Insights into the function of ESCRT and its role in enveloped virus infection
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 bila...
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Frontiers Media S.A.
2023-10-01
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Series: | Frontiers in Microbiology |
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Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2023.1261651/full |
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author | Chunxuan Wang Yu Chen Shunlin Hu Xiufan Liu Xiufan Liu Xiufan Liu |
author_facet | Chunxuan Wang Yu Chen Shunlin Hu Xiufan Liu Xiufan Liu Xiufan Liu |
author_sort | Chunxuan Wang |
collection | DOAJ |
description | 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. |
first_indexed | 2024-03-11T19:42:08Z |
format | Article |
id | doaj.art-138f4c7cc0ba44ec92d7978bdc2ef2ed |
institution | Directory Open Access Journal |
issn | 1664-302X |
language | English |
last_indexed | 2024-03-11T19:42:08Z |
publishDate | 2023-10-01 |
publisher | Frontiers Media S.A. |
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series | Frontiers in Microbiology |
spelling | doaj.art-138f4c7cc0ba44ec92d7978bdc2ef2ed2023-10-06T07:31:19ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2023-10-011410.3389/fmicb.2023.12616511261651Insights into the function of ESCRT and its role in enveloped virus infectionChunxuan Wang0Yu Chen1Shunlin Hu2Xiufan Liu3Xiufan Liu4Xiufan Liu5Animal Infectious Disease Laboratory, College of Veterinary Medicine, Yangzhou University, Yangzhou, ChinaAnimal Infectious Disease Laboratory, College of Veterinary Medicine, Yangzhou University, Yangzhou, ChinaAnimal Infectious Disease Laboratory, College of Veterinary Medicine, Yangzhou University, Yangzhou, ChinaAnimal Infectious Disease Laboratory, College of Veterinary Medicine, Yangzhou University, Yangzhou, ChinaJiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonosis, Yangzhou University, Yangzhou, ChinaJiangsu Key Laboratory of Zoonosis, Yangzhou University, Yangzhou, ChinaThe 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.https://www.frontiersin.org/articles/10.3389/fmicb.2023.1261651/fullESCRTMVBSenveloped virusviral entryviral buddingviral replication |
spellingShingle | Chunxuan Wang Yu Chen Shunlin Hu Xiufan Liu Xiufan Liu Xiufan Liu Insights into the function of ESCRT and its role in enveloped virus infection Frontiers in Microbiology ESCRT MVBS enveloped virus viral entry viral budding viral replication |
title | Insights into the function of ESCRT and its role in enveloped virus infection |
title_full | Insights into the function of ESCRT and its role in enveloped virus infection |
title_fullStr | Insights into the function of ESCRT and its role in enveloped virus infection |
title_full_unstemmed | Insights into the function of ESCRT and its role in enveloped virus infection |
title_short | Insights into the function of ESCRT and its role in enveloped virus infection |
title_sort | insights into the function of escrt and its role in enveloped virus infection |
topic | ESCRT MVBS enveloped virus viral entry viral budding viral replication |
url | https://www.frontiersin.org/articles/10.3389/fmicb.2023.1261651/full |
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