Mass spectrometry of murine leukemia virus core proteins.
A mass spectrometry (MS) approach was used to analyze viral core proteins of the murine leukemia virus (MuLV)-based gene delivery vector. The retroviral particles produced by traditional methods were concentrated and purified by ultracentrifugation and spin column for matrix-assisted laser desorption ionization (MALDI) and electrospray ionization (ESI) MS. MALDI application detected all core MuLV proteins, partial degradation of p10, phosphorylation of p12, as well as the previously unknown formation of a polymeric supramolecular complex between p15 and p30 core proteins. ESI provided information on the post-translational modifications of MuLV core proteins. Data suggest myristoylation of p15 and oxidation of methionine residues in both p12 and p30, whereas cysteine residues in p10, p15 and p30 were not oxidized. The current study demonstrates that MALDI and ESI are efficient tools for viral core protein analysis and can be used as analytical tools in virology and biotechnology of gene delivery vectors.
Medvedkin
Viacheslav
V
Gene Therapy Laboratories, University of Southern California School of Medicine, 1441 Eastlake Avenue, 612, Los Angeles, CA 90033, USA.
Moore
Roger
R
Falick
Arnold M
AM
Conner
John
J
Omelchenko
Tatiana
T
Young
Mary
M
Anderson
W French
WF
Golubkov
Vladislav S
VS
Rozenberg-Adler
Yanina
Y
D009052:Leukemia Virus, Murine / Q000737:chemistry* / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014461:Ultracentrifugation; D014758:Viral Core Proteins / Q000737:chemistry* / Q000302:isolation & purification
D014758:Viral Core Proteins