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Retrovirology2014; 11; 26; doi: 10.1186/1742-4690-11-26

Structural and biochemical insights into the V/I505T mutation found in the EIAV gp45 vaccine strain.

Abstract: The equine infectious anemia virus (EIAV) is a lentivirus of the Retrovirus family, which causes persistent infection in horses often characterized by recurrent episodes of high fever. It has a similar morphology and life cycle to the human immunodeficiency virus (HIV). Its transmembrane glycoprotein, gp45 (analogous to gp41 in HIV), mediates membrane fusion during the infection. However, the post-fusion conformation of EIAV gp45 has not yet been determined. EIAV is the first member of the lentiviruses for which an effective vaccine has been successfully developed. The attenuated vaccine strain, FDDV, has been produced from a pathogenic strain by a series of passages in donkey dermal cells. We have previously reported that a V/I505T mutation in gp45, in combination with other mutations in gp90, may potentially contribute to the success of the vaccine strain. To this end, we now report on our structural and biochemical studies of the gp45 protein from both wide type and vaccine strain, providing a valuable structural model for the advancement of the EIAV vaccine. Results: We resolved crystal structures of the ecto-domain of gp45 from both the wild-type EIAV and the vaccine strain FDDV. We found that the V/I505T mutation in gp45 was located in a highly conserved d position within the heptad repeat, which protruded into a 3-fold symmetry axis within the six-helix bundle. Our crystal structure analyses revealed a shift of a hydrophobic to hydrophilic interaction due to this specific mutation, and further biochemical and virological studies confirmed that the mutation reduced the overall stability of the six-helix bundle in post-fusion conformation. Moreover, we found that altering the temperatures drastically affected the viral infectivity. Conclusions: Our high-resolution crystal structures of gp45 exhibited high conservation between the gp45/gp41 structures of lentiviruses. In addition, a hydrophobic to hydrophilic interaction change in the EIAV vaccine strain was found to modulate the stability and thermal-sensitivity of the overall gp45 structure. Our observations suggest that lowering the stability of the six-helix bundle (post-fusion), which may stabilizes the pre-fusion conformation, might be one of the reasons of acquired dominance for FDDV in viral attenuation.
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Publication Date: 2014-03-21 PubMed ID: 24656154PubMed Central: PMC3997929DOI: 10.1186/1742-4690-11-26Google Scholar: Lookup
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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 focuses on understanding the structure and biochemical properties of a mutation found in a vaccine strain (FDDV) of the equine infectious anemia virus (EIAV). The findings reveal that a specific mutation causes a change in the protein structure, reducing its stability and making it more sensitive to temperature changes, which could potentially contribute to the vaccine’s effectiveness.

Research Objective and Background

  • The main aim of this research is to investigate the impact of the V/I505T mutation in the equine infectious anemia virus (EIAV) gp45 vaccine strain. The EIAV is a lentivirus, similar in structure and life cycle to HIV. An effective vaccine has been developed for EIAV, with the vaccine strain FDDV produced from a pathogenic strain created through various passages in donkey dermal cells. In the vaccine strain, a mutation V/I505T was found in the gp45 protein, along with other mutations in gp90 that could potentially contribute to the vaccine’s success. The researchers intended to analyze the structural and biochemical aspects of the gp45 protein for better understanding of the vaccine’s function.

Results

  • The researchers were able to discern the crystal structures of the gp45 ecto-domain in both the wild type EIAV and the vaccine strain FDDV. They observed that the V/I505T mutation in gp45 was situated in a key position within the heptad repeat part of the protein, leading to an interaction change from hydrophobic to hydrophilic, thereby reducing the stability of the six-helix bundle in the post-fusion conformation.
  • Furthermore, the team noted that adjustments in temperatures significantly affected the viral infectivity. Moreover, they identified a high level of structural conservation between the gp45/gp41 structures of lentiviruses.

Conclusions

  • The researchers concluded that understanding the high-resolution crystal structures of gp45 can provide valuable insight into the development and effectiveness of the EIAV vaccine. In particular, the identified change in the protein structure, from hydrophobic to hydrophilic interaction due to the specific mutation, seems to decrease the stability and increase thermal-sensitivity of the entire gp45 structure.
  • Based on their findings, the researchers suggest that the reduction in the stability of the six-helix bundle, which likely stabilizes the pre-fusion conformation, may be one of the reasons for the attained dominance of the FDDV vaccine strain in viral attenuation or weakening of the virus.

Cite This Article

APA
Du J, Wang X, Ma J, Wang J, Qin Y, Zhu C, Liu F, Shao Y, Zhou J, Qiao W, Liu X. (2014). Structural and biochemical insights into the V/I505T mutation found in the EIAV gp45 vaccine strain. Retrovirology, 11, 26. https://doi.org/10.1186/1742-4690-11-26

Publication

Retrovirology
ISSN: 1742-4690
NlmUniqueID: 101216893
Country: England
Language: English
Volume: 11
Pages: 26

Researcher Affiliations

Du, Jiansen
    Wang, Xuefeng
      Ma, Jing
        Wang, Jianxin
          Qin, Yuyin
            Zhu, Chunhui
              Liu, Fang
                Shao, Yiming
                  Zhou, Jianhua
                  • State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin 300071, China. jianhua_uc@126.com.
                  Qiao, Wentao
                    Liu, Xinqi

                      MeSH Terms

                      • Animals
                      • Crystallography, X-Ray
                      • Horses
                      • Infectious Anemia Virus, Equine / chemistry
                      • Infectious Anemia Virus, Equine / genetics
                      • Infectious Anemia Virus, Equine / physiology
                      • Mutant Proteins / chemistry
                      • Mutant Proteins / genetics
                      • Mutant Proteins / metabolism
                      • Mutation, Missense
                      • Protein Conformation
                      • Protein Stability / radiation effects
                      • Temperature
                      • Viral Envelope Proteins / chemistry
                      • Viral Envelope Proteins / genetics
                      • Viral Envelope Proteins / metabolism
                      • Viral Vaccines / chemistry
                      • Viral Vaccines / genetics

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