Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion

Research output: Contribution to journalLetter

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Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion. / Gray, Robert D.M.; Albrecht, David; Beerli, Corina; Huttunen, Moona; Cohen, Gary H.; White, Ian J.; Burden, Jemima J.; Henriques, Ricardo; Mercer, Jason.

In: Nature Microbiology, Vol. 4, No. 10, 10.2019, p. 1636-1644.

Research output: Contribution to journalLetter

Harvard

Gray, RDM, Albrecht, D, Beerli, C, Huttunen, M, Cohen, GH, White, IJ, Burden, JJ, Henriques, R & Mercer, J 2019, 'Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion', Nature Microbiology, vol. 4, no. 10, pp. 1636-1644. https://doi.org/10.1038/s41564-019-0488-4

APA

Gray, R. D. M., Albrecht, D., Beerli, C., Huttunen, M., Cohen, G. H., White, I. J., Burden, J. J., Henriques, R., & Mercer, J. (2019). Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion. Nature Microbiology, 4(10), 1636-1644. https://doi.org/10.1038/s41564-019-0488-4

Vancouver

Author

Gray, Robert D.M. ; Albrecht, David ; Beerli, Corina ; Huttunen, Moona ; Cohen, Gary H. ; White, Ian J. ; Burden, Jemima J. ; Henriques, Ricardo ; Mercer, Jason. / Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion. In: Nature Microbiology. 2019 ; Vol. 4, No. 10. pp. 1636-1644.

Bibtex

@article{bb40b861ed0d4edaa44cd8cfa94203ab,
title = "Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion",
abstract = "To achieve efficient binding and subsequent fusion, most enveloped viruses encode between one and five proteins1. For many viruses, the clustering of fusion proteins—and their distribution on virus particles—is crucial for fusion activity2,3. Poxviruses, the most complex mammalian viruses, dedicate 15 proteins to binding and membrane fusion4. However, the spatial organization of these proteins and how this influences fusion activity is unknown. Here, we show that the membrane of vaccinia virus is organized into distinct functional domains that are critical for the efficiency of membrane fusion. Using super-resolution microscopy and single-particle analysis, we found that the fusion machinery of vaccinia virus resides exclusively in clusters at virion tips. Repression of individual components of the fusion complex disrupts fusion-machinery polarization, consistent with the reported loss of fusion activity5. Furthermore, we show that displacement of functional fusion complexes from virion tips disrupts the formation of fusion pores and infection kinetics. Our results demonstrate how the protein architecture of poxviruses directly contributes to the efficiency of membrane fusion, and suggest that nanoscale organization may be an intrinsic property of these viruses to assure successful infection.",
author = "Gray, {Robert D.M.} and David Albrecht and Corina Beerli and Moona Huttunen and Cohen, {Gary H.} and White, {Ian J.} and Burden, {Jemima J.} and Ricardo Henriques and Jason Mercer",
year = "2019",
month = oct,
doi = "10.1038/s41564-019-0488-4",
language = "English",
volume = "4",
pages = "1636--1644",
journal = "Nature Microbiology",
issn = "2058-5276",
publisher = "Nature Publishing Group",
number = "10",

}

RIS

TY - JOUR

T1 - Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion

AU - Gray, Robert D.M.

AU - Albrecht, David

AU - Beerli, Corina

AU - Huttunen, Moona

AU - Cohen, Gary H.

AU - White, Ian J.

AU - Burden, Jemima J.

AU - Henriques, Ricardo

AU - Mercer, Jason

PY - 2019/10

Y1 - 2019/10

N2 - To achieve efficient binding and subsequent fusion, most enveloped viruses encode between one and five proteins1. For many viruses, the clustering of fusion proteins—and their distribution on virus particles—is crucial for fusion activity2,3. Poxviruses, the most complex mammalian viruses, dedicate 15 proteins to binding and membrane fusion4. However, the spatial organization of these proteins and how this influences fusion activity is unknown. Here, we show that the membrane of vaccinia virus is organized into distinct functional domains that are critical for the efficiency of membrane fusion. Using super-resolution microscopy and single-particle analysis, we found that the fusion machinery of vaccinia virus resides exclusively in clusters at virion tips. Repression of individual components of the fusion complex disrupts fusion-machinery polarization, consistent with the reported loss of fusion activity5. Furthermore, we show that displacement of functional fusion complexes from virion tips disrupts the formation of fusion pores and infection kinetics. Our results demonstrate how the protein architecture of poxviruses directly contributes to the efficiency of membrane fusion, and suggest that nanoscale organization may be an intrinsic property of these viruses to assure successful infection.

AB - To achieve efficient binding and subsequent fusion, most enveloped viruses encode between one and five proteins1. For many viruses, the clustering of fusion proteins—and their distribution on virus particles—is crucial for fusion activity2,3. Poxviruses, the most complex mammalian viruses, dedicate 15 proteins to binding and membrane fusion4. However, the spatial organization of these proteins and how this influences fusion activity is unknown. Here, we show that the membrane of vaccinia virus is organized into distinct functional domains that are critical for the efficiency of membrane fusion. Using super-resolution microscopy and single-particle analysis, we found that the fusion machinery of vaccinia virus resides exclusively in clusters at virion tips. Repression of individual components of the fusion complex disrupts fusion-machinery polarization, consistent with the reported loss of fusion activity5. Furthermore, we show that displacement of functional fusion complexes from virion tips disrupts the formation of fusion pores and infection kinetics. Our results demonstrate how the protein architecture of poxviruses directly contributes to the efficiency of membrane fusion, and suggest that nanoscale organization may be an intrinsic property of these viruses to assure successful infection.

UR - http://www.scopus.com/inward/record.url?scp=85068937655&partnerID=8YFLogxK

U2 - 10.1038/s41564-019-0488-4

DO - 10.1038/s41564-019-0488-4

M3 - Letter

C2 - 31285583

AN - SCOPUS:85068937655

VL - 4

SP - 1636

EP - 1644

JO - Nature Microbiology

JF - Nature Microbiology

SN - 2058-5276

IS - 10

ER -