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Journal of virology2015; 90(4); 1824-1838; doi: 10.1128/JVI.02814-15

Equine Infectious Anemia Virus Gag Assembly and Export Are Directed by Matrix Protein through trans-Golgi Networks and Cellular Vesicles.

Abstract: Gag intracellular assembly and export are very important processes for lentiviruses replication. Previous studies have demonstrated that equine infectious anemia virus (EIAV) matrix (MA) possesses distinct phosphoinositide affinity compared with HIV-1 MA and that phosphoinositide-mediated targeting to peripheral and internal membranes is a critical factor in EIAV assembly and release. In this study, we compared the cellular assembly sites of EIAV and HIV-1. We observed that the assembly of EIAV particles occurred on interior cellular membranes, while HIV-1 was targeted to the plasma membrane (PM) for assembly. Then, we determined that W7 and K9 in the EIAV MA N terminus were essential for Gag assembly and release but did not affect the cellular distribution of Gag. The replacement of EIAV MA with HIV-1 MA directed chimeric Gag to the PM but severely impaired Gag release. MA structural analysis indicated that the EIAV and HIV-1 MAs had similar spatial structures but that helix 1 of the EIAV MA was closer to loop 2. Further investigation indicated that EIAV Gag accumulated in the trans-Golgi network (TGN) but not the early and late endosomes. The 9 N-terminal amino acids of EIAV MA harbored the signal that directed Gag to the TGN membrane system. Additionally, we demonstrated that EIAV particles were transported to the extracellular space by the cellular vesicle system. This type of EIAV export was not associated with multivesicular bodies or microtubule depolymerization but could be inhibited by the actin-depolymerizing drug cytochalasin D, suggesting that dynamic actin depolymerization may be associated with EIAV production. Objective: In previous studies, EIAV Gag was reported to localize to both the cell interior and the plasma membrane. Here, we demonstrate that EIAV likely uses the TGN as the assembly site in contrast to HIV-1, which is targeted to the PM for assembly. These distinct assembly features are determined by the MA domain. We also identified two sites in the N terminus of EIAV MA that were important for Gag assembly and release. Furthermore, the observation of EIAV transport by cellular vesicles but not by multivesicular bodies sheds light on the mechanisms underlying EIAV cellular replication.
Copyright © 2016, American Society for Microbiology. All Rights Reserved.
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Publication Date: 2015-12-04 PubMed ID: 26637458PubMed Central: PMC4734017DOI: 10.1128/JVI.02814-15Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article focuses on understanding the unique replication process of the Equine Infectious Anemia Virus (EIAV) at a cellular level, particularly how it assembles and exports its proteins, and how it differs from the HIV-1 virus in this regard.

Objective

The researchers compare the EIAV with HIV-1 with respect to their cellular assembly and export sites. Their objective is to highlight the differences in assembly between the two viruses and reveal the specificities in cellular replication of the EIAV.

Assembly Sites of EIAV and HIV-1

  • While HIV-1 targets the plasma membrane (PM), the study found that EIAV particles assemble on internal cellular membranes.

Importance of Phosphoinositide Affinity in EIAV “Matrix (MA)”

  • The research underscores the differing phosphoinositide affinities between EIAV MA and HIV-1 MA and how it plays a vital role in the assembly and release of EIAV.

Role of W7 and K9 in Gag Assembly and Release

  • The researchers found that amino acid residues W7 and K9 in EIAV MA’s N terminus are crucial for Gag assembly and release, but do not affect Gag’s cellular distribution.
  • Substituting EIAV MA with HIV-1 MA directed the chimeric Gag to the PM but severely impeded Gag release.

Spatial Structure Differences Between EIAV and HIV-1 MA

  • Although HIV-1 MA and EIAV MA are similar in spatial structure, helix 1 of the EIAV MA was observed closer to loop 2.

EIAV Gag’s Localization in Trans-Golgi Network (TGN)

  • EIAV Gag was shown to aggregate in the TGN, rather than early and late endosomes.
  • The signal directing Gag to the TGN membrane system was found within the 9 N-terminal amino acids of EIAV MA.

Export of EIAV Particles

  • The study demonstrated that EIAV particles are transported to the extracellular space via the cellular vesicle system.
  • This type of EIAV export is independent of multivesicular bodies involvement or microtubule depolymerization; however, it can be inhibited by the actin-depolymerizing drug cytochalasin D, suggesting a possible connection between dynamic actin depolymerization and EIAV production.

Conclusion

The researchers discovered distinct cellular mechanisms of assembly and export of EIAV in comparison to HIV-1. These findings can enhance our understanding of how lentiviruses replicate and potentially lead to the development of more effective treatments for diseases caused by such viruses.

Cite This Article

APA
Zhang Z, Ma J, Zhang X, Su C, Yao QC, Wang X. (2015). Equine Infectious Anemia Virus Gag Assembly and Export Are Directed by Matrix Protein through trans-Golgi Networks and Cellular Vesicles. J Virol, 90(4), 1824-1838. https://doi.org/10.1128/JVI.02814-15

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 90
Issue: 4
Pages: 1824-1838

Researcher Affiliations

Zhang, Zeli
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, Harbin, Heilongjiang, China.
Ma, Jian
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, Harbin, Heilongjiang, China.
Zhang, Xiang
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, Harbin, Heilongjiang, China.
Su, Chao
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, Harbin, Heilongjiang, China.
Yao, Qiu-Cheng
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, Harbin, Heilongjiang, China.
Wang, Xiaojun
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, Harbin, Heilongjiang, China xjw@hvri.ac.cn.

MeSH Terms

  • Cytoplasmic Vesicles / metabolism
  • Gene Products, gag / metabolism
  • HIV-1 / physiology
  • Humans
  • Infectious Anemia Virus, Equine / physiology
  • Protein Transport
  • Viral Matrix Proteins / metabolism
  • Virus Assembly
  • trans-Golgi Network / metabolism

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