Open AccessMouse cytomegalovirus egress protein pM50 interacts with cellular endophilin‐ A 2
Author(s) -
Lemnitzer Frederic,
Raschbichler Verena,
Kolodziejczak Dominika,
Israel Lars,
Imhof Axel,
Bailer Susanne M.,
Koszinowski Ulrich,
Ruzsics Zsolt
Publication year - 2013
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/cmi.12080
Subject(s) - biology , cytoplasm , recombinant dna , microbiology and biotechnology , capsid , nucleus , nuclear transport , viral replication , virology , cell nucleus , genetics , virus , gene
Summary The herpesvirus replication cycle comprises maturation processes in the nucleus and cytoplasm of the infected cells. After their nuclear assembly viral capsids translocate via primary envelopment towards the cytoplasm. This event is mediated by the nuclear envelopment complex, which is composed by two conserved viral proteins belonging to the UL34 and UL31 protein families. Here, we generated recombinant viruses, which express affinity‐tagged pM50 and/or pM53 , the pUL34 and pUL31 homologues of the murine cytomegalovirus. We extracted pM50 ‐ and pM53 ‐associated protein complexes from infected cells and analysed their composition after affinity purification by mass spectrometry. We observed reported interaction partners and identified new putative protein–protein interactions for both proteins. Endophilin‐ A 2 was observed as the most prominent cellular partner of pM50 . We found that endophilin‐ A 2 binds to pM50 directly, and this interaction seems to be conserved in the pUL34 family.