  
Massimo Resti ◽  
Luisa Galli ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Virus Infection ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Tt Virus ◽  
Immunodeficiency Virus
Sign in / Sign up

Export Citation Format

Share Document