Abstract
We compared the anti-HIV-1 activity of CC-chemokine LD78beta with that of MIP-1alpha, another CC-chemokine which shows 94% sequence homology with LD78beta. Despite its close similarity to MIP-1alpha, the anti-HIV-1 activity of LD78beta appeared to be nearly 10 times higher than that of MIP-1alpha. Mutagenesis of MIP-1alpha showed that the N-terminal additional tetrapeptide, which was present in LD78beta and absent in MIP-1alpha, is responsible for enhanced anti-HIV-1 activity. The N-terminal structure-function relationship of LD78beta described here will be of value in understanding the chemokine-receptor interactions and designing anti-HIV-1 compounds based on LD78beta.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Anti-HIV Agents / metabolism
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Anti-HIV Agents / pharmacology*
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CD4 Antigens / metabolism
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Chemokine CCL3
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Chemokine CCL4
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Chemokines / metabolism
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Chemokines / pharmacology
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Dipeptidyl Peptidase 4 / metabolism
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Genetic Vectors
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HIV-1 / drug effects*
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Haplorhini
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Humans
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Leukocytes, Mononuclear / cytology
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Leukocytes, Mononuclear / metabolism
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Macrophage Inflammatory Proteins / metabolism
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Macrophage Inflammatory Proteins / pharmacology*
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Peptides / metabolism
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Peptides / pharmacology
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Respirovirus / genetics
Substances
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Anti-HIV Agents
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CD4 Antigens
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Chemokine CCL3
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Chemokine CCL4
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Chemokines
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Macrophage Inflammatory Proteins
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Peptides
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Dipeptidyl Peptidase 4