Molecular Requirements for Self-Interaction of the Respiratory Syncytial Virus Matrix Protein in Living Mammalian Cells

Marta Trevisan; Veronica Di Antonio; Annalisa Radeghieri; Giorgio Palù; Reena Ghildyal; Gualtiero Alvisi

doi:10.3390/v10030109

Molecular Requirements for Self-Interaction of the Respiratory Syncytial Virus Matrix Protein in Living Mammalian Cells

Marta Trevisan, Veronica Di Antonio, Annalisa Radeghieri, Giorgio Palù, Reena Ghildyal, Gualtiero Alvisi

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Abstract

Respiratory syncytial virus (RSV) is an important human pathogen, which infects respiratory tract epithelial cells causing bronchiolitis and pneumonia in children and the elderly. Recent studies have linked RSV matrix (M) ability to self-interaction and viral budding. However, RSV M has been crystalized both as a monomer and a dimer, and no formal proof exists to date that it forms dimers in cells. Here, by using a combination of confocal laser scanning microscopy and bioluminescent resonant energy transfer applied to differently tagged deletion mutants of RSV M, we show that the protein can self-interact in living mammalian cells and that both the N and C-terminus of the protein are strictly required for the process, consistent with the reported dimeric crystal structure.

Original language	English
Article number	109
Pages (from-to)	1-13
Number of pages	13
Journal	Viruses
Volume	10
Issue number	3
DOIs	https://doi.org/10.3390/v10030109
Publication status	Published - 3 Mar 2018

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ArticleFinal published version, 2.29 MBLicence: CC BY

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title = "Molecular Requirements for Self-Interaction of the Respiratory Syncytial Virus Matrix Protein in Living Mammalian Cells",

abstract = "Respiratory syncytial virus (RSV) is an important human pathogen, which infects respiratory tract epithelial cells causing bronchiolitis and pneumonia in children and the elderly. Recent studies have linked RSV matrix (M) ability to self-interaction and viral budding. However, RSV M has been crystalized both as a monomer and a dimer, and no formal proof exists to date that it forms dimers in cells. Here, by using a combination of confocal laser scanning microscopy and bioluminescent resonant energy transfer applied to differently tagged deletion mutants of RSV M, we show that the protein can self-interact in living mammalian cells and that both the N and C-terminus of the protein are strictly required for the process, consistent with the reported dimeric crystal structure.",

keywords = "Bioluminescence resonance energy transfer (BRET), Confocal microscopy, RSV M protein, Virus assembly",

author = "Marta Trevisan and {Di Antonio}, Veronica and Annalisa Radeghieri and Giorgio Pal{\`u} and Reena Ghildyal and Gualtiero Alvisi",

note = "Funding Information: This work was supported by the Ministero dell{\textquoteright}Istruzione, Universit{\`a} e Ricerca MURST EX60% to Gualtiero Alvisi. Plasmid pCDNA3.1-RSV M (1–256), encoding for codon optimized M, was a generous gift from Monika Bajorek (INRA, France). Publisher Copyright: {\textcopyright} 2018 by the authors. Licensee MDPI, Basel, Switzerland.",

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doi = "10.3390/v10030109",

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AU - Trevisan, Marta

AU - Di Antonio, Veronica

AU - Radeghieri, Annalisa

AU - Palù, Giorgio

AU - Ghildyal, Reena

AU - Alvisi, Gualtiero

N1 - Funding Information: This work was supported by the Ministero dell’Istruzione, Università e Ricerca MURST EX60% to Gualtiero Alvisi. Plasmid pCDNA3.1-RSV M (1–256), encoding for codon optimized M, was a generous gift from Monika Bajorek (INRA, France). Publisher Copyright: © 2018 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2018/3/3

Y1 - 2018/3/3

N2 - Respiratory syncytial virus (RSV) is an important human pathogen, which infects respiratory tract epithelial cells causing bronchiolitis and pneumonia in children and the elderly. Recent studies have linked RSV matrix (M) ability to self-interaction and viral budding. However, RSV M has been crystalized both as a monomer and a dimer, and no formal proof exists to date that it forms dimers in cells. Here, by using a combination of confocal laser scanning microscopy and bioluminescent resonant energy transfer applied to differently tagged deletion mutants of RSV M, we show that the protein can self-interact in living mammalian cells and that both the N and C-terminus of the protein are strictly required for the process, consistent with the reported dimeric crystal structure.

AB - Respiratory syncytial virus (RSV) is an important human pathogen, which infects respiratory tract epithelial cells causing bronchiolitis and pneumonia in children and the elderly. Recent studies have linked RSV matrix (M) ability to self-interaction and viral budding. However, RSV M has been crystalized both as a monomer and a dimer, and no formal proof exists to date that it forms dimers in cells. Here, by using a combination of confocal laser scanning microscopy and bioluminescent resonant energy transfer applied to differently tagged deletion mutants of RSV M, we show that the protein can self-interact in living mammalian cells and that both the N and C-terminus of the protein are strictly required for the process, consistent with the reported dimeric crystal structure.

KW - Bioluminescence resonance energy transfer (BRET)

KW - Confocal microscopy

KW - RSV M protein

KW - Virus assembly

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M3 - Article

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JO - Viruses

JF - Viruses

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ER -

Molecular Requirements for Self-Interaction of the Respiratory Syncytial Virus Matrix Protein in Living Mammalian Cells

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