Lipid biosensor interactions with wild type and matrix deletion HIV-1 Gag proteins

Eric Barklis, August O. Staubus, Andrew Mack, Logan Harper, Robin Lid Barklis, Ayna Alfadhli

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The matrix (MA) domain of the HIV-1 precursor Gag protein (PrGag) has been shown interact with the HIV-1 envelope (Env) protein, and to direct PrGag proteins to plasma membrane (PM) assembly sites by virtue of its affinity to phosphatidylinositol-4,5-bisphosphate (PI[4,5]P2). Unexpectedly, HIV-1 viruses with large MA deletions (ΔMA) have been shown to be conditionally infectious as long as they are matched with Env truncation mutant proteins or alternative viral glycoproteins. To characterize the interactions of wild type (WT) and ΔMA Gag proteins with PI(4,5)P2 and other acidic phospholipids, we have employed a set of lipid biosensors as probes. Our investigations showed marked differences in WT and ΔMA Gag colocalization with biosensors, effects on biosensor release, and association of biosensors with virus-like particles. These results demonstrate an alternative approach to the analysis of viral protein-lipid associations, and provide new data as to the lipid compositions of HIV-1 assembly sites.

Original languageEnglish (US)
Pages (from-to)264-271
Number of pages8
JournalVirology
Volume518
DOIs
StatePublished - May 1 2018

Fingerprint

gag Gene Products
Biosensing Techniques
HIV-1
Lipids
Viral Proteins
Mutant Proteins
Phosphatidylinositols
Virion
Phospholipids
Glycoproteins
Proteins
Cell Membrane
Viruses

Keywords

  • Gag
  • HIV-1
  • Lipid biosensors
  • Matrix
  • Phospholipids

ASJC Scopus subject areas

  • Virology

Cite this

Lipid biosensor interactions with wild type and matrix deletion HIV-1 Gag proteins. / Barklis, Eric; Staubus, August O.; Mack, Andrew; Harper, Logan; Barklis, Robin Lid; Alfadhli, Ayna.

In: Virology, Vol. 518, 01.05.2018, p. 264-271.

Research output: Contribution to journalArticle

Barklis, Eric ; Staubus, August O. ; Mack, Andrew ; Harper, Logan ; Barklis, Robin Lid ; Alfadhli, Ayna. / Lipid biosensor interactions with wild type and matrix deletion HIV-1 Gag proteins. In: Virology. 2018 ; Vol. 518. pp. 264-271.
@article{7550de15657a4cabb48692c98a113278,
title = "Lipid biosensor interactions with wild type and matrix deletion HIV-1 Gag proteins",
abstract = "The matrix (MA) domain of the HIV-1 precursor Gag protein (PrGag) has been shown interact with the HIV-1 envelope (Env) protein, and to direct PrGag proteins to plasma membrane (PM) assembly sites by virtue of its affinity to phosphatidylinositol-4,5-bisphosphate (PI[4,5]P2). Unexpectedly, HIV-1 viruses with large MA deletions (ΔMA) have been shown to be conditionally infectious as long as they are matched with Env truncation mutant proteins or alternative viral glycoproteins. To characterize the interactions of wild type (WT) and ΔMA Gag proteins with PI(4,5)P2 and other acidic phospholipids, we have employed a set of lipid biosensors as probes. Our investigations showed marked differences in WT and ΔMA Gag colocalization with biosensors, effects on biosensor release, and association of biosensors with virus-like particles. These results demonstrate an alternative approach to the analysis of viral protein-lipid associations, and provide new data as to the lipid compositions of HIV-1 assembly sites.",
keywords = "Gag, HIV-1, Lipid biosensors, Matrix, Phospholipids",
author = "Eric Barklis and Staubus, {August O.} and Andrew Mack and Logan Harper and Barklis, {Robin Lid} and Ayna Alfadhli",
year = "2018",
month = "5",
day = "1",
doi = "10.1016/j.virol.2018.03.004",
language = "English (US)",
volume = "518",
pages = "264--271",
journal = "Virology",
issn = "0042-6822",
publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - Lipid biosensor interactions with wild type and matrix deletion HIV-1 Gag proteins

AU - Barklis, Eric

AU - Staubus, August O.

AU - Mack, Andrew

AU - Harper, Logan

AU - Barklis, Robin Lid

AU - Alfadhli, Ayna

PY - 2018/5/1

Y1 - 2018/5/1

N2 - The matrix (MA) domain of the HIV-1 precursor Gag protein (PrGag) has been shown interact with the HIV-1 envelope (Env) protein, and to direct PrGag proteins to plasma membrane (PM) assembly sites by virtue of its affinity to phosphatidylinositol-4,5-bisphosphate (PI[4,5]P2). Unexpectedly, HIV-1 viruses with large MA deletions (ΔMA) have been shown to be conditionally infectious as long as they are matched with Env truncation mutant proteins or alternative viral glycoproteins. To characterize the interactions of wild type (WT) and ΔMA Gag proteins with PI(4,5)P2 and other acidic phospholipids, we have employed a set of lipid biosensors as probes. Our investigations showed marked differences in WT and ΔMA Gag colocalization with biosensors, effects on biosensor release, and association of biosensors with virus-like particles. These results demonstrate an alternative approach to the analysis of viral protein-lipid associations, and provide new data as to the lipid compositions of HIV-1 assembly sites.

AB - The matrix (MA) domain of the HIV-1 precursor Gag protein (PrGag) has been shown interact with the HIV-1 envelope (Env) protein, and to direct PrGag proteins to plasma membrane (PM) assembly sites by virtue of its affinity to phosphatidylinositol-4,5-bisphosphate (PI[4,5]P2). Unexpectedly, HIV-1 viruses with large MA deletions (ΔMA) have been shown to be conditionally infectious as long as they are matched with Env truncation mutant proteins or alternative viral glycoproteins. To characterize the interactions of wild type (WT) and ΔMA Gag proteins with PI(4,5)P2 and other acidic phospholipids, we have employed a set of lipid biosensors as probes. Our investigations showed marked differences in WT and ΔMA Gag colocalization with biosensors, effects on biosensor release, and association of biosensors with virus-like particles. These results demonstrate an alternative approach to the analysis of viral protein-lipid associations, and provide new data as to the lipid compositions of HIV-1 assembly sites.

KW - Gag

KW - HIV-1

KW - Lipid biosensors

KW - Matrix

KW - Phospholipids

UR - http://www.scopus.com/inward/record.url?scp=85046021428&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85046021428&partnerID=8YFLogxK

U2 - 10.1016/j.virol.2018.03.004

DO - 10.1016/j.virol.2018.03.004

M3 - Article

C2 - 29549788

AN - SCOPUS:85046021428

VL - 518

SP - 264

EP - 271

JO - Virology

JF - Virology

SN - 0042-6822

ER -