Si-Yu Bai, Wenlian Weng, Hua Wang, Zhiying Cui, Jiajun Wu, Yajin Qu, Yuxin Hao, Peng Gao, Yongning Zhang, Lei Zhou, Xinna Ge, Xin Guo, Jun Han, Hanchun Yang
{"title":"非洲猪瘟病毒及其编码蛋白 pEP153R 对自噬-溶酶体轴的调控","authors":"Si-Yu Bai, Wenlian Weng, Hua Wang, Zhiying Cui, Jiajun Wu, Yajin Qu, Yuxin Hao, Peng Gao, Yongning Zhang, Lei Zhou, Xinna Ge, Xin Guo, Jun Han, Hanchun Yang","doi":"10.3390/cimb46100667","DOIUrl":null,"url":null,"abstract":"<p><p>The autophagy-lysosome axis is an evolutionarily conserved intracellular degradation pathway which constitutes an important component of host innate immunity against microbial infections. Here, we show that African swine fever virus (ASFV), one of most devastating pathogens to the worldwide swine industry, can reshape the autophagy-lysosome axis by recruiting the critical lysosome membrane proteins (LAMP1 and LAMP2) to viral factories while inhibiting autophagic induction in macrophages. The screening of viral membrane proteins led to the identification of several ASFV membrane proteins, exemplified by viral protein pEP153R, that could significantly alter the subcellular localization of LAMP1/2 when expressed alone in transfected cells. Further analysis showed that pEP153R was also a component of viral factories and could induce endoplasmic reticulum (ER) retention of LAMP1/2, leading to the inhibition of the fusion of autophagosomes with lysosomes. Interestingly, the ASFV mutant lacking <i>EP153R</i> could still actively recruit LAMP into viral factories (VFs) and inhibit autophagic flux, indicating the existence of a functional redundancy of other viral proteins in the absence of pEP153R and highlighting the complexity of ASFV replication biology. Taken together, our results reveal novel information about the interplay of ASFV with the autophagy-lysosome axis and a previously unrecognized function of ASFV protein pEP153R in regulating the cellular autophagic process.</p>","PeriodicalId":10839,"journal":{"name":"Current Issues in Molecular Biology","volume":null,"pages":null},"PeriodicalIF":2.8000,"publicationDate":"2024-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11505880/pdf/","citationCount":"0","resultStr":"{\"title\":\"Modulation of Autophagy-Lysosome Axis by African Swine Fever Virus and Its Encoded Protein pEP153R.\",\"authors\":\"Si-Yu Bai, Wenlian Weng, Hua Wang, Zhiying Cui, Jiajun Wu, Yajin Qu, Yuxin Hao, Peng Gao, Yongning Zhang, Lei Zhou, Xinna Ge, Xin Guo, Jun Han, Hanchun Yang\",\"doi\":\"10.3390/cimb46100667\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The autophagy-lysosome axis is an evolutionarily conserved intracellular degradation pathway which constitutes an important component of host innate immunity against microbial infections. Here, we show that African swine fever virus (ASFV), one of most devastating pathogens to the worldwide swine industry, can reshape the autophagy-lysosome axis by recruiting the critical lysosome membrane proteins (LAMP1 and LAMP2) to viral factories while inhibiting autophagic induction in macrophages. The screening of viral membrane proteins led to the identification of several ASFV membrane proteins, exemplified by viral protein pEP153R, that could significantly alter the subcellular localization of LAMP1/2 when expressed alone in transfected cells. Further analysis showed that pEP153R was also a component of viral factories and could induce endoplasmic reticulum (ER) retention of LAMP1/2, leading to the inhibition of the fusion of autophagosomes with lysosomes. Interestingly, the ASFV mutant lacking <i>EP153R</i> could still actively recruit LAMP into viral factories (VFs) and inhibit autophagic flux, indicating the existence of a functional redundancy of other viral proteins in the absence of pEP153R and highlighting the complexity of ASFV replication biology. Taken together, our results reveal novel information about the interplay of ASFV with the autophagy-lysosome axis and a previously unrecognized function of ASFV protein pEP153R in regulating the cellular autophagic process.</p>\",\"PeriodicalId\":10839,\"journal\":{\"name\":\"Current Issues in Molecular Biology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.8000,\"publicationDate\":\"2024-10-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11505880/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Issues in Molecular Biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.3390/cimb46100667\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Issues in Molecular Biology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.3390/cimb46100667","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Modulation of Autophagy-Lysosome Axis by African Swine Fever Virus and Its Encoded Protein pEP153R.
The autophagy-lysosome axis is an evolutionarily conserved intracellular degradation pathway which constitutes an important component of host innate immunity against microbial infections. Here, we show that African swine fever virus (ASFV), one of most devastating pathogens to the worldwide swine industry, can reshape the autophagy-lysosome axis by recruiting the critical lysosome membrane proteins (LAMP1 and LAMP2) to viral factories while inhibiting autophagic induction in macrophages. The screening of viral membrane proteins led to the identification of several ASFV membrane proteins, exemplified by viral protein pEP153R, that could significantly alter the subcellular localization of LAMP1/2 when expressed alone in transfected cells. Further analysis showed that pEP153R was also a component of viral factories and could induce endoplasmic reticulum (ER) retention of LAMP1/2, leading to the inhibition of the fusion of autophagosomes with lysosomes. Interestingly, the ASFV mutant lacking EP153R could still actively recruit LAMP into viral factories (VFs) and inhibit autophagic flux, indicating the existence of a functional redundancy of other viral proteins in the absence of pEP153R and highlighting the complexity of ASFV replication biology. Taken together, our results reveal novel information about the interplay of ASFV with the autophagy-lysosome axis and a previously unrecognized function of ASFV protein pEP153R in regulating the cellular autophagic process.
期刊介绍:
Current Issues in Molecular Biology (CIMB) is a peer-reviewed journal publishing review articles and minireviews in all areas of molecular biology and microbiology. Submitted articles are subject to an Article Processing Charge (APC) and are open access immediately upon publication. All manuscripts undergo a peer-review process.