Membrane transplantation to correct integral membrane protein defects

Kimberly V. Curlee, Jeong S. Hong, J. P. Clancy, Scott A. King, Eric Hunter, Bakhrom Berdiev, Dale Benos, Maja A. Sommerfelt, Eric J. Sorscher, Michael Sakalian

Research output: Contribution to journalArticle

Abstract

In this report we show that the tendency of certain viruses to carry host membrane proteins in their envelopes can be harnessed for transplantation of small patches of plasma membrane, including fully functional, polytopic ion channel proteins and their regulatory binding partners. As a stringent model we tested the topologically complex epithelial ion channel CFTR. Initially an attenuated vaccinia virus was found capable of transferring CFTR in a properly folded, functional and regulatable form to CFTR negative cells. Next we generated viruslike particles (VLPs) composed of retroviral structural proteins that assemble and bud at the host cell plasma membrane. These particles were also shown to mediate functional ion channel transfer. By testing the capacity of complex membrane proteins to incorporate into viral envelopes these experiments provide new insight into the permissiveness of viral envelopment, including the ability of incorporated proteins to retain function and repair defects at the cell surface, and serve as a platform for studies of ion channel and membrane protein biochemistry.

Original languageEnglish
Pages (from-to)511-520
Number of pages10
JournalJournal of Molecular Medicine
Volume81
Issue number8
DOIs
Publication statusPublished - Aug 1 2003
Externally publishedYes

Fingerprint

Ion Channels
Membrane Proteins
Transplantation
Membranes
Cell Membrane
Permissiveness
Proteins
Aptitude
Vaccinia virus
Biochemistry
Viruses

Keywords

  • CFTR
  • Membrane protein transfer
  • Rous sarcoma virus
  • Viral envelope

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Curlee, K. V., Hong, J. S., Clancy, J. P., King, S. A., Hunter, E., Berdiev, B., ... Sakalian, M. (2003). Membrane transplantation to correct integral membrane protein defects. Journal of Molecular Medicine, 81(8), 511-520. https://doi.org/10.1007/s00109-003-0446-7

Membrane transplantation to correct integral membrane protein defects. / Curlee, Kimberly V.; Hong, Jeong S.; Clancy, J. P.; King, Scott A.; Hunter, Eric; Berdiev, Bakhrom; Benos, Dale; Sommerfelt, Maja A.; Sorscher, Eric J.; Sakalian, Michael.

In: Journal of Molecular Medicine, Vol. 81, No. 8, 01.08.2003, p. 511-520.

Research output: Contribution to journalArticle

Curlee, KV, Hong, JS, Clancy, JP, King, SA, Hunter, E, Berdiev, B, Benos, D, Sommerfelt, MA, Sorscher, EJ & Sakalian, M 2003, 'Membrane transplantation to correct integral membrane protein defects', Journal of Molecular Medicine, vol. 81, no. 8, pp. 511-520. https://doi.org/10.1007/s00109-003-0446-7
Curlee KV, Hong JS, Clancy JP, King SA, Hunter E, Berdiev B et al. Membrane transplantation to correct integral membrane protein defects. Journal of Molecular Medicine. 2003 Aug 1;81(8):511-520. https://doi.org/10.1007/s00109-003-0446-7
Curlee, Kimberly V. ; Hong, Jeong S. ; Clancy, J. P. ; King, Scott A. ; Hunter, Eric ; Berdiev, Bakhrom ; Benos, Dale ; Sommerfelt, Maja A. ; Sorscher, Eric J. ; Sakalian, Michael. / Membrane transplantation to correct integral membrane protein defects. In: Journal of Molecular Medicine. 2003 ; Vol. 81, No. 8. pp. 511-520.
@article{d9dd7118adfd471cbe9171be0f50c68f,
title = "Membrane transplantation to correct integral membrane protein defects",
abstract = "In this report we show that the tendency of certain viruses to carry host membrane proteins in their envelopes can be harnessed for transplantation of small patches of plasma membrane, including fully functional, polytopic ion channel proteins and their regulatory binding partners. As a stringent model we tested the topologically complex epithelial ion channel CFTR. Initially an attenuated vaccinia virus was found capable of transferring CFTR in a properly folded, functional and regulatable form to CFTR negative cells. Next we generated viruslike particles (VLPs) composed of retroviral structural proteins that assemble and bud at the host cell plasma membrane. These particles were also shown to mediate functional ion channel transfer. By testing the capacity of complex membrane proteins to incorporate into viral envelopes these experiments provide new insight into the permissiveness of viral envelopment, including the ability of incorporated proteins to retain function and repair defects at the cell surface, and serve as a platform for studies of ion channel and membrane protein biochemistry.",
keywords = "CFTR, Membrane protein transfer, Rous sarcoma virus, Viral envelope",
author = "Curlee, {Kimberly V.} and Hong, {Jeong S.} and Clancy, {J. P.} and King, {Scott A.} and Eric Hunter and Bakhrom Berdiev and Dale Benos and Sommerfelt, {Maja A.} and Sorscher, {Eric J.} and Michael Sakalian",
year = "2003",
month = "8",
day = "1",
doi = "10.1007/s00109-003-0446-7",
language = "English",
volume = "81",
pages = "511--520",
journal = "Journal of Molecular Medicine",
issn = "0946-2716",
publisher = "Springer Verlag",
number = "8",

}

TY - JOUR

T1 - Membrane transplantation to correct integral membrane protein defects

AU - Curlee, Kimberly V.

AU - Hong, Jeong S.

AU - Clancy, J. P.

AU - King, Scott A.

AU - Hunter, Eric

AU - Berdiev, Bakhrom

AU - Benos, Dale

AU - Sommerfelt, Maja A.

AU - Sorscher, Eric J.

AU - Sakalian, Michael

PY - 2003/8/1

Y1 - 2003/8/1

N2 - In this report we show that the tendency of certain viruses to carry host membrane proteins in their envelopes can be harnessed for transplantation of small patches of plasma membrane, including fully functional, polytopic ion channel proteins and their regulatory binding partners. As a stringent model we tested the topologically complex epithelial ion channel CFTR. Initially an attenuated vaccinia virus was found capable of transferring CFTR in a properly folded, functional and regulatable form to CFTR negative cells. Next we generated viruslike particles (VLPs) composed of retroviral structural proteins that assemble and bud at the host cell plasma membrane. These particles were also shown to mediate functional ion channel transfer. By testing the capacity of complex membrane proteins to incorporate into viral envelopes these experiments provide new insight into the permissiveness of viral envelopment, including the ability of incorporated proteins to retain function and repair defects at the cell surface, and serve as a platform for studies of ion channel and membrane protein biochemistry.

AB - In this report we show that the tendency of certain viruses to carry host membrane proteins in their envelopes can be harnessed for transplantation of small patches of plasma membrane, including fully functional, polytopic ion channel proteins and their regulatory binding partners. As a stringent model we tested the topologically complex epithelial ion channel CFTR. Initially an attenuated vaccinia virus was found capable of transferring CFTR in a properly folded, functional and regulatable form to CFTR negative cells. Next we generated viruslike particles (VLPs) composed of retroviral structural proteins that assemble and bud at the host cell plasma membrane. These particles were also shown to mediate functional ion channel transfer. By testing the capacity of complex membrane proteins to incorporate into viral envelopes these experiments provide new insight into the permissiveness of viral envelopment, including the ability of incorporated proteins to retain function and repair defects at the cell surface, and serve as a platform for studies of ion channel and membrane protein biochemistry.

KW - CFTR

KW - Membrane protein transfer

KW - Rous sarcoma virus

KW - Viral envelope

UR - http://www.scopus.com/inward/record.url?scp=10744232678&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=10744232678&partnerID=8YFLogxK

U2 - 10.1007/s00109-003-0446-7

DO - 10.1007/s00109-003-0446-7

M3 - Article

VL - 81

SP - 511

EP - 520

JO - Journal of Molecular Medicine

JF - Journal of Molecular Medicine

SN - 0946-2716

IS - 8

ER -