TITLE

Pertussis Toxin and Its Binding Unit Inhibit HIV-1 Infection of Human Cervical Tissue and Macrophages Involving a CD14 Pathway

AUTHOR(S)
Qinxue Hu; Younson, Justine; Griffin, George E.; Kelly, Charles; Shattock, Robin J.
PUB. DATE
December 2006
SOURCE
Journal of Infectious Diseases;12/1/2006, Vol. 194 Issue 11, p1547
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Pertussis toxin (PTX) and its binding unit (PTX-B) have been shown to inhibit human immunodeficiency virus (HIV)—1 infection of primary cells. However, the anti-HIV mechanisms have yet to be defined. We demonstrate that PTX inhibits HIV-1 infection of human cervical tissue independently of viral tropism. PTXB showed a similar pattern of HIV-1 inhibition. Further investigation in macrophages demonstrated that PTX/ PTX-B inhibited HIV-1 expression but that other G protein inhibitors and activators had no effect on HIV-1 replication. Unlike the anti-HIV bacterial lipopolysaccharide, the anti-HIV effects of PTX/PTX-B were not due to β-chemokine production or coreceptor down-modulation, but they were dependent on interaction with cell-surface receptors. Antibody blocking studies suggested that cell-surface CD14 is very likely to be the principal receptor involved in the anti-HIV effects of PTX/PTX-B. This was further strengthened by the results of surface plasmon resonance analyses. Further definition of the mechanisms of such inhibition may lead to the development of novel HIV-1 prevention strategies.
ACCESSION #
23082506

 

Related Articles

  • The phosphorylation of HIV-1 Gag by atypical protein kinase C facilitates viral infectivity by promoting Vpr incorporation into virions. Ayumi Kudoh; Shoukichi Takahama; Tatsuya Sawasaki; Hirotaka Ode; Masaru Yokoyama; Akiko Okayama; Akiyo Ishikawa; Kei Miyakawa; Satoko Matsunaga; Hirokazu Kimura; Wataru Sugiura; Hironori Sato; Hisashi Hirano; Shigeo Ohno; Naoki Yamamoto; Akihide Ryo // Retrovirology; 

    Background Human immunodeficiency virus type 1 (HIV-1) Gag is the main structural protein that mediates the assembly and release of virus-like particles (VLPs) from an infected cell membrane. The Gag C-terminal p6 domain contains short sequence motifs that facilitate virus release from the...

  • Can India avoid being devastated by HIV? Ramasundaram, S // BMJ: British Medical Journal (International Edition);01/26/2002, Vol. 324 Issue 7331, p182 

    Editorial. Comments on the HIV epidemic in India. Number of HIV-infected people in the country; Need for effective and sustained prevention efforts; Concern that rising HIV rates will fuel the epidemic of tuberculosis; Need for the prevention of unprotected heterosexual intercourse with an...

  • Native and Genetically Inactivated Pertussis Toxins Induce Human Dendritic Cell Maturation and Synergize with Lipopolysaccharide in Promoting T Helper Type 1 Responses. Ausiello, Clara M.; Fedele, Giorgio; Urbani, Francesca; Lande, Roberto; Di Carlo, Beatrice; Cassone, Antonio // Journal of Infectious Diseases;8/1/2002, Vol. 186 Issue 3, p351 

    The capacity of pertussis toxin (PT) to induce maturation and functional activities of human monocyte-derived dendritic cells (DCs) was investigated. Both native PT (nPT) and genetically detoxified PT (dPT) efficiently promoted expression on DCs of CD80, CD86, human leukocyte antigen-DR, and...

  • The SET Complex Acts as a Barrier to Autointegration of HIV-1. Nan Yan; Cherepanov, Peter; Daigle, Janet E.; Engelman, Alan; Lieberman, Judy // PLoS Pathogens;Mar2009, Vol. 5 Issue 3, p1 

    Retroviruses and retrotransposons are vulnerable to a suicidal pathway known as autointegration, which occurs when the 3′-ends of the reverse transcript are activated by integrase and then attack sites within the viral DNA. Retroelements have diverse strategies for suppressing...

  • Class II Transactivator (CIITA) Enhances Cytoplasmic Processing of HIV-1 Pr55Gag. Porter, Kristen A.; Kelley, Lauren N.; George, Annette; Harton, Jonathan A.; Duus, Karen M. // PLoS ONE;2010, Vol. 5 Issue 6, p1 

    Background: The Pr55gag (Gag) polyprotein of HIV serves as a scaffold for virion assembly and is thus essential for progeny virion budding and maturation. Gag localizes to the plasma membrane (PM) and membranes of late endosomes, allowing for release of infectious virus directly from the cell...

  • Cells of the Macrophage Lineage and their Role in the Pathogenesis of HIV-1 Infection: An Update. Kedzierska, Katherine; Maslin, Clare L. V.; Crowe, Suzanne M. // Medicinal Chemistry Reviews - Online;Jul2004, Vol. 1 Issue 3, p351 

    Cells of macrophage lineage contribute to the pathogenesis of HIV-1 infection throughout the course of disease. Blood monocytes and tissue macrophages can be infected with HIV-1 in vivo and in vitro. In contrast to tissue macrophages, which are highly susceptible to HIV-1 infection, blood...

  • Critical roles for Akt kinase in controlling HIV envelope-mediated depletion of CD4 T cells. Haishan Li; Pauza, C. David // Retrovirology;2013, Vol. 10 Issue 1, p1 

    Background: The cell surface receptors CD4 and CCR5 bind CCR5-tropic HIV Envelope (Env) glycoprotein during virus attachment. These same receptors have signaling activities related to normal immune cell functions. We also know that Env binds to CCR5 present at high levels on CD4-negative...

  • Molecular architecture of native HIV-1 gp120 trimers. Jun Liu; Bartesaghi, Alberto; Borgnia, Mario J.; Sapiro, Guillermo; Subramaniam, Sriram // Nature;9/4/2008, Vol. 455 Issue 7209, p109 

    The envelope glycoproteins (Env) of human and simian immunodeficiency viruses (HIV and SIV, respectively) mediate virus binding to the cell surface receptor CD4 on target cells to initiate infection. Env is a heterodimer of a transmembrane glycoprotein (gp41) and a surface glycoprotein (gp120),...

  • Efficient trapping of HIV-1 envelope protein by hetero-oligomerization with an N-helix chimera. Wu Ou; Silver, Jonathan // Retrovirology;2005, Vol. 2, p51 

    Background: The N-heptad repeat region of the HIV-1 Transmembrane Envelope protein is a trimerization domain that forms part of a "six helix bundle" crucial to Envelope-mediated membrane fusion. N-heptad repeat peptides have been used as extracellular reagents to inhibit virus fusion. Results:...

Share

Read the Article

Courtesy of VIRGINIA BEACH PUBLIC LIBRARY AND SYSTEM

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics