HIV-1 envelope glycoprotein structure

被引：69

作者：

Merk, Alan ^{[1
]}

Subramaniam, Sriram ^{[1
]}

机构：

[1] NCI, Cell Biol Lab, Ctr Canc Res, NIH, Bethesda, MD 20892 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2013年 / 23卷 / 02期

关键词：

VIRUS TYPE-1 GP41; INTERHELICAL INTERACTIONS; CRYOELECTRON TOMOGRAPHY; POTENT NEUTRALIZATION; FUNCTIONAL-ANALYSIS; ATOMIC-STRUCTURE; ANTIBODY; GP120; CORE; MEMBRANE;

D O I：

10.1016/j.sbi.2013.03.007

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The trimeric envelope glycoprotein of HIV-1, composed of gp120 and gp41 subunits, remains a major target for vaccine development. The structures of the core regions of monomeric gp120 and gp41 have been determined previously by X-ray crystallography. New insights into the structure of trimeric HIV-1 envelope glycoproteins are now coming from cryo-electron tomographic studies of the gp120/gp41 trimer as displayed on intact viruses and from cryo-electron microscopic studies of purified, soluble versions of the ectodomain of the trimer. Here, we review recent developments in these fields as they relate to our understanding of the structure and function of HIV-1 envelope glycoproteins.

引用

页码：268 / 276

页数：9

共 50 条

[31] Peptides presenting the binding site of human CD4 for the HIV-1 envelope glycoprotein gp120 [J].

Meier, Julia ;

Kassler, Kristin ;

Sticht, Heinrich ;

Eichler, Jutta .

BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY, 2012, 8 :1858-1866

[32] Antigenic landscape of the HIV-1 envelope and new immunological concepts defined by HIV-1 broadly neutralizing antibodies [J].

Wu, Xueling ;

Kong, Xiang-Peng .

CURRENT OPINION IN IMMUNOLOGY, 2016, 42 :56-64

[33] HIV-1 Envelope and MPER Antibody Structures in Lipid Assemblies [J].

Rantalainen, Kimmo ;

Berndsen, Zachary T. ;

Antanasijevic, Aleksandar ;

Schiffner, Torben ;

Zhang, Xi ;

Lee, Wen-Hsin ;

Torres, Jonathan L. ;

Zhang, Lei ;

Irimia, Adriana ;

Copps, Jeffrey ;

Zhou, Kenneth H. ;

Kwon, Young D. ;

Law, William H. ;

Schramm, Chaim A. ;

Verardi, Raffaello ;

Krebs, Shelly J. ;

Kwong, Peter D. ;

Doria-Rose, Nicole A. ;

Wilson, Ian A. ;

Zwick, Michael B. ;

Yates, John R., III ;

Schief, William R. ;

Ward, Andrew B. .

CELL REPORTS, 2020, 31 (04)

[34] HIV-1 Resistance to Maraviroc Conferred by a CD4 Binding Site Mutation in the Envelope Glycoprotein gp120 [J].

Ratcliff, Annette N. ;

Shi, Wuxian ;

Arts, Eric J. .

JOURNAL OF VIROLOGY, 2013, 87 (02) :923-934

[35] MARCH2 is upregulated in HIV-1 infection and inhibits HIV-1 production through envelope protein translocation or degradation [J].

Zhang, You ;

Lu, Jing ;

Liu, Xinqi .

VIROLOGY, 2018, 518 :293-300

[36] Mutations of Glu560 within HIV-1 Envelope Glycoprotein N-terminal heptad repeat region contribute to resistance to peptide inhibitors of virus entry [J].

Yuan, Chen ;

Wang, Jia-Ye ;

Zhao, Hai-Jiao ;

Li, Yan ;

Li, Di ;

Ling, Hong ;

Zhuang, Min .

RETROVIROLOGY, 2019, 16 (01)

[37] CD4-Induced Antibodies Promote Association of the HIV-1 Envelope Glycoprotein with CD4-Binding Site Antibodies [J].

Gardner, Matthew R. ;

Fellinger, Christoph H. ;

Prasad, Neha R. ;

Zhou, Amber S. ;

Kondur, Hema R. ;

Joshi, Vinita R. ;

Quinlan, Brian D. ;

Farzan, Michael .

JOURNAL OF VIROLOGY, 2016, 90 (17) :7822-7832

[38] Single-molecule imaging of HIV-1 envelope glycoprotein dynamics and Gag lattice association exposes determinants responsible for virus incorporation [J].

Pezeshkian, Nairi ;

Groves, Nicholas S. ;

van Engelenburg, Schuyler B. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2019, 116 (50) :25269-25277

[39] Binding Thermodynamics of the N-Terminal Peptide of the CCR5 Coreceptor to HIV-1 Envelope Glycoprotein gp120 [J].

Brower, Evan T. ;

Schon, Arne ;

Klein, Jeffrey C. ;

Freire, Ernesto .

BIOCHEMISTRY, 2009, 48 (04) :779-785

[40] HIV Entry and Envelope Glycoprotein-mediated Fusion [J].

Blumenthal, Robert ;

Durell, Stewart ;

Viard, Mathias .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2012, 287 (49) :40841-40849

← 1 2 3 4 5 →