Acid-labile formylation of amino terminal proline of human immunodeficiency virus type 1 p24gag was found by proteomics using two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry

2002 ◽  
Vol 293 (3) ◽  
pp. 1107-1113 ◽  
Author(s):  
Takashi Fuchigami ◽  
Shogo Misumi ◽  
Nobutoki Takamune ◽  
Ichiro Takahashi ◽  
Michiho Takama ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Laser Desorption ◽  
Laser Desorption Ionization ◽  
Two Dimensional Gel Electrophoresis ◽  
Ionization Time ◽  
Amino Terminal ◽  
Flight Mass Spectrometry ◽  
Immunodeficiency Virus ◽  
Acid Labile

scholarly journals Three Isoforms of Cyclophilin A Associated with Human Immunodeficiency Virus Type 1 Were Found by Proteomics by Using Two-Dimensional Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry

2002 ◽  
Vol 76 (19) ◽  
pp. 10000-10008 ◽  
Author(s):  
Shogo Misumi ◽  
Takashi Fuchigami ◽  
Nobutoki Takamune ◽  
Ichiro Takahashi ◽  
Michiho Takama ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Cyclophilin A ◽  
Laser Desorption Ionization ◽  
Ionization Time ◽  
Viral Membrane ◽  
Flight Mass Spectrometry ◽  
Immunodeficiency Virus ◽  
2D Gel ◽  
Hiv 1

ABSTRACT Human immunodeficiency virus type 1 (HIV-1) strain LAV-1 (HIV-1LAV-1) particles were collected by ultracentrifugation, treated with subtilisin, and then purified by Sepharose CL-4B column chromatography to remove microvesicles. The lysate of the purified HIV-1LAV-1 particles was subjected to two-dimensional (2D) gel electrophoresis and stained. The 2D gel electrophoresis image suggested that 24 proteins can be identified inside the virion. Furthermore, the stained protein spots were excised and digested with trypsin. The resulting peptide fragments were characterized by matrix-assisted laser desorption ionization-time of flight mass spectrometry. Peptide mass fingerprinting data suggested that two isoforms of cyclophilin A (CyPA), one with an isoelectric point (pI) of 6.40 and one with a pI of 6.53, are inside the viral membrane; that another isoform, with a pI of 6.88, is outside the viral membrane; and that the CyPA isoform with a pI of 6.53 is N acetylated. The mechanisms that permit the redistribution of CyPA on the viral surface have not yet been clarified, but it is surmised that the CyPA isoform with a pI of 6.88 may play a critical role in the attachment of virions to the surface of target cells and that both CyPA isoforms with pIs of 6.40 and 6.53 may regulate the conformation of the HIV-1 capsid protein.

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