Minimal exclusion of plasma membrane proteins during retroviral envelope formation
(2000) In Proceedings of the National Academy of Sciences 97(13). p.7527-7532- Abstract
- The retrovirus forms its envelope by budding at the plasma membrane (PM). This process is primarily driven by its cytoplasmic core-precursor protein, Gag, as shown by the efficient formation of virus-like Gag particles in the absence of its envelope protein, Env. Most interestingly, several studies have demonstrated incorporation of various PM proteins into retrovirus, but the underlying mechanism of this phenomenon has remained elusive. We have purified Moloney murine leukemia virus Gag particles by sedimentation in an iodixanol gradient and donor PMs by flotation in a sucrose gradient and compared their protein compositions at equal lipid basis. We found that most PM proteins are present at similar density in both membranes. The... (More)
- The retrovirus forms its envelope by budding at the plasma membrane (PM). This process is primarily driven by its cytoplasmic core-precursor protein, Gag, as shown by the efficient formation of virus-like Gag particles in the absence of its envelope protein, Env. Most interestingly, several studies have demonstrated incorporation of various PM proteins into retrovirus, but the underlying mechanism of this phenomenon has remained elusive. We have purified Moloney murine leukemia virus Gag particles by sedimentation in an iodixanol gradient and donor PMs by flotation in a sucrose gradient and compared their protein compositions at equal lipid basis. We found that most PM proteins are present at similar density in both membranes. The inclusion of PM proteins was unaffected by incorporation of Env protein into the envelope of the Gag particles and whether these were produced at high or low level in the cells. These findings indicate that most PM proteins become incorporated into the retrovirus envelope without significant sorting. This feature of retrovirus assembly should be considered when studying retrovirus functions and developing retrovirus vectors. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1297022
- author
- Hammarstedt, Maria LU ; Wallengren, K ; Pedersen, K W ; Roos, N and Garoff, H
- publishing date
- 2000
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Proceedings of the National Academy of Sciences
- volume
- 97
- issue
- 13
- pages
- 7527 - 7532
- publisher
- National Academy of Sciences
- external identifiers
-
- wos:000087811600107
- scopus:0034691083
- ISSN
- 1091-6490
- DOI
- 10.1073/pnas.120051597
- language
- English
- LU publication?
- no
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Stem Cell and Pancreas Developmental Biology (013212044)
- id
- feb11e72-2a23-49d1-9f73-2212e69f4dc2 (old id 1297022)
- date added to LUP
- 2016-04-01 11:58:33
- date last changed
- 2022-01-26 21:00:36
@article{feb11e72-2a23-49d1-9f73-2212e69f4dc2,
abstract = {{The retrovirus forms its envelope by budding at the plasma membrane (PM). This process is primarily driven by its cytoplasmic core-precursor protein, Gag, as shown by the efficient formation of virus-like Gag particles in the absence of its envelope protein, Env. Most interestingly, several studies have demonstrated incorporation of various PM proteins into retrovirus, but the underlying mechanism of this phenomenon has remained elusive. We have purified Moloney murine leukemia virus Gag particles by sedimentation in an iodixanol gradient and donor PMs by flotation in a sucrose gradient and compared their protein compositions at equal lipid basis. We found that most PM proteins are present at similar density in both membranes. The inclusion of PM proteins was unaffected by incorporation of Env protein into the envelope of the Gag particles and whether these were produced at high or low level in the cells. These findings indicate that most PM proteins become incorporated into the retrovirus envelope without significant sorting. This feature of retrovirus assembly should be considered when studying retrovirus functions and developing retrovirus vectors.}},
author = {{Hammarstedt, Maria and Wallengren, K and Pedersen, K W and Roos, N and Garoff, H}},
issn = {{1091-6490}},
language = {{eng}},
number = {{13}},
pages = {{7527--7532}},
publisher = {{National Academy of Sciences}},
series = {{Proceedings of the National Academy of Sciences}},
title = {{Minimal exclusion of plasma membrane proteins during retroviral envelope formation}},
url = {{http://dx.doi.org/10.1073/pnas.120051597}},
doi = {{10.1073/pnas.120051597}},
volume = {{97}},
year = {{2000}},
}