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
Protein N-myristoylation is an important fatty acylation catalyzed by N-myristoyltransferases(NMTs),which are ubiquitous enzymes in eukaryotes.Specifically,attachment of a myristoyl group is vital for proteins partici...Protein N-myristoylation is an important fatty acylation catalyzed by N-myristoyltransferases(NMTs),which are ubiquitous enzymes in eukaryotes.Specifically,attachment of a myristoyl group is vital for proteins participating in various biological functions,including signal transduction,cellular localization,and oncogenesis.Recent studies have revealed unexpected mechanisms indicating that protein N-myristoylation is involved in host defense against microbial and viral infections.In this review,we describe the current understanding of protein N-myristoylation(mainly focusing on myristoyl switches)and summarize its crucial roles in regulating innate immune responses,including TLR4-dependent inflammatory responses and demyristoylation-induced innate immunosuppression during Shigella flexneri infection.Furthermore,we examine the role of myristoylation in viral assembly,intracellular host interactions,and viral spread during human immunodeficiency virus-1(HIV-1)infection.Deeper insight into the relationship between protein N-myristoylation and innate immunity might enable us to clarify the pathogenesis of certain infectious diseases and better harness protein N-myristoylation for new therapeutics.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.
基金supported by a special program from the Ministry o f Science and Technology of China(2016YFA0502500 to L.Z.)the Chinese National Natural Science Funds(U20A20393,82041009,31925013,31671457,and 91753139 to LZ.,31871405 and 31571460 to FZ.)+3 种基金Jiangsu National Science Foundation(BK20180043 and 19KJA550003 to F.Z.)the Zhejiang Natural Science Fund(LD19C070001 to L.Z.)the Key Project of University Natural Science Foundation of Jiangsu Province(19KJA550003)a project funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions.
文摘Protein N-myristoylation is an important fatty acylation catalyzed by N-myristoyltransferases(NMTs),which are ubiquitous enzymes in eukaryotes.Specifically,attachment of a myristoyl group is vital for proteins participating in various biological functions,including signal transduction,cellular localization,and oncogenesis.Recent studies have revealed unexpected mechanisms indicating that protein N-myristoylation is involved in host defense against microbial and viral infections.In this review,we describe the current understanding of protein N-myristoylation(mainly focusing on myristoyl switches)and summarize its crucial roles in regulating innate immune responses,including TLR4-dependent inflammatory responses and demyristoylation-induced innate immunosuppression during Shigella flexneri infection.Furthermore,we examine the role of myristoylation in viral assembly,intracellular host interactions,and viral spread during human immunodeficiency virus-1(HIV-1)infection.Deeper insight into the relationship between protein N-myristoylation and innate immunity might enable us to clarify the pathogenesis of certain infectious diseases and better harness protein N-myristoylation for new therapeutics.
