Both viruses and host cells compete for intracellular polyamines for efficient propagation.Currently,how the key polyamine-metabolizing enzymes,including ornithine decarboxylase 1(ODC1)and its antizyme 1(OAZ1),are act...Both viruses and host cells compete for intracellular polyamines for efficient propagation.Currently,how the key polyamine-metabolizing enzymes,including ornithine decarboxylase 1(ODC1)and its antizyme 1(OAZ1),are activated to co-ordinate viral propagation and polyamine biosynthesis remains unknown.Here,we report that the matrix protein of rice stripe mosaic virus(RSMV),a cytorhabdovirus,directly hijacks OAZ1 to ensure the proper assembly of rigid bacilliform non-enveloped virions in leafhopper vector.Viral matrix protein effectively competes with ODC1 to bind to OAZ1,and thus,the ability of OAZ1 to target and mediate the degradation of ODC1 is significantly inhibited during viral propagation,which finally promotes polyamines production.Thus,OAZ1 and ODC1 are activated to synergistically promote viral persistent propagation and polyamine biosynthesis in viruliferous vectors.Our data suggest that it is a novel mechanism for rhabdovirus to exploit OAZ1 for facilitating viral assembly.展开更多
基金supported by funds from the National Natural Science Foundation of China to Taiyun Wei under grant number 31920103014the National Natural Science Foundation of China to Dongsheng Jia under grant number 31970160+1 种基金the National Natural Science Foundation of China to Xiaofeng Zhang under grant number 31871931the Natural Science Foundation of Fujian Province to Dongsheng Jia under grant number 2020 J06015.
文摘Both viruses and host cells compete for intracellular polyamines for efficient propagation.Currently,how the key polyamine-metabolizing enzymes,including ornithine decarboxylase 1(ODC1)and its antizyme 1(OAZ1),are activated to co-ordinate viral propagation and polyamine biosynthesis remains unknown.Here,we report that the matrix protein of rice stripe mosaic virus(RSMV),a cytorhabdovirus,directly hijacks OAZ1 to ensure the proper assembly of rigid bacilliform non-enveloped virions in leafhopper vector.Viral matrix protein effectively competes with ODC1 to bind to OAZ1,and thus,the ability of OAZ1 to target and mediate the degradation of ODC1 is significantly inhibited during viral propagation,which finally promotes polyamines production.Thus,OAZ1 and ODC1 are activated to synergistically promote viral persistent propagation and polyamine biosynthesis in viruliferous vectors.Our data suggest that it is a novel mechanism for rhabdovirus to exploit OAZ1 for facilitating viral assembly.
