Protein pE120R of African swine fever virus is post-translationally acetylated as revealed by post-source decay MALDI mass spectrometry.
Post-translational modification of proteins is a key regulatory event in many cellular processes. African swine fever virus (ASFV) is a large DNA virus that contains about 150 open reading frames (ORF) which encode for more than 150 polypeptides, most of them without assigned function. Two-dimensional gel electrophoresis (2DE) followed by Post-Source Decay Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry (PSD-MALDI-MS) revealed that ASFV protein pE120R, essential for virus transport from assembly sites to plasma membranes, is acetylated at the N-terminal Ala residue during infection. To our knowledge, this is the first acetylated ASFV protein described and this modification might be relevant to ASFV life cycle since many viruses use the acetylation signaling pathway as a primary target for viral proteins after infection.
Alfonso
Patricia
P
Departamento de Biotecnología, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, Ctra de la Coruña Km 7, 28040, Madrid, Spain.
Quetglas
José I
JI
Escribano
José M
JM
Alonso
Covadonga
C
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism*; D000358:African Swine Fever Virus / Q000378:metabolism*; D000595:Amino Acid Sequence; D004268:DNA-Binding Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D015678:Viral Structural Proteins / Q000378:metabolism*
C105175:African swine fever virus structural protein p14.5; D004268:DNA-Binding Proteins; D015678:Viral Structural Proteins; D000123:Acetyltransferases