Enhanced anti-HIV-1 activity of CC-chemokine LD78beta, a non-allelic variant of MIP-1alpha/LD78alpha.
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.
Xin
X
X
Department of Viral Infection, Institute of Medical Science, University of Tokyo, Tokyo, Japan.
Shioda
T
T
Kato
A
A
Liu
H
H
Sakai
Y
Y
Nagai
Y
Y
D000818:Animals; D019380:Anti-HIV Agents / Q000378:metabolism / Q000494:pharmacology*; D015704:CD4 Antigens / Q000378:metabolism; D054405:Chemokine CCL3; D054407:Chemokine CCL4; D018925:Chemokines / Q000378:metabolism / Q000494:pharmacology; D018819:Dipeptidyl Peptidase 4 / Q000378:metabolism; D005822:Genetic Vectors; D015497:HIV-1 / Q000187:drug effects*; D000882:Haplorhini; D006801:Humans; D007963:Leukocytes, Mononuclear / Q000166:cytology / Q000378:metabolism; D019402:Macrophage Inflammatory Proteins / Q000378:metabolism / Q000494:pharmacology*; D010455:Peptides / Q000378:metabolism / Q000494:pharmacology; D018108:Respirovirus / Q000235:genetics
D019380:Anti-HIV Agents; D015704:CD4 Antigens; D054405:Chemokine CCL3; D054407:Chemokine CCL4; D018925:Chemokines; D019402:Macrophage Inflammatory Proteins; D010455:Peptides; D018819:Dipeptidyl Peptidase 4