HIV-1 gp41 by N-domain binds the potential receptor protein P45

Yi Xiao; Weicheng Wu; Manfred P. Dierich; Ying Hua Chen

doi:10.1159/000024325

HIV-1 gp41 by N-domain binds the potential receptor protein P45

Yi Xiao, Weicheng Wu, Manfred P. Dierich, Ying Hua Chen

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

8 Scopus citations

Abstract

Recent crystal structure analysis of HIV-1 gp41 revealed that two domains (N- and C-domains) on gp41 play an important role in mediating membrane fusion and HIV-1 entry. The experimental evidence that gp41 by N-domain bound the potential receptor protein P45 could help to understand the mechanism of HIV entry. A recombinant soluble gp41 (rsgp41: Env aa539-684) could bind to P45 in the affinity capillary electrophoresis analysis and the surface plasmon resonance assay. In a blockade assay, peptide P1 (Env aa583-599) could inhibit interaction between rsgp41 and P45, while a control peptide could not. Direct binding of rsgp41, rgp41DP (aa567-648), P1 peptide and (P1)₂ peptide [(aa586-596)₂] to P45 was examined in an ELISA assay. Rsgp41 bound the potential receptor protein P45 strongly, while rgp41DP and P1 as well as (P1)₂ could all weakly bind to P45, indicating that gp41 by N-domain weakly binds P45 and the region RILAVERYLKD located in the N-domain is defined as the binding site for P45 binding. Copyright (C) 2000 S. Karger AG. Basel.

Original language	English (US)
Pages (from-to)	253-257
Number of pages	5
Journal	International Archives of Allergy and Immunology
Volume	121
Issue number	3
DOIs	https://doi.org/10.1159/000024325
State	Published - 2000
Externally published	Yes

Keywords

Binding site
HIV-1 gp41
N-domain
Potential receptor protein

ASJC Scopus subject areas

Immunology and Allergy
Immunology

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10.1159/000024325

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title = "HIV-1 gp41 by N-domain binds the potential receptor protein P45",

abstract = "Recent crystal structure analysis of HIV-1 gp41 revealed that two domains (N- and C-domains) on gp41 play an important role in mediating membrane fusion and HIV-1 entry. The experimental evidence that gp41 by N-domain bound the potential receptor protein P45 could help to understand the mechanism of HIV entry. A recombinant soluble gp41 (rsgp41: Env aa539-684) could bind to P45 in the affinity capillary electrophoresis analysis and the surface plasmon resonance assay. In a blockade assay, peptide P1 (Env aa583-599) could inhibit interaction between rsgp41 and P45, while a control peptide could not. Direct binding of rsgp41, rgp41DP (aa567-648), P1 peptide and (P1)2 peptide [(aa586-596)2] to P45 was examined in an ELISA assay. Rsgp41 bound the potential receptor protein P45 strongly, while rgp41DP and P1 as well as (P1)2 could all weakly bind to P45, indicating that gp41 by N-domain weakly binds P45 and the region RILAVERYLKD located in the N-domain is defined as the binding site for P45 binding. Copyright (C) 2000 S. Karger AG. Basel.",

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T1 - HIV-1 gp41 by N-domain binds the potential receptor protein P45

AU - Xiao, Yi

AU - Wu, Weicheng

AU - Dierich, Manfred P.

AU - Chen, Ying Hua

PY - 2000

Y1 - 2000

N2 - Recent crystal structure analysis of HIV-1 gp41 revealed that two domains (N- and C-domains) on gp41 play an important role in mediating membrane fusion and HIV-1 entry. The experimental evidence that gp41 by N-domain bound the potential receptor protein P45 could help to understand the mechanism of HIV entry. A recombinant soluble gp41 (rsgp41: Env aa539-684) could bind to P45 in the affinity capillary electrophoresis analysis and the surface plasmon resonance assay. In a blockade assay, peptide P1 (Env aa583-599) could inhibit interaction between rsgp41 and P45, while a control peptide could not. Direct binding of rsgp41, rgp41DP (aa567-648), P1 peptide and (P1)2 peptide [(aa586-596)2] to P45 was examined in an ELISA assay. Rsgp41 bound the potential receptor protein P45 strongly, while rgp41DP and P1 as well as (P1)2 could all weakly bind to P45, indicating that gp41 by N-domain weakly binds P45 and the region RILAVERYLKD located in the N-domain is defined as the binding site for P45 binding. Copyright (C) 2000 S. Karger AG. Basel.

AB - Recent crystal structure analysis of HIV-1 gp41 revealed that two domains (N- and C-domains) on gp41 play an important role in mediating membrane fusion and HIV-1 entry. The experimental evidence that gp41 by N-domain bound the potential receptor protein P45 could help to understand the mechanism of HIV entry. A recombinant soluble gp41 (rsgp41: Env aa539-684) could bind to P45 in the affinity capillary electrophoresis analysis and the surface plasmon resonance assay. In a blockade assay, peptide P1 (Env aa583-599) could inhibit interaction between rsgp41 and P45, while a control peptide could not. Direct binding of rsgp41, rgp41DP (aa567-648), P1 peptide and (P1)2 peptide [(aa586-596)2] to P45 was examined in an ELISA assay. Rsgp41 bound the potential receptor protein P45 strongly, while rgp41DP and P1 as well as (P1)2 could all weakly bind to P45, indicating that gp41 by N-domain weakly binds P45 and the region RILAVERYLKD located in the N-domain is defined as the binding site for P45 binding. Copyright (C) 2000 S. Karger AG. Basel.

KW - Binding site

KW - HIV-1 gp41

KW - N-domain

KW - Potential receptor protein

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HIV-1 gp41 by N-domain binds the potential receptor protein P45

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