Subhashri, R and Shaila, MS (2007) Characterization of membrane association of Rinderpest virus matrix protein. In: Biochemical and Biophysical Research Communications, 355 (4). pp. 1096-1101.
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Paramyxovirus matrix protein is believed to play a crucial role in the assembly and maturation of the virus particle by bringing the major viral components together at the budding site in the host cell. The membrane association capability of many enveloped virus matrix proteins has been characterized to be their intrinsic property. In this work, we have characterized the membrane association of Rinderpest virus matrix (M) protein. The M protein of Rinderpest virus when expressed in the absence of other viral proteins is present both in the cytoplasm and plasma membrane. When expressed as GFP fusion protein, the M protein gets localized into plasma membrane protrusions. High salt and alkaline conditions resulted in partial dissociation of M protein from cell membrane. Thus, M protein behaves like an integral membrane protein although its primary structure suggests it to be a peripheral membrane protein.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier.|
|Keywords:||Morbillivirus matrix protein; Rinderpest virus matrix protein;Membrane protein;Peripheral membrane protein;GFP-fusion protein|
|Department/Centre:||Division of Biological Sciences > Microbiology & Cell Biology|
|Date Deposited:||04 Jun 2008|
|Last Modified:||19 Sep 2010 04:45|
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