Mutation of Phenylalanine 23 of Newcastle Disease Virus Matrix Protein Inhibits Virus Release by Disrupting the Interaction between the FPIV L-Domain and Charged Multivesicular Body Protein 4B

Yu, Pei; Xue, Jia; Feng, Delan; Huang, Min; Liang, Rong; Li, Xiao; Zhao, Ye; Zhao, Jing; Zhang, Guozhong

doi:10.1128/spectrum.04116-22

Cited by 5 publications

(3 citation statements)

References 53 publications

(67 reference statements)

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“…Previous studies by Li et al 97 confirmed that the binding between NDV M protein and charged multivesicular body protein (CHMP4) promotes virus replication. Similarly, the study by Pei et al 98 demonstrated that the ESCRT-III complex CHMP4s directly interacts with NDV M protein through the FPIV L domain, independently of TSG101, ESCRT-II, or ALIX as assembly factors. In summary, critical amino acid mutations in the FPIV L domain prevent effective interaction between NDV M protein and CHMP4B, resulting in the stalling of viral sub-particles during membrane budding and leading to defects in NDV release and growth.…”

Section: The Role Of Escrt Machinery In Retroviral Buddingmentioning

confidence: 82%

Insights into the Function of ESCRT and Its Role in Enveloped Virus Infection

Wang¹,

Chen²,

Hu³

et al. 2023

Preprint

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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 remodeling, 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.

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Section: The Role Of Escrt Machinery In Retroviral Buddingmentioning

confidence: 82%

Insights into the Function of ESCRT and Its Role in Enveloped Virus Infection

Wang¹,

Chen²,

Hu³

et al. 2023

Preprint

View full text Add to dashboard Cite

show abstract

“…Previous studies by Li et al (2013) confirmed that the binding between NDV M protein and CHMP4 promotes virus replication. Similarly, the study by Pei et al (Pei et al, 2023) demonstrated that the ESCRT-III complex CHMP4s directly interact with NDV M protein through the FPIV L domain, independently of TSG101, ESCRT-II, or ALIX as assembly factors. In summary, critical amino acid mutations in the FPIV L domain prevent effective interaction between NDV M protein and CHMP4B, resulting in the stalling of viral sub-particles during membrane budding and leading to defects in NDV release and growth.…”

Section: The Role Of Escrt Machinery In Paramyxovirus Buddingmentioning

confidence: 89%

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

Wang,

Chen,

et al. 2023

Front. Microbiol.

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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.

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“…The newly described sequence motifs PLPPV and FPIV have been shown to also provide late domain activity for viral budding of mouse mammary tumor virus (MMTV) and paramyxoviruses, respectively [ 26 – 29 ]. Although the ESCRT proteins recruited through the PLPPV motif remain to be identified, the FPIV motif encoded in Newcastle disease virus matrix protein (M protein) appears to facilitate an interaction with CHMP4B [ 30 ]. Nonetheless, it is well established that viral late domain motifs have evolved to mimic the function of proline-rich motifs that facilitate physiological and structural organization of ESCRT components [ 8 ].…”

Section: Overview Of the Host Endosomal Sorting Complex Required For ...mentioning

confidence: 99%

The multifaceted interactions between pathogens and host ESCRT machinery

Rivera-Cuevas

Carruthers

2023

PLoS Pathog

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The Endosomal Sorting Complex Required for Transport (ESCRT) machinery consists of multiple protein complexes that coordinate vesicle budding away from the host cytosol. ESCRTs function in many fundamental cellular processes including the biogenesis of multivesicular bodies and exosomes, membrane repair and restoration, and cell abscission during cytokinesis. Work over the past 2 decades has shown that a diverse cohort of viruses critically rely upon host ESCRT machinery for virus replication and envelopment. More recent studies reported that intracellular bacteria and the intracellular parasite Toxoplasma gondii benefit from, antagonize, or exploit host ESCRT machinery to preserve their intracellular niche, gain resources, or egress from infected cells. Here, we review how intracellular pathogens interact with the ESCRT machinery of their hosts, highlighting the variety of strategies they use to bind ESCRT complexes using short linear amino acid motifs like those used by ESCRTs to sequentially assemble on target membranes. Future work exposing new mechanisms of this molecular mimicry will yield novel insight of how pathogens exploit host ESCRT machinery and how ESCRTs facilitate key cellular processes.

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Mutation of Phenylalanine 23 of Newcastle Disease Virus Matrix Protein Inhibits Virus Release by Disrupting the Interaction between the FPIV L-Domain and Charged Multivesicular Body Protein 4B

Cited by 5 publications

References 53 publications

Insights into the Function of ESCRT and Its Role in Enveloped Virus Infection

Insights into the Function of ESCRT and Its Role in Enveloped Virus Infection

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

The multifaceted interactions between pathogens and host ESCRT machinery

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