The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Overlapping Motifs (PTAP and PPEY) within the Ebola Virus VP40 Protein Function Independently as Late Budding Domains: Involvement of Host Proteins TSG101 and VPS-4
Open accessAbstract
The VP40 protein of Ebola virus can bud from mammalian cells in the form of lipid-bound, virus-like particles (VLPs), and late budding domains (L-domains) are conserved motifs (PTAP, PPxY, or YxxL; where “x” is any amino acid) that facilitate the budding of VP40-containing VLPs. VP40 is unique in that potential overlapping L-domains with the sequences PTAP and PPEY are present at amino acids 7 to 13 of VP40 (PTAPPEY). L-domains are thought to function by interacting with specific cellular proteins, such as the ubiquitin ligase Nedd4, and a component of the vacuolar protein sorting (vps) pathway, tsg101. Mutational analysis of the PTAPPEY sequence of VP40 was performed to understand further the contribution of each individual motif in promoting VP40 budding. In addition, the contribution of tsg101 and a second member of the vps pathway, vps4, in facilitating budding was addressed. Our results indicate that (i) both the PTAP and PPEY motifs contribute to efficient budding of VP40-containing VLPs; (ii) PTAP and PPEY can function as L-domains when separated and moved from the N terminus (amino acid position 7) to the C terminus (amino acid position 316) of full-length VP40; (iii) A VP40-PTAP/tsg101 interaction recruits tsg101 into budding VLPs; (iv) a VP40-PTAP/tsg101 interaction recruits VP40 into lipid raft microdomains; and (v) a dominant-negative mutant of vps4 (E228Q), but not wild-type vps4, significantly inhibited the budding of Ebola virus (Zaire). These results provide important insights into the complex interplay between viral and host proteins during the late stages of Ebola virus budding.
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Cites
Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
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Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55 Gag
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Ubiquitin is part of the retrovirus budding machinery
Patnaik, A., Chau, V., & Wills, J. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.24.13069 · Cited by 292
Ebola Virus VP40-Induced Particle Formation and Association with the Lipid Bilayer
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“As docking sites for cellular proteins, these viral L-domains would be predicted to function when moved to a new location within the viral protein and, indeed, this phenomenon has been observed (8, 27, 31).”
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Vesicular Release of Ebola Virus Matrix Protein VP40
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Cited by
Endosomal and non-endosomal functions of ESCRT proteins
Slagsvold, T., Pattni, K., Malerød, L., & Stenmark, H. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.04.004 · Cited by 238
Human immunodeficiency virus type 1 assembly, release, and maturation
Adamson, C. S., & Freed, E. O. (2007) · Advances in Pharmacology · doi:10.1016/s1054-3589(07)55010-6 · Cited by 179
Ebola Virus Matrix Protein VP40 Uses the COPII Transport System for Its Intracellular Transport
Yamayoshi, S., Noda, T., Ebihara, H., Goto, H., Morikawa, Y., Lukashevich, I. S., Neumann, G., Feldmann, H., & Kawaoka, Y. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.02.001 · Cited by 100
Spurgers, K. B., Alefantis, T., Peyser, B. D., Ruthel, G. T., Bergeron, A. A., Costantino, J. A., Enterlein, S., Kota, K. P., Boltz, R. C. D., Aman, M. J., et al. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.003418 · Cited by 71
Importance of viral late domains in budding and release of enveloped RNA viruses
Welker, L., Paillart, J.-C., & Bernacchi, S. (2021) · Viruses · doi:10.3390/v13081559 · Cited by 36
Metadata
- Authors
- Licata, J. M., Simpson-Holley, M., Wright, N. T., Han, Z., Paragas, J., & Harty, R. N.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2003-02
- Volume
- 77
- Issue
- 3
- Pages
- 1812-1819
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W2096284021
- Cited by
- 275
- References
- 11
- FWCI
- 14.07
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Overlapping Motifs (PTAP and PPEY) within the Ebola Virus VP40 Protein Function Independently as Late Budding Domains: Involvement of Host Proteins TSG101 and VPS-4. https://app.cochat.ai/papers/10.1128/jvi.77.3.1812-1819.2003
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- Licata, J. M., Simpson-Holley, M., Wright, N. T., Han, Z., Paragas, J., & Harty, R. N. (2003). Overlapping Motifs (PTAP and PPEY) within the Ebola Virus VP40 Protein Function Independently as Late Budding Domains: Involvement of Host Proteins TSG101 and VPS-4. Journal of Virology. https://doi.org/10.1128/jvi.77.3.1812-1819.2003
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