HIV-1 entry: Duels between Env and host antiviral transmembrane proteins on the surface of virus particles

Murakami, Tomoyuki; Ono, Akira

doi:10.1016/j.coviro.2021.07.005

Cited by 8 publications

(7 citation statements)

References 132 publications

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“…Collectively, Env exhibits a high capacity to undergo conformational switching events upon interacting with host cells, which are essential for virus entry and immune evasion during HIV-1 infection life cycle. Thus, a better understanding of conformational changes and dynamics of native Env on infectious viruses will inform the development of HIV-1 prevention and treatment strategies, such as vaccines, antibodies, and small-molecule inhibitors 1,[7][8][9][10] .…”

Section: Introductionmentioning

confidence: 99%

“…Thus, Env is one of the major targets for designing vaccines, antibodies, and antiviral drugs. Env interacts with the host cellular receptor CD4 and coreceptor CCR5/CXCR4 to mediate viral membrane fusion into target cells through a series of large-scale conformational changes [1][2][3][4][5][6][7][8][9][10] . Functional Env is a homotrimer-of-heterodimer consisting of gp120 exterior subunits and gp41 transmembrane subunits [11][12][13][14][15][16] .…”

Section: Introductionmentioning

confidence: 99%

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An intact amber-free HIV-1 system for in-virus protein bioorthogonal click labeling that delineates envelope conformational dynamics

Grover

Han

et al. 2023

Preprint

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The HIV-1 envelope (Env) glycoprotein is conformationally dynamic and mediates membrane fusion required for cell entry. Single-molecule fluorescence resonance energy transfer (smFRET) of Env using peptide tags has provided mechanistic insights into the dynamics of Env conformations. Nevertheless, using peptide tags risks potential effects on structural integrity. Here, we aim to establish minimally invasive smFRET systems of Env on the virus by combining genetic code expansion and bioorthogonal click chemistry. Amber stop-codon suppression allows site-specifically incorporating noncanonical/unnatural amino acids (ncAAs) at introduced amber sites into proteins. However, ncAA incorporation into Env (or other HIV-1 proteins) in the virus context has been challenging due to low copies of Env on virions and incomplete amber suppression in mammalian cells. Here, we developed an intact amber-free virus system that overcomes impediments from preexisting ambers in HIV-1. Using this system, we successfully incorporated dual ncAAs at amber-introduced sites into Env on intact virions. Dual-ncAA incorporated Env retained similar neutralization sensitivities to neutralizing antibodies as wildtype. smFRET of click-labeled Env on intact amber-free virions recapitulated conformational profiles of Env. The amber-free HIV-1 infectious system also permits in-virus protein bioorthogonal labeling, compatible with various advanced microscopic studies of virus entry, trafficking, and egress in living cells.Amber-free HIV-1 infectious systems actualized minimal invasive Env tagging for smFRET, versatile for in-virus bioorthogonal click labeling in advanced microscopic studies of virus-host interactions.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

An intact amber-free HIV-1 system for in-virus protein bioorthogonal click labeling that delineates envelope conformational dynamics

Grover

Han

et al. 2023

Preprint

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“…For bacteria, ROS preferentially attacks the phospholipid bilayer and lipopolysaccharide of the bacterial cell membrane, and oxidizes unsaturated fatty acids on the cell membrane to form lipid-peroxyl radicals [ 148 ]. For enveloped viruses, the components of the envelope are similar to those of bacterial cell membranes, both composed of a phospholipid bilayer and glycoproteins [ 149 ], so that ROS can also damage the viral envelope. Upon passage through the viral envelope, ROS can significantly interfere with protein function, including altering protein structure, oxidizing amino acids, modifying sulfur groups, and carbonylation [ 150 , 151 ].…”

Section: Potential Antiviral Mechanisms At Physicochemical Levelmentioning

confidence: 99%

Chemical Nature of Metals and Metal-Based Materials in Inactivation of Viruses

Tian

Yin

et al. 2022

Nanomaterials

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In response to the enormous threat to human survival and development caused by the large number of viruses, it is necessary to strengthen the defense against and elimination of viruses. Metallic materials have been used against viruses for thousands of years due to their broad-spectrum antiviral properties, wide sources and excellent physicochemical properties; in particular, metal nanoparticles have advanced biomedical research. However, researchers in different fields hold dissimilar views on the antiviral mechanisms, which has slowed down the antiviral application of metal nanoparticles. As such, this review begins with an exhaustive compilation of previously published work on the antiviral capacity of metal nanoparticles and other materials. Afterwards, the discussion is centered on the antiviral mechanisms of metal nanoparticles at the biological and physicochemical levels. Emphasis is placed on the fact that the strong reducibility of metal nanoparticles may be the main reason for their efficient inactivation of viruses. We hope that this review will benefit the promotion of metal nanoparticles in the antiviral field and expedite the construction of a barrier between humans and viruses.

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“…Anti-viral transmembrane proteins are also incorporated into progeny virions. SERINC3 and SERINC5 restrict HIV-1 fusion when these proteins are incorporated into virions [7][8][9][10]. Virion-incorporated IFITM proteins also suppress the fusion of HIV-1 [10][11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

“…SERINC3 and SERINC5 restrict HIV-1 fusion when these proteins are incorporated into virions [7][8][9][10]. Virion-incorporated IFITM proteins also suppress the fusion of HIV-1 [10][11][12][13][14]. Therefore, virus-incorporated host transmembrane proteins can have broad impacts, either positive or negative, on HIV-1 spread.…”

Section: Introductionmentioning

confidence: 99%

Roles of Virion-Incorporated CD162 (PSGL-1), CD43, and CD44 in HIV-1 Infection of T Cells

Murakami

Ono

2021

Viruses

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Nascent HIV-1 particles incorporate the viral envelope glycoprotein and multiple host transmembrane proteins during assembly at the plasma membrane. At least some of these host transmembrane proteins on the surface of virions are reported as pro-viral factors that enhance virus attachment to target cells or facilitate trans-infection of CD4+ T cells via interactions with non-T cells. In addition to the pro-viral factors, anti-viral transmembrane proteins are incorporated into progeny virions. These virion-incorporated transmembrane proteins inhibit HIV-1 entry at the point of attachment and fusion. In infected polarized CD4+ T cells, HIV-1 Gag localizes to a rear-end protrusion known as the uropod. Regardless of cell polarization, Gag colocalizes with and promotes the virion incorporation of a subset of uropod-directed host transmembrane proteins, including CD162, CD43, and CD44. Until recently, the functions of these virion-incorporated proteins had not been clear. Here, we review the recent findings about the roles played by virion-incorporated CD162, CD43, and CD44 in HIV-1 spread to CD4+ T cells.

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HIV-1 entry: Duels between Env and host antiviral transmembrane proteins on the surface of virus particles

Cited by 8 publications

References 132 publications

An intact amber-free HIV-1 system for in-virus protein bioorthogonal click labeling that delineates envelope conformational dynamics

An intact amber-free HIV-1 system for in-virus protein bioorthogonal click labeling that delineates envelope conformational dynamics

Chemical Nature of Metals and Metal-Based Materials in Inactivation of Viruses

Roles of Virion-Incorporated CD162 (PSGL-1), CD43, and CD44 in HIV-1 Infection of T Cells

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