Characterization of Bovine Foamy Virus Gag Late Assembly Domain Motifs and Their Role in Recruiting ESCRT for Budding
A large number of retroviruses, such as human immunodeficiency virus (HIV) and prototype foamy virus (PFV), recruit the endosomal sorting complex required for transport (ESCRT) through the late domain (L domain) on the Gag structural protein for virus budding. However, little is known about the mole...
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| Format: | Article |
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MDPI AG
2022-03-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/14/3/522 |
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| author | Zhaohuan Wang Rui Li Chenxi Liu Wentao Qiao Juan Tan |
| author_facet | Zhaohuan Wang Rui Li Chenxi Liu Wentao Qiao Juan Tan |
| author_sort | Zhaohuan Wang |
| collection | DOAJ |
| description | A large number of retroviruses, such as human immunodeficiency virus (HIV) and prototype foamy virus (PFV), recruit the endosomal sorting complex required for transport (ESCRT) through the late domain (L domain) on the Gag structural protein for virus budding. However, little is known about the molecular mechanism of bovine foamy virus (BFV) budding. In the present study, we report that BFV recruits ESCRT for budding through the L domain of Gag. Specifically, knockdown of <i>VPS4</i> (encoding vacuolar protein sorting 4), <i>ALIX</i> (encoding ALG-2-interacting protein X), and <i>TSG101</i> (encoding tumor susceptibility 101) indicated that BFV uses ESCRT for budding. Mutational analysis of BFV Gag (BGag) showed that, in contrast to the classical L domain motifs, BGag contains two motifs, P<sub>56</sub>LPI and Y<sub>103</sub>GPL, with L domain functions. In addition, the two L domains are necessary for the cytoplasmic localization of BGag, which is important for effective budding. Furthermore, we demonstrated that the functional site of Alix is V498 in the V domain and the functional site of Tsg101 is N69 in the UBC-like domain for BFV budding. Taken together, these results demonstrate that BFV recruits ESCRT for budding through the PLPI and YGPL L domain motifs in BGag. |
| first_indexed | 2024-03-09T12:16:30Z |
| format | Article |
| id | doaj.art-1da0cb733f9b4cadb9033de5dd82c657 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-09T12:16:30Z |
| publishDate | 2022-03-01 |
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| record_format | Article |
| series | Viruses |
| spelling | doaj.art-1da0cb733f9b4cadb9033de5dd82c6572023-11-30T22:45:45ZengMDPI AGViruses1999-49152022-03-0114352210.3390/v14030522Characterization of Bovine Foamy Virus Gag Late Assembly Domain Motifs and Their Role in Recruiting ESCRT for BuddingZhaohuan Wang0Rui Li1Chenxi Liu2Wentao Qiao3Juan Tan4Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, ChinaKey Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, ChinaKey Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, ChinaKey Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, ChinaKey Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, ChinaA large number of retroviruses, such as human immunodeficiency virus (HIV) and prototype foamy virus (PFV), recruit the endosomal sorting complex required for transport (ESCRT) through the late domain (L domain) on the Gag structural protein for virus budding. However, little is known about the molecular mechanism of bovine foamy virus (BFV) budding. In the present study, we report that BFV recruits ESCRT for budding through the L domain of Gag. Specifically, knockdown of <i>VPS4</i> (encoding vacuolar protein sorting 4), <i>ALIX</i> (encoding ALG-2-interacting protein X), and <i>TSG101</i> (encoding tumor susceptibility 101) indicated that BFV uses ESCRT for budding. Mutational analysis of BFV Gag (BGag) showed that, in contrast to the classical L domain motifs, BGag contains two motifs, P<sub>56</sub>LPI and Y<sub>103</sub>GPL, with L domain functions. In addition, the two L domains are necessary for the cytoplasmic localization of BGag, which is important for effective budding. Furthermore, we demonstrated that the functional site of Alix is V498 in the V domain and the functional site of Tsg101 is N69 in the UBC-like domain for BFV budding. Taken together, these results demonstrate that BFV recruits ESCRT for budding through the PLPI and YGPL L domain motifs in BGag.https://www.mdpi.com/1999-4915/14/3/522bovine foamy virusL domainESCRTvirus-like particles |
| spellingShingle | Zhaohuan Wang Rui Li Chenxi Liu Wentao Qiao Juan Tan Characterization of Bovine Foamy Virus Gag Late Assembly Domain Motifs and Their Role in Recruiting ESCRT for Budding Viruses bovine foamy virus L domain ESCRT virus-like particles |
| title | Characterization of Bovine Foamy Virus Gag Late Assembly Domain Motifs and Their Role in Recruiting ESCRT for Budding |
| title_full | Characterization of Bovine Foamy Virus Gag Late Assembly Domain Motifs and Their Role in Recruiting ESCRT for Budding |
| title_fullStr | Characterization of Bovine Foamy Virus Gag Late Assembly Domain Motifs and Their Role in Recruiting ESCRT for Budding |
| title_full_unstemmed | Characterization of Bovine Foamy Virus Gag Late Assembly Domain Motifs and Their Role in Recruiting ESCRT for Budding |
| title_short | Characterization of Bovine Foamy Virus Gag Late Assembly Domain Motifs and Their Role in Recruiting ESCRT for Budding |
| title_sort | characterization of bovine foamy virus gag late assembly domain motifs and their role in recruiting escrt for budding |
| topic | bovine foamy virus L domain ESCRT virus-like particles |
| url | https://www.mdpi.com/1999-4915/14/3/522 |
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