{"title":"The selective autophagic degradation of avian metapneumovirus subgroup C M2-2 protein via SQSTM1 suppresses viral replication.","authors":"Lei Hou, Jinshuo Guo, Jianwei Zhou, Jue Liu","doi":"10.1080/27694127.2024.2375936","DOIUrl":null,"url":null,"abstract":"<p><p>Avian metapneumovirus subgroup C (aMPV/C) is an emerging pathogen that causes acute respiratory infection in chickens and turkeys. Sequestosome 1 (SQSTM1), a selective autophagy receptor, regulates cellular activity or viral replication by recognizing ubiquitinated substrates. Here, we found that SQSTM1 expression inhibits aMPV/C replication through selective autophagy. In particular, SQSTM1 interacts with the aMPV/C M2-2 protein via its PB1 domain, and by recognizing a ubiquitinated lysine at position 67 of viral M2-2 protein. This recognition leads to the autophagic degradation of the aMPV/C M2-2 protein, suppressing viral replication.</p>","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"3 1","pages":"2375936"},"PeriodicalIF":0.0000,"publicationDate":"2024-09-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11864695/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Autophagy reports","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/27694127.2024.2375936","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Avian metapneumovirus subgroup C (aMPV/C) is an emerging pathogen that causes acute respiratory infection in chickens and turkeys. Sequestosome 1 (SQSTM1), a selective autophagy receptor, regulates cellular activity or viral replication by recognizing ubiquitinated substrates. Here, we found that SQSTM1 expression inhibits aMPV/C replication through selective autophagy. In particular, SQSTM1 interacts with the aMPV/C M2-2 protein via its PB1 domain, and by recognizing a ubiquitinated lysine at position 67 of viral M2-2 protein. This recognition leads to the autophagic degradation of the aMPV/C M2-2 protein, suppressing viral replication.