Trimerization of the reovirus cell attachment protein (σI) induces conformational changes in σI necessary for its cell-binding function

Gustavo Leone; Roy Duncan; Patrick W.K. Lee

doi:10.1016/0042-6822(91)90447-J

Trimerization of the reovirus cell attachment protein (σI) induces conformational changes in σI necessary for its cell-binding function

Gustavo Leone, Roy Duncan, Patrick W.K. Lee

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

The implications of reovirus σI protein trimerization on its cell-binding function were investigated. Both monomeric and trimeric forms of σI were found to be present when full-length type 3 reovirus SI transcripts prepared in vitro were translated in rabbit reticulocyte lysates. Pulse-chase experiments demonstrated that monomers were precursors of trimers. However, only the trimeric form was capable of binding to cell surface receptors. Protease and antibody recognition analyses revealed significant structural differences between these two σI forms at both the N- and C-termini. Our results suggest that trimerization of protein of is accompanied by extensive conformational changes necessary for its cell attachment function.

Original language	English
Pages (from-to)	758-761
Number of pages	4
Journal	Virology
Volume	184
Issue number	2
DOIs	https://doi.org/10.1016/0042-6822(91)90447-J
Publication status	Published - Oct 1991
Externally published	Yes

Bibliographical note

Funding Information:
This work was supported by the Medical Research Council Canada. G.L. and R.D. are recipients of the Alberta Heritage Foundation for Medical Research (AHFMR) Studentship and Fellowship, respectively. P.W.K.L. is AHFMR Scholar.

ASJC Scopus Subject Areas

Virology

PubMed: MeSH publication types

Journal Article
Research Support, Non-U.S. Gov't

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10.1016/0042-6822(91)90447-J

Cite this

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title = "Trimerization of the reovirus cell attachment protein (σI) induces conformational changes in σI necessary for its cell-binding function",

abstract = "The implications of reovirus σI protein trimerization on its cell-binding function were investigated. Both monomeric and trimeric forms of σI were found to be present when full-length type 3 reovirus SI transcripts prepared in vitro were translated in rabbit reticulocyte lysates. Pulse-chase experiments demonstrated that monomers were precursors of trimers. However, only the trimeric form was capable of binding to cell surface receptors. Protease and antibody recognition analyses revealed significant structural differences between these two σI forms at both the N- and C-termini. Our results suggest that trimerization of protein of is accompanied by extensive conformational changes necessary for its cell attachment function.",

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note = "Funding Information: This work was supported by the Medical Research Council Canada. G.L. and R.D. are recipients of the Alberta Heritage Foundation for Medical Research (AHFMR) Studentship and Fellowship, respectively. P.W.K.L. is AHFMR Scholar.",

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AU - Duncan, Roy

AU - Lee, Patrick W.K.

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N2 - The implications of reovirus σI protein trimerization on its cell-binding function were investigated. Both monomeric and trimeric forms of σI were found to be present when full-length type 3 reovirus SI transcripts prepared in vitro were translated in rabbit reticulocyte lysates. Pulse-chase experiments demonstrated that monomers were precursors of trimers. However, only the trimeric form was capable of binding to cell surface receptors. Protease and antibody recognition analyses revealed significant structural differences between these two σI forms at both the N- and C-termini. Our results suggest that trimerization of protein of is accompanied by extensive conformational changes necessary for its cell attachment function.

AB - The implications of reovirus σI protein trimerization on its cell-binding function were investigated. Both monomeric and trimeric forms of σI were found to be present when full-length type 3 reovirus SI transcripts prepared in vitro were translated in rabbit reticulocyte lysates. Pulse-chase experiments demonstrated that monomers were precursors of trimers. However, only the trimeric form was capable of binding to cell surface receptors. Protease and antibody recognition analyses revealed significant structural differences between these two σI forms at both the N- and C-termini. Our results suggest that trimerization of protein of is accompanied by extensive conformational changes necessary for its cell attachment function.

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Trimerization of the reovirus cell attachment protein (σI) induces conformational changes in σI necessary for its cell-binding function

Abstract

Bibliographical note

ASJC Scopus Subject Areas

PubMed: MeSH publication types

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