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

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• 作者：Jiansen Du (5)
  Xuefeng Wang (4)
  Jing Ma (5)
  Jianxin Wang (5)
  Yuyin Qin (4)
  Chunhui Zhu (4)
  Fang Liu (5)
  Yiming Shao (5)
  Jianhua Zhou (4)
  Wentao Qiao (5)
  Xinqi Liu (5)
  
  5. State Key Laboratory for Infectious Disease Prevention and Control ; and National Center for AIDS/STD Control and Prevention ; Chinese Center for Disease Control and Prevention ; Beijing ; 102206 ; China
  4. State Key Laboratory of Veterinary Biotechnology ; Harbin Veterinary Research Institute ; Chinese Academy of Agricultural Sciences ; Harbin ; 150001 ; China
  
• 关键词：EIAV ; gp45 ; Crystal structure ; Stability ; Vaccine strain ; Heptad repeat ; Pre ; fusion conformation ; Replication
• 刊名：Retrovirology
• 出版年：2014
• 出版时间：December 2014
• 年：2014
• 卷：11
• 期：1
• 全文大小：1,224 KB
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• 刊物主题：Virology; Infectious Diseases; Cancer Research;
• 出版者：BioMed Central
• ISSN：1742-4690

文摘

Background 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.