Structural and functional properties of the membranotropic HIV-1 glycoprotein gp41 loop region are modulated by its intrinsic hydrophobic core

Jiayin Qiu; Avraham Ashkenazi; Shuwen Liu; Yechiel Shai

doi:10.1074/jbc.M113.496646

Structural and functional properties of the membranotropic HIV-1 glycoprotein gp41 loop region are modulated by its intrinsic hydrophobic core

Jiayin Qiu
, Avraham Ashkenazi
, Shuwen Liu
, Yechiel Shai

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

4 Scopus citations

Abstract

Background:HIV-1 infectivity is decreased by specific mutations that alter the hydrophobicity level in the HIV-1 gp41 loop core. Results:Antibody recognition, disulfide-bond formation, and lipid mixing of loop domain peptides are strongly affected by these mutations. Conclusion:The hydrophobic core maintains proper function and structure of the loop region. Significance:A better understanding of the membrane fusion mechanism of HIV and similar viruses is provided.

Original language	English
Pages (from-to)	29143-29150
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	288
Issue number	40
DOIs	https://doi.org/10.1074/jbc.M113.496646
State	Published - 4 Oct 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1074/jbc.M113.496646

Cite this

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title = "Structural and functional properties of the membranotropic HIV-1 glycoprotein gp41 loop region are modulated by its intrinsic hydrophobic core",

abstract = "Background:HIV-1 infectivity is decreased by specific mutations that alter the hydrophobicity level in the HIV-1 gp41 loop core. Results:Antibody recognition, disulfide-bond formation, and lipid mixing of loop domain peptides are strongly affected by these mutations. Conclusion:The hydrophobic core maintains proper function and structure of the loop region. Significance:A better understanding of the membrane fusion mechanism of HIV and similar viruses is provided.",

author = "Jiayin Qiu and Avraham Ashkenazi and Shuwen Liu and Yechiel Shai",

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T1 - Structural and functional properties of the membranotropic HIV-1 glycoprotein gp41 loop region are modulated by its intrinsic hydrophobic core

AU - Qiu, Jiayin

AU - Ashkenazi, Avraham

AU - Liu, Shuwen

AU - Shai, Yechiel

PY - 2013/10/4

Y1 - 2013/10/4

N2 - Background:HIV-1 infectivity is decreased by specific mutations that alter the hydrophobicity level in the HIV-1 gp41 loop core. Results:Antibody recognition, disulfide-bond formation, and lipid mixing of loop domain peptides are strongly affected by these mutations. Conclusion:The hydrophobic core maintains proper function and structure of the loop region. Significance:A better understanding of the membrane fusion mechanism of HIV and similar viruses is provided.

AB - Background:HIV-1 infectivity is decreased by specific mutations that alter the hydrophobicity level in the HIV-1 gp41 loop core. Results:Antibody recognition, disulfide-bond formation, and lipid mixing of loop domain peptides are strongly affected by these mutations. Conclusion:The hydrophobic core maintains proper function and structure of the loop region. Significance:A better understanding of the membrane fusion mechanism of HIV and similar viruses is provided.

UR - https://www.scopus.com/pages/publications/84885098420

U2 - 10.1074/jbc.M113.496646

DO - 10.1074/jbc.M113.496646

M3 - Article

C2 - 23960077

AN - SCOPUS:84885098420

SN - 0021-9258

VL - 288

SP - 29143

EP - 29150

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 40

ER -

Structural and functional properties of the membranotropic HIV-1 glycoprotein gp41 loop region are modulated by its intrinsic hydrophobic core

Abstract

ASJC Scopus subject areas

UN SDGs

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