Sumoylation of Human Parainfluenza Virus Type 3 Phosphoprotein Correlates with A Reduction in Viral

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Human parainfluenza virus type 3(HPIV3),a member of the Paramyxoviridae family,can cause lower respiratory disease in infants and young children.The phosphoprotein(P)of HPIV3 is an essential cofactor of the viral RNA-dependent RNA polymerase large protein(L).P connects nucleocapsid protein(N)with L to initiate genome transcription and replication.Sumoylation influences many important pathways of the target proteins,and many viral proteins are also themselves sumoylated.In this study,we found that the P of HPIV3 could be sumoylated,and mutation of K492 and K532 to arginine(PK492R/K532R)failed to be sumoylated within P,which enhances HPIV3 minigenome activity.Biochemical studies showed that PK492R/K532R had no effect on its interactions with N,formation of homo-tetramers and formation of inclusion bodies.Finally,we found that incorporation of K492R/K532R into a recombinant HPIV3(rHPIV3-PK492R/K532R)increased viral production in culture cells,suggesting that sumoylation attenuates functions of P and down-regulates viral replication.
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