Language:

Selective targeting and clustering of phosphatidylserine lipids by RSV M protein is critical for virus particle production

The Journal of biological chemistry, 2023-11, Vol.299 (11), p.105323-105323, Article 105323 [Peer Reviewed Journal]

2023 The Authors ;Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved. ;Attribution ;2023 The Authors 2023 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1016/j.jbc.2023.105323 ;PMID: 37805138

Full text available

Citations Cited by

Actions
1. Add to My Research
2. Remove from My Research
3. E-mail
4. Print
5. Permalink
6. Citation
7. EasyBib
8. EndNote
9. RefWorks
10. Delicious
11. Export RIS
12. Export BibTeX

Title:
Selective targeting and clustering of phosphatidylserine lipids by RSV M protein is critical for virus particle production
Author: Swain, Jitendriya ; Bierre, Maxime ; Veyrié, Laura ; Richard, Charles-Adrien ; Eleouet, Jean-Francois ; Muriaux, Delphine ; Bajorek, Monika
Subjects: Cell Line, Tumor ; Cell Membrane - metabolism ; Humans ; Life Sciences ; lipid bilayer ; lipid-protein interaction ; LUVs ; M phosphorylation ; membrane lipid ; Membrane Lipids - metabolism ; phosphatidylserine ; Phosphatidylserines - metabolism ; Respiratory Syncytial Virus, Human ; RNA virus ; RSV matrix protein ; Viral Fusion Proteins - metabolism ; Viral Matrix Proteins - genetics ; Viral Matrix Proteins - metabolism ; Virion - metabolism ; Virus Assembly
Is Part Of: The Journal of biological chemistry, 2023-11, Vol.299 (11), p.105323-105323, Article 105323
Description: Human respiratory syncytial virus (RSV) is the leading cause of infantile bronchiolitis in the developed world and of childhood deaths in resource-poor settings. The elderly and the immunosuppressed are also affected. It is a major unmet target for vaccines and antiviral drugs. RSV assembles and buds from the host cell plasma membrane by forming infectious viral particles which are mostly filamentous. A key interaction during RSV assembly is the interaction of the matrix (M) protein with cell plasma membrane lipids forming a layer at assembly sites. Although the structure of RSV M protein dimer is known, it is unclear how the viral M proteins interact with cell membrane lipids, and with which one, to promote viral assembly. Here, we demonstrate that M proteins are able to cluster at the plasma membrane by selectively binding with phosphatidylserine (PS). Our in vitro studies suggest that M binds PS lipid as a dimer and upon M oligomerization, PS clustering is observed. In contrast, the presence of other negatively charged lipids like PI(4, 5)P2 does not enhance M binding beyond control zwitterionic lipids, while cholesterol negatively affects M interaction with membrane lipids. Moreover, we show that the initial binding of the RSV M protein with PS lipids is independent of the cytoplasmic tail of the fusion (F) glycoprotein (FCT). Here, we highlight that M binding on membranes occurs directly through PS lipids, this interaction is electrostatic in nature, and M oligomerization generates PS clusters.
Publisher: United States: Elsevier Inc
Language: English
Identifier: ISSN: 0021-9258
EISSN: 1083-351X
DOI: 10.1016/j.jbc.2023.105323
PMID: 37805138
Source: Hyper Article en Ligne (HAL) (Open Access)
MEDLINE
PubMed Central
Alma/SFX Local Collection
DOAJ

Back to results list


INSPIRE LIBRARY - TON DUC THANG UNIVERSITY	(84-028) 37 755 057	Feedback
19 Nguyen Huu Tho St. Dist.7, HCM	thuvien@tdtu.edu.vn	Feedback

Selective targeting and clustering of phosphatidylserine lipids by RSV M protein is critical for virus particle production

2023 The Authors ;Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved. ;Attribution ;2023 The Authors 2023 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1016/j.jbc.2023.105323 ;PMID: 37805138

Searching Remote Databases, Please Wait