目的全面地了解和研究鸟氨酸脱羧酶1(ODC1)的生物学功能以及在多种肿瘤中的表达情况。方法利用The Human Protein Atlas、NCBI、Oncomine等数据库对ODC1的蛋白定位、蛋白-蛋白互作网络及在多种癌症中的表达与预后情况进行分析。结果对...目的全面地了解和研究鸟氨酸脱羧酶1(ODC1)的生物学功能以及在多种肿瘤中的表达情况。方法利用The Human Protein Atlas、NCBI、Oncomine等数据库对ODC1的蛋白定位、蛋白-蛋白互作网络及在多种癌症中的表达与预后情况进行分析。结果对通过数据库获取的数据进行分析发现,ODC1主要定位于细胞质与细胞膜,并且存在复杂的蛋白-蛋白互作网络。在多种肿瘤细胞中,ODC1的表达显著高于正常细胞,ODC1高表达癌症患者的预后更差。结论ODC1具有复杂的生物学功能,在多种癌症中处于高表达状态,其高表达也显著影响着癌症患者的预后。因此,本研究旨在为以ODC1为靶点的抗癌作用机制的研究提供理论依据与线索。展开更多
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
文摘目的全面地了解和研究鸟氨酸脱羧酶1(ODC1)的生物学功能以及在多种肿瘤中的表达情况。方法利用The Human Protein Atlas、NCBI、Oncomine等数据库对ODC1的蛋白定位、蛋白-蛋白互作网络及在多种癌症中的表达与预后情况进行分析。结果对通过数据库获取的数据进行分析发现,ODC1主要定位于细胞质与细胞膜,并且存在复杂的蛋白-蛋白互作网络。在多种肿瘤细胞中,ODC1的表达显著高于正常细胞,ODC1高表达癌症患者的预后更差。结论ODC1具有复杂的生物学功能,在多种癌症中处于高表达状态,其高表达也显著影响着癌症患者的预后。因此,本研究旨在为以ODC1为靶点的抗癌作用机制的研究提供理论依据与线索。
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.
