A snapshot of HIV-1 capsid–host interactions

Temple, Joshua; Tripler, Therese; Shen, Qijun; Xiong, Yong

doi:10.1016/j.crstbi.2020.10.002

Cited by 30 publications

(39 citation statements)

References 42 publications

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“…Restriction of HIV infection depends also on the NTE, to some extent on the MxB GTPase function, and on its dimerization (Buffone et al ., 2015; Fricke et al ., 2014; Goujon et al ., 2014; Schulte et al ., 2015; Xie et al ., 2021). It will be interesting to determine whether MxB only competes for important HIV interactions with promoting host factors (reviewed in Temple et al ., 2020), or whether it also induces HIV capsid disassembly.…”

Section: Discussionmentioning

confidence: 99%

The interferon-inducible GTPase MxB promotes capsid disassembly and genome release of herpesviruses

Sodeik

Serrero²,

Girault

et al. 2022

Preprint

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Host proteins sense viral products and induce defence mechanisms, particularly in immune cells. Using cell-free assays and quantitative mass spectrometry, we determined the interactome of capsid-host protein complexes of herpes simplex virus and identified the large dynamin-like GTPase myxovirus resistance protein B (MxB) as an interferon-inducible protein interacting with capsids. Electron microscopy analyses showed that cytosols containing MxB had the remarkable capability to disassemble the icosahedral capsids of herpes simplex viruses and varicella zoster virus into flat sheets of connected triangular faces. In contrast, capsids remained intact in cytosols with MxB mutants unable to hydrolyse GTP or to dimerize. Our data suggest that MxB senses herpesviral capsids, mediates their disassembly, and thereby restricts the efficiency of nuclear targeting of incoming capsids and/or the assembly of progeny capsids. The resulting premature release of viral genomes from capsids may enhance the activation of DNA sensors, and thereby amplify the innate immune responses.

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Section: Discussionmentioning

confidence: 99%

The interferon-inducible GTPase MxB promotes capsid disassembly and genome release of herpesviruses

Sodeik

Serrero²,

Girault

et al. 2022

Preprint

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“…During the assembly and budding of HIV-1, several host factors remain associated with the newly emerging viruses [62][63][64]. These virus-associated or encapsidated host proteins may influence the infectivity of the virus population and decide the fate of disease progression [65][66][67]. Since Staufen-1, one such protein, is known to be packaged in several RNA viruses and acts as a positive effector for viral infectivity [12,14,35], here we comprehensively analyzed the viral packaging efficiency of Staufen-2, especially in HIV-1 for the first time.…”

Section: Discussionmentioning

confidence: 99%

Encapsidation of Staufen-2 Enhances Infectivity of HIV-1

Balakrishnan

Vasudevan

Mohareer

et al. 2021

Viruses

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Staufen, the RNA-binding family of proteins, affects various steps in the Human Immuno-Deficiency Virus (HIV-1) replication cycle. While our previous study established Staufen-2–HIV-1 Rev interaction and its role in augmenting nucleocytoplasmic export of RRE-containing viral RNA, viral incorporation of Staufen-2 and its effect on viral propagation were unknown. Here, we report that Staufen-2 interacts with HIV-1 Gag and is incorporated into virions and that encapsidated Staufen-2 boosted viral infectivity. Further, Staufen-2 gets co-packaged into virions, possibly by interacting with host factors Staufen-1 or antiviral protein APOBEC3G, which resulted in different outcomes on the infectivity of Staufen-2-encapsidated virions. These observations suggest that encapsidated host factors influence viral population dynamics and infectivity. With the explicit identification of the incorporation of Staufen proteins into HIV-1 and other retroviruses, such as Simian Immunodeficiency Virus (SIV), we propose that packaging of RNA binding proteins, such as Staufen, in budding virions of retroviruses is probably a general phenomenon that can drive or impact the viral population dynamics, infectivity, and evolution.

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“…The nature of the mechanism governing the location and timing of uncoating remains a pivotal question. Several studies suggest a correlation between capsid stability, uncoating, and viral infectivity [ 57 , 58 , 59 , 60 , 61 ]. Furthermore, capsid uncoating and reverse transcription are thought to be coupled.…”

Section: The Mechanics Of Virus Uncoatingmentioning

confidence: 99%

Applications of Atomic Force Microscopy in HIV-1 Research

Rousso

Deshpande

2022

Viruses

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Obtaining an understanding of the mechanism underlying the interrelations between the structure and function of HIV-1 is of pivotal importance. In previous decades, this mechanism was addressed extensively in a variety of studies using conventional approaches. More recently, atomic force microscopy, which is a relatively new technique with unique capabilities, has been utilized to study HIV-1 biology. Atomic force microscopy can generate high-resolution images at the nanometer-scale and analyze the mechanical properties of individual HIV-1 virions, virus components (e.g., capsids), and infected live cells under near-physiological environments. This review describes the working principles and various imaging and analysis modes of atomic force microscopy, and elaborates on its distinctive contributions to HIV-1 research in areas such as mechanobiology and the physics of infection.

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A snapshot of HIV-1 capsid–host interactions

Cited by 30 publications

References 42 publications

The interferon-inducible GTPase MxB promotes capsid disassembly and genome release of herpesviruses

The interferon-inducible GTPase MxB promotes capsid disassembly and genome release of herpesviruses

Encapsidation of Staufen-2 Enhances Infectivity of HIV-1

Applications of Atomic Force Microscopy in HIV-1 Research

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