15 A Processing Protease for gp 160 HIV-1 Envelope Glycoprotein Precursor in Human T4+ Lymphocytes

2015 ◽  
pp. 199-212
Author(s):  
Hiroshi Kido ◽  
Keiichi Kamoshita ◽  
Nobuhiko Katunuma
Keyword(s):  
Envelope Glycoprotein ◽  
Glycoprotein Precursor ◽  
Processing Protease ◽  
Hiv 1

scholarly journals Structural insights into the conformational plasticity of the full-length trimeric HIV-1 envelope glycoprotein precursor

2018 ◽  
Author(s):  
Shijian Zhang ◽  
Wei Li Wang ◽  
Shuobing Chen ◽  
Maolin Lu ◽  
Eden P. Go ◽  
...  
Keyword(s):  
Viral Entry ◽  
Envelope Glycoprotein ◽  
Structural Data ◽  
Full Length ◽  
Heptad Repeat ◽  
Structural Basis ◽  
Glycoprotein Precursor ◽  
Helix Bundle ◽  
Conformational Plasticity ◽  
Hiv 1

SummaryThe human immunodeficiency virus (HIV-1) envelope glycoprotein (Env) trimer mediates viral entry into cells and is the major target for the host antibody response. In infected cells, the mature Env [(gp120/gp41)3] is produced by cleavage of a trimeric gp160 precursor. Proteolytic cleavage decreases Env conformational flexibility, allowing the mature Env to resist antibody binding to conserved elements. The conformational plasticity of the Env precursor skews the humoral immune response towards the elicitation of ineffectual antibodies, contributing to HIV-1 persistence in the infected host. The structural basis for the plasticity of the Env precursor remains elusive. Here we use cryo-electron microscopy to visualize two coexisting conformational states of the full-length Env precursor at nominal resolutions of 5.5 and 8.0 Å. The State-P2 conformation features a three-helix bundle of the gp41 heptad repeat region in the core, but has disordered membrane-interactive regions. State-P1 trimers lack the three-helix bundle and instead retain ordered transmembrane and membrane-proximal external regions embracing a central cavity. Our structural data shed light on the unusual plasticity of the Env precursor and provide new clues to Env immunogen discovery.

scholarly journals Proteolytic Processing of the Human Immunodeficiency Virus Envelope Glycoprotein Precursor Decreases Conformational Flexibility

2012 ◽  
Vol 87 (3) ◽  
pp. 1884-1889 ◽  
Author(s):  
Hillel Haim ◽  
Ignacio Salas ◽  
Joseph Sodroski
Keyword(s):  
Human Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Conformational Flexibility ◽  
Proteolytic Processing ◽  
Virus Envelope ◽  
Glycoprotein Precursor ◽  
Trimeric Complex ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACTThe mature envelope glycoprotein (Env) spike on the surface of human immunodeficiency virus type 1 (HIV-1) virions is derived by proteolytic cleavage of a trimeric gp160 glycoprotein precursor. Remarkably, proteolytic processing of the HIV-1 Env precursor results in changes in Env antigenicity that resemble those associated with glutaraldehyde fixation. Apparently, proteolytic processing of the HIV-1 Env precursor decreases conformational flexibility of the Env trimeric complex, differentially affecting the integrity/accessibility of epitopes for neutralizing and nonneutralizing antibodies.

Identification of Membrane Anchorage Domains of the HIV-1 gp160 Envelope Glycoprotein Precursor

1991 ◽  
Vol 4 (1) ◽  
pp. 34???40 ◽  
Author(s):  
Dana Gabuzda ◽  
Udy Olshevsky ◽  
Philip Bertani ◽  
William A. Haseltine ◽  
Joseph Sodroski
Keyword(s):  
Envelope Glycoprotein ◽  
Glycoprotein Precursor ◽  
Hiv 1

scholarly journals Antigenic characterization of the human immunodeficiency virus (HIV-1) envelope glycoprotein precursor incorporated into nanodiscs

PLoS ONE ◽  
2017 ◽  
Vol 12 (2) ◽  
pp. e0170672 ◽  
Author(s):  
Kristen C. Witt ◽  
Luis Castillo-Menendez ◽  
Haitao Ding ◽  
Nicole Espy ◽  
Shijian Zhang ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Glycoprotein Precursor ◽  
Antigenic Characterization ◽  
Immunodeficiency Virus ◽  
Hiv 1

scholarly journals The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM).

1994 ◽  
Vol 269 (16) ◽  
pp. 12240-12247 ◽  
Author(s):  
E. Decroly ◽  
M. Vandenbranden ◽  
J.M. Ruysschaert ◽  
J. Cogniaux ◽  
G.S. Jacob ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Immunodeficiency Virus ◽  
Hiv 1

scholarly journals Cross-Reactive Antibodies With the Capacity to Mediate HIV-1 Envelope Glycoprotein–Targeted Antibody-Dependent Cellular Cytotoxicity Identified in HIV-2–Infected Individuals

2019 ◽  
Vol 219 (11) ◽  
pp. 1749-1754 ◽  
Author(s):  
Ingrid Karlsson ◽  
Jeanette Linnea Tingstedt ◽  
Gülşen Özkaya Şahin ◽  
Mikkel Hansen ◽  
Zsofia Szojka ◽  
...  
Keyword(s):  
Envelope Glycoprotein ◽  
Cellular Cytotoxicity ◽  
Antibody Dependent Cellular Cytotoxicity ◽  
Hiv 1

scholarly journals Targeting HIV-1 Envelope Glycoprotein Trimers to B Cells by Using APRIL Improves Antibody Responses

2011 ◽  
Vol 86 (5) ◽  
pp. 2488-2500 ◽  
Author(s):  
M. Melchers ◽  
I. Bontjer ◽  
T. Tong ◽  
N. P. Y. Chung ◽  
P. J. Klasse ◽  
...  
Keyword(s):  
B Cells ◽  
Envelope Glycoprotein ◽  
Antibody Responses ◽  
Hiv 1

scholarly journals Short Communication: Virion Aggregation by Neutralizing and Nonneutralizing Antibodies to the HIV-1 Envelope Glycoprotein

2015 ◽  
Vol 31 (11) ◽  
pp. 1160-1165 ◽  
Author(s):  
Marina R. Alexander ◽  
Rogier W. Sanders ◽  
John P. Moore ◽  
Per Johan Klasse
Keyword(s):  
Envelope Glycoprotein ◽  
Short Communication ◽  
Hiv 1
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