CEEPC/IPM/CMSC - Abstrakt prezentace

(Česká konference hmotnostní spektrometrie 2017 - P-002)
Deeper clarification of the interaction between plasma membrane and matrix protein of human immunodeficiency virus 1

Tereza Bláhová 1 *, Petra Junková 1, Jan Prchal 1, Radovan Hynek 1

  1. Vysoká škola chemicko-technologická v Praze

Abstrakt

The matrix protein plays a key role in the retroviral life cycle since it mediates the transport and binding of the viral structural proteins to the plasma membrane, where the formation of the new viral particles takes place. Subject of our interest was the matrix protein of human immunodeficiency virus 1. It has been already proven that the interaction of its highly basic region with phosphatidylinositol-4,5-bisphosphate (PI-4,5-P2) is essential for the binding of viral structural proteins to the plasma membrane. For the deeper clarification of the matrix protein interaction with the membrane, the surface mapping of matrix protein was used. The experimental part of this study was therefore focused on the monitoring of the changes in the surface accessibility of the matrix protein residues after its binding to the liposomes containing phosphatidylserine (PS) and PI-4,5-P2.
Changes of surface accessibility of the residues R19, K21, K25, K26, K29 and W35 were detected. These residues are localized in the highly basic region and obviously mediate the interaction with the PI-4,5-P2 and PS. These results are in a very good agreement with previous studies of other scientific groups, especially with the NMR experiments of the matrix protein with PI-4,5-P2 in solution [1] and with the coarse-grained molecular dynamics analysis of the interaction between matrix protein and the membrane with different phospholipids [2]. The changes of surface accessibility of the residues R38, E39, E41, R42 and E73 localized aside from the highly basic region were also detected. This fact indicates that the matrix protein trimerization proceeds during its interaction with the membrane and may be very important for the finally anchoring the matrix protein into the plasma membrane.

* Korespondující autor: blahovab@vscht.cz

Literatura

  1. Saad J. S. et al.: Proc Natl Acad Sci U S A. 103(30), 1364-9 (2006).
  2. Charlier L. et al.: Biophys J. 106(3), 577-85 (2014).

Partneři společnosti

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Partneři

Bruker HPST Merck Pragolab Amedis EastPort Shimadzu Waters