Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus.
The major inducible 70-kDa heat shock protein (hsp72) binds measles virus (MV) nucleocapsids and increases MV gene expression. The cytoplasmic tail of the MV N protein (N(TAIL)) contains three hydrophobic domains (Box-1-3) that are potential targets of hsp72 interaction. Low affinity binding to Box-3 is correlated to hsp72-dependent stimulation of MV minireplicon reporter gene expression whereas interactions between hsp72 and Box-1 and/or -2 have not been documented. The present work showed that virus deficient in Box-3/hsp72 interaction retains the ability to form nucleocapsid/hsp72 complexes, identifying Box-2 but not Box-1 as a mediator of high affinity hsp72 binding. Box-2 is the binding site for the viral P protein X domain (XD), where P tethers the viral polymerase to nucleocapsid in support of transcription and genome replication, and competitive inhibition of XD binding to N(TAIL) by hsp72 was shown. Recognition of a common binding site by P and hsp72 represents a potential mechanism for host cell modulation of viral gene expression.
Zhang
Xinsheng
X
Department of Veterinary Biosciences, The Ohio State University, Columbus, 43210, USA.
Bourhis
Jean-Marie
JM
Longhi
Sonia
S
Carsillo
Thomas
T
Buccellato
Matthew
M
Morin
Benjamin
B
Canard
Bruno
B
Oglesbee
Michael
M
D020816:Amino Acid Motifs; D001665:Binding Sites; D002460:Cell Line; D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans / Q000378:metabolism; D008459:Measles virus / Q000737:chemistry*; D019590:Nucleocapsid Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D014779:Virus Replication
D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D019590:Nucleocapsid Proteins