The possible involvement of CXCR4 in the inhibition of HIV-1 infection mediated by DP178/gp41

Younong Xu; Xiaoyan Zhang; Masao Matsuoka; Toshio Hattori

doi:10.1016/S0014-5793(00)02336-X

The possible involvement of CXCR4 in the inhibition of HIV-1 infection mediated by DP178/gp41

Younong Xu, Xiaoyan Zhang, Masao Matsuoka, Toshio Hattori

International Research Institute of Disaster Science (IRIDeS)

Research output: Contribution to journal › Article › peer-review

18 Citations (Scopus)

Abstract

The N- (N36/DP107) and C-terminal peptides (C34/DP178) from two α-helical domains of human immunodeficiency virus type 1 (HIV-1) gp41 inhibited HIV infection. A single-round infection using pseudotyped virus clarified that a greater amount of gp41-derived peptides was necessary for the inhibition of R5 virus (ADA) infection than for that of X4 virus (LAI) infection. Furthermore, R5X4 virus (89.6) infection via CCR5 needs more peptides for inhibition than its infection via CXCR4 does. A high sensitivity of X4 virus was partially ascribed to the inhibition of the 12G5 binding to CXCR4 by DP178LAI.

Original language	English
Pages (from-to)	185-188
Number of pages	4
Journal	FEBS Letters
Volume	487
Issue number	2
DOIs	https://doi.org/10.1016/S0014-5793(00)02336-X
Publication status	Published - 2000 Dec 29

Keywords

R5 virus
R5X4 virus
X4 virus
gp41-derived peptide

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

UN SDGs

This output contributes to the following Sustainable Development Goal(s)

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title = "The possible involvement of CXCR4 in the inhibition of HIV-1 infection mediated by DP178/gp41",

abstract = "The N- (N36/DP107) and C-terminal peptides (C34/DP178) from two α-helical domains of human immunodeficiency virus type 1 (HIV-1) gp41 inhibited HIV infection. A single-round infection using pseudotyped virus clarified that a greater amount of gp41-derived peptides was necessary for the inhibition of R5 virus (ADA) infection than for that of X4 virus (LAI) infection. Furthermore, R5X4 virus (89.6) infection via CCR5 needs more peptides for inhibition than its infection via CXCR4 does. A high sensitivity of X4 virus was partially ascribed to the inhibition of the 12G5 binding to CXCR4 by DP178LAI.",

keywords = "R5 virus, R5X4 virus, X4 virus, gp41-derived peptide",

author = "Younong Xu and Xiaoyan Zhang and Masao Matsuoka and Toshio Hattori",

note = "Funding Information: This work was supported by Grants-in-Aid from the Ministry of Education, Science, Sports, and Culture of Japan and the Scientific Research Expenses for Health and Welfare Program from the Ministry of Health and Welfare, Japan. The authors are grateful to Dr. D. Littman for providing U87.CD4.CCR5 and U87.CD4.CXCR4 cells, pNL4-3-Luc-E − R − , and psp272-89.6, Dr. C. Weiss for providing pSMADA and pSMHXB-2, Dr. A. Koito for providing SF162, Dr. A. Adachi for providing pNL432. The authors thank Dr. N. Fujii (Graduate School of Pharmaceutical Sciences, Kyoto University) for the generous gift of synthetic T22. The authors thank Dr. Y. Maeda for providing CEM-CCR5. The authors are also indebted to Dr. J.A. Hoxie for 12G5 and to LeukoSite, Inc. for the 2D7 monoclonal antibodies from the NIH AIDS Research and Reference Program.",

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day = "29",

doi = "10.1016/S0014-5793(00)02336-X",

language = "English",

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pages = "185--188",

journal = "FEBS Letters",

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AU - Xu, Younong

AU - Zhang, Xiaoyan

AU - Matsuoka, Masao

AU - Hattori, Toshio

N1 - Funding Information: This work was supported by Grants-in-Aid from the Ministry of Education, Science, Sports, and Culture of Japan and the Scientific Research Expenses for Health and Welfare Program from the Ministry of Health and Welfare, Japan. The authors are grateful to Dr. D. Littman for providing U87.CD4.CCR5 and U87.CD4.CXCR4 cells, pNL4-3-Luc-E − R − , and psp272-89.6, Dr. C. Weiss for providing pSMADA and pSMHXB-2, Dr. A. Koito for providing SF162, Dr. A. Adachi for providing pNL432. The authors thank Dr. N. Fujii (Graduate School of Pharmaceutical Sciences, Kyoto University) for the generous gift of synthetic T22. The authors thank Dr. Y. Maeda for providing CEM-CCR5. The authors are also indebted to Dr. J.A. Hoxie for 12G5 and to LeukoSite, Inc. for the 2D7 monoclonal antibodies from the NIH AIDS Research and Reference Program.

PY - 2000/12/29

Y1 - 2000/12/29

N2 - The N- (N36/DP107) and C-terminal peptides (C34/DP178) from two α-helical domains of human immunodeficiency virus type 1 (HIV-1) gp41 inhibited HIV infection. A single-round infection using pseudotyped virus clarified that a greater amount of gp41-derived peptides was necessary for the inhibition of R5 virus (ADA) infection than for that of X4 virus (LAI) infection. Furthermore, R5X4 virus (89.6) infection via CCR5 needs more peptides for inhibition than its infection via CXCR4 does. A high sensitivity of X4 virus was partially ascribed to the inhibition of the 12G5 binding to CXCR4 by DP178LAI.

AB - The N- (N36/DP107) and C-terminal peptides (C34/DP178) from two α-helical domains of human immunodeficiency virus type 1 (HIV-1) gp41 inhibited HIV infection. A single-round infection using pseudotyped virus clarified that a greater amount of gp41-derived peptides was necessary for the inhibition of R5 virus (ADA) infection than for that of X4 virus (LAI) infection. Furthermore, R5X4 virus (89.6) infection via CCR5 needs more peptides for inhibition than its infection via CXCR4 does. A high sensitivity of X4 virus was partially ascribed to the inhibition of the 12G5 binding to CXCR4 by DP178LAI.

KW - R5 virus

KW - R5X4 virus

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The possible involvement of CXCR4 in the inhibition of HIV-1 infection mediated by DP178/gp41

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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