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Review
. 2023 Oct 6:14:1261651.
doi: 10.3389/fmicb.2023.1261651. eCollection 2023.

Insights into the function of ESCRT and its role in enveloped virus infection

Chunxuan Wang  1 , Yu Chen  1 , Shunlin Hu  1 , Xiufan Liu  1   2   3
Affiliations
Review

Insights into the function of ESCRT and its role in enveloped virus infection

Chunxuan Wang et al. Front Microbiol. .

Abstract

The endosomal sorting complex required for transport (ESCRT) is an essential molecular machinery in eukaryotic cells that facilitates the invagination of endosomal membranes, leading to the formation of multivesicular bodies (MVBs). It participates in various cellular processes, including lipid bilayer remodeling, cytoplasmic separation, autophagy, membrane fission and re-modeling, plasma membrane repair, as well as the invasion, budding, and release of certain enveloped viruses. The ESCRT complex consists of five complexes, ESCRT-0 to ESCRT-III and VPS4, along with several accessory proteins. ESCRT-0 to ESCRT-II form soluble complexes that shuttle between the cytoplasm and membranes, mainly responsible for recruiting and transporting membrane proteins and viral particles, as well as recruiting ESCRT-III for membrane neck scission. ESCRT-III, a soluble monomer, directly participates in vesicle scission and release, while VPS4 hydrolyzes ATP to provide energy for ESCRT-III complex disassembly, enabling recycling. Studies have confirmed the hijacking of ESCRT complexes by enveloped viruses to facilitate their entry, replication, and budding. Recent research has focused on the interaction between various components of the ESCRT complex and different viruses. In this review, we discuss how different viruses hijack specific ESCRT regulatory proteins to impact the viral life cycle, aiming to explore commonalities in the interaction between viruses and the ESCRT system.

Keywords: ESCRT; MVBS; enveloped virus; viral budding; viral entry; viral replication.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
The main components of the ESCRT complex. ESCRT-0 is a dimer composed of HRS and STAM-1, primarily responsible for recognizing ubiquitinated substrates. ESCRT-I connects to ESCRT-0’s HRS through TSG101. ESCRT-II consists of one EAP45, one EAP30, and two EAP20, forming a “Y” shaped structure. The linkage between ESCRT-I and ESCRT-II is achieved through the connection of VPS28 and EAP45. ESCRT-III assembles into a tight fila-mentous structure on the cell membrane, and ESCRT-II and ESCRT-III recruit CHMP6 through EAP20. The ESCRT-associated protein ALIX is composed of the N-terminal Bro1 domain and the C-terminal proline-rich domain (PRD), located on either side of the “V” shaped central region. Through its Bro1 domain, ALIX recruits TSG101 and CHMP4B. Membrane neck constriction and ESCRT-III disassembly are catalyzed by the ATPase VPS4. The VPS4 complex hydrolyzes ATP to provide energy for thinning the bud neck and for disassembling and recycling ESCRT-III aggre-gates through the central pore.
Figure 2
Figure 2
Molecular mechanism of ESCRT complex. The ESCRT-mediated budding process involves a series of coordinated steps. First, ESCRT-0 recognizes and enriches ubiquitinated substrates to recruit ESCRT-I and initiate its budding process. Then, ESCRT-I and ESCRT-II interact to induce invagination of the endosomal membrane, forming the initial bud. Subsequently, ESCRT-III cleaves the bud neck to release the cargo into the endosomal lumen, completing the budding process. Finally, the VPS4-VTA1 complex uses ATP hydrolysis to provide energy, dissociating the ESCRT-III complex from the endosomal membrane and allowing the recycling of ESCRT machinery and the endosomal membrane to occur.
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Grants and funding

The author(s) declare financial support was received for the research, authorship, and/or publication of this article. This work was supported by the National Natural Science Foundation (32202767), the Earmarked Fund for China Agriculture Research System (CARS-40), and the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD).

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