Source:http://linkedlifedata.com/resource/pubmed/id/18028978
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-1-15
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pubmed:abstractText |
Following primary infection with human immunodeficiency virus type-1 (HIV-1), macrophages are thought to play an important role, as they are one of the first target cells the virus encounters and can also sustain a significant production of viruses over extended periods of time. While the interaction between the primary cellular receptor CD4 and the virus-encoded external envelope glycoprotein gp120 initiates the infection process, it has been suggested that various host factors are exploited by HIV-1 to facilitate adsorption onto the cell surface. Macrophages and other cells found at the infection site can secrete a soluble mammalian lectin, galectin-1, which binds to beta-galactoside residues through its carbohydrate recognition domain. Being a dimer, galectin-1 can cross-link ligands expressed on different constituents to mediate adhesion between cells or between cells and pathogens. We report here that galectin-1, but not galectin-3, increased HIV-1 infectivity in monocyte-derived macrophages (MDMs). This phenomenon was likely due to an enhancement of virus adsorption kinetics, which facilitates HIV-1 entry. The fusion inhibitors T-20 and TAK779 remained effective at reducing infection even in the presence of galectin-1, indicating that the galectin-1-mediated effect is occurring at a step prior to fusion. Together, our data suggest that galectin-1 can facilitate HIV-1 infection in MDMs by promoting early events of the virus replicative cycle (i.e. adsorption).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
371
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
121-9
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pubmed:meshHeading |
pubmed-meshheading:18028978-Cell Differentiation,
pubmed-meshheading:18028978-Galectin 1,
pubmed-meshheading:18028978-HIV Infections,
pubmed-meshheading:18028978-HIV-1,
pubmed-meshheading:18028978-Humans,
pubmed-meshheading:18028978-Kinetics,
pubmed-meshheading:18028978-Macrophages,
pubmed-meshheading:18028978-Monocytes,
pubmed-meshheading:18028978-Recombinant Proteins,
pubmed-meshheading:18028978-Viruses
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pubmed:year |
2008
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pubmed:articleTitle |
Galectin-1 promotes HIV-1 infectivity in macrophages through stabilization of viral adsorption.
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pubmed:affiliation |
Research Center for Infectious Diseases, CHUL Research Center, Quebec, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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