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The Cytoplasmic Tails of Infectious Bronchitis Virus E and M Proteins Mediate Their Interaction

Overview
Journal Virology
Specialty Microbiology
Date 2003 Aug 2
PMID 12890618
Citations 96
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Abstract

Virus-like particle (VLP) formation by the coronavirus E and M proteins suggests that interactions between these proteins play a critical role in coronavirus assembly. We studied interactions between the infectious bronchitis virus (IBV) E and M proteins using in vivo crosslinking and VLP assembly assays. We show that IBV E and M can be crosslinked to each other in IBV-infected and transfected cells, indicating that they interact. The cytoplasmic tails of both proteins are important for this interaction. We also examined the ability of the mutant and chimeric E and M proteins to form VLPs. IBV M proteins that are missing portions of their cytoplasmic tails or transmembrane regions were not able to support VLP formation, regardless of their ability to be crosslinked to IBV E. Interactions between the E and M proteins and the membrane bilayer are likely to play an important role in VLP formation and virus budding.

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References
1.
Lim K, Liu D . The missing link in coronavirus assembly. Retention of the avian coronavirus infectious bronchitis virus envelope protein in the pre-Golgi compartments and physical interaction between the envelope and membrane proteins. J Biol Chem. 2001; 276(20):17515-23. PMC: 7982318. DOI: 10.1074/jbc.M009731200. View

2.
Weisz O, SWIFT A, Machamer C . Oligomerization of a membrane protein correlates with its retention in the Golgi complex. J Cell Biol. 1993; 122(6):1185-96. PMC: 2119850. DOI: 10.1083/jcb.122.6.1185. View

3.
Klumperman J, Locker J, Meijer A, Horzinek M, Geuze H, Rottier P . Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding. J Virol. 1994; 68(10):6523-34. PMC: 237073. DOI: 10.1128/JVI.68.10.6523-6534.1994. View

4.
Machamer C, Mentone S, Rose J, Farquhar M . The E1 glycoprotein of an avian coronavirus is targeted to the cis Golgi complex. Proc Natl Acad Sci U S A. 1990; 87(18):6944-8. PMC: 54658. DOI: 10.1073/pnas.87.18.6944. View

5.
Stern D, Burgess L, Sefton B . Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus. J Virol. 1982; 42(1):208-19. PMC: 256062. DOI: 10.1128/JVI.42.1.208-219.1982. View