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Direct observation of membrane insertion by enveloped virus matrix proteins by phosphate displacement.

Neuman BW, Kiss G, Al-Mulla HM, Dokland T, Buchmeier MJ, Weikl T, Schley D - PLoS ONE (2013)

Bottom Line: Enveloped virus release is driven by poorly understood proteins that are functional analogs of the coat protein assemblies that mediate intracellular vesicle trafficking.We used differential electron density mapping to detect membrane integration by membrane-bending proteins from five virus families.This demonstrates that virus matrix proteins replace an unexpectedly large portion of the lipid content of the inner membrane face, a generalized feature likely to play a role in reshaping cellular membranes.

View Article: PubMed Central - PubMed

Affiliation: School of Biological Sciences, University of Reading, Reading, Berkshire, United Kingdom. b.w.neuman@reading.ac.uk

ABSTRACT
Enveloped virus release is driven by poorly understood proteins that are functional analogs of the coat protein assemblies that mediate intracellular vesicle trafficking. We used differential electron density mapping to detect membrane integration by membrane-bending proteins from five virus families. This demonstrates that virus matrix proteins replace an unexpectedly large portion of the lipid content of the inner membrane face, a generalized feature likely to play a role in reshaping cellular membranes.

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Related in: MedlinePlus

Cryo-electron micrographs of virus preparations.The images include virus particles (v), GP vesicles (g), empty vesicles (e) and tubular hollow particles (t). Preparations of Tacaribe virus (A), Porcine respiratory and reproductive syndrome virus (B), Severe acute respiratory syndrome coronavirus (C) and Influenza A virus (D) are shown to illustrate the double-ringed appearance of the membrane.
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pone-0057916-g001: Cryo-electron micrographs of virus preparations.The images include virus particles (v), GP vesicles (g), empty vesicles (e) and tubular hollow particles (t). Preparations of Tacaribe virus (A), Porcine respiratory and reproductive syndrome virus (B), Severe acute respiratory syndrome coronavirus (C) and Influenza A virus (D) are shown to illustrate the double-ringed appearance of the membrane.

Mentions: In order to see how working matrix proteins interact with the membrane, we used cryo-electron microscopy to take pictures of virus populations in a near-native environment. In addition to viruses, these populations naturally contained a few empty vesicles and a heterogeneous collection of incompletely assembled viruses that were released from the same cells as the virus. Of these, the most interesting were called GP vesicles, which had virus surface glycoproteins but lacked a visible matrix (GP vesicles; Fig. 1).


Direct observation of membrane insertion by enveloped virus matrix proteins by phosphate displacement.

Neuman BW, Kiss G, Al-Mulla HM, Dokland T, Buchmeier MJ, Weikl T, Schley D - PLoS ONE (2013)

Cryo-electron micrographs of virus preparations.The images include virus particles (v), GP vesicles (g), empty vesicles (e) and tubular hollow particles (t). Preparations of Tacaribe virus (A), Porcine respiratory and reproductive syndrome virus (B), Severe acute respiratory syndrome coronavirus (C) and Influenza A virus (D) are shown to illustrate the double-ringed appearance of the membrane.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3585246&req=5

pone-0057916-g001: Cryo-electron micrographs of virus preparations.The images include virus particles (v), GP vesicles (g), empty vesicles (e) and tubular hollow particles (t). Preparations of Tacaribe virus (A), Porcine respiratory and reproductive syndrome virus (B), Severe acute respiratory syndrome coronavirus (C) and Influenza A virus (D) are shown to illustrate the double-ringed appearance of the membrane.
Mentions: In order to see how working matrix proteins interact with the membrane, we used cryo-electron microscopy to take pictures of virus populations in a near-native environment. In addition to viruses, these populations naturally contained a few empty vesicles and a heterogeneous collection of incompletely assembled viruses that were released from the same cells as the virus. Of these, the most interesting were called GP vesicles, which had virus surface glycoproteins but lacked a visible matrix (GP vesicles; Fig. 1).

Bottom Line: Enveloped virus release is driven by poorly understood proteins that are functional analogs of the coat protein assemblies that mediate intracellular vesicle trafficking.We used differential electron density mapping to detect membrane integration by membrane-bending proteins from five virus families.This demonstrates that virus matrix proteins replace an unexpectedly large portion of the lipid content of the inner membrane face, a generalized feature likely to play a role in reshaping cellular membranes.

View Article: PubMed Central - PubMed

Affiliation: School of Biological Sciences, University of Reading, Reading, Berkshire, United Kingdom. b.w.neuman@reading.ac.uk

ABSTRACT
Enveloped virus release is driven by poorly understood proteins that are functional analogs of the coat protein assemblies that mediate intracellular vesicle trafficking. We used differential electron density mapping to detect membrane integration by membrane-bending proteins from five virus families. This demonstrates that virus matrix proteins replace an unexpectedly large portion of the lipid content of the inner membrane face, a generalized feature likely to play a role in reshaping cellular membranes.

Show MeSH
Related in: MedlinePlus