A conservative domain shared by HIV gp120 and EIAV gp90: implications for HIV vaccine design.
Abstract: Both HIV and EIAV belong to the retroviridae family and lentivirus genus. Two variable regions (V3 and V4) of equine infectious anemia virus (EIAV) gp90 and two variable regions (V1 and V2) of HIV gp120 possibly adopt the same topology. We have studied the N-glycosylation properties and B cell linear epitope distribution profile of these two regions. Our results indicated that V3 and V4 of EIAV gp90 are very similar to V1 and V2 of HIV gp120. The differences between EIAV virulent and vaccine strains are mainly located at these two regions. Vaccine strains lose two N-glycosylation sites at these two regions. Because of the conservative domain shared by EIAV gp90 and HIV gp120, V1 and V2 of HIV gp120 and their glycosylation properties should be the regions preferably considered for HIV vaccine design.
Publication Date: 2005-12-29 PubMed ID: 16379610DOI: 10.1089/aid.2005.21.1057Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article discusses the similarities found in proteins of HIV and EIAV, pointing towards implications for designing an effective HIV vaccine.
Objective of the Study
- The study aimed to explore the similarities between variable regions (V3 and V4) of equine infectious anemia virus (EIAV) gp90 protein and variable regions (V1 and V2) of Human Immunodeficiency Virus (HIV) gp120 protein, with an emphasis on their N-glycosylation properties and B cell linear epitope distribution profile. These insights could provide valuable information for designing an effective HIV vaccine.
Comparative Analysis of EIAV gp90 and HIV gp120
- The researchers found a significant similarity between the variable regions V3 and V4 of EIAV gp90 and V1 and V2 of HIV gp120, in terms of structure and behavior.
- This comparison was particularly illumining as both EIAV and HIV belong to the same family and genus of viruses, namely Retroviridae and Lentivirus, respectively.
The Role of N-glycosylation
- The research highlighted N-glycosylation, a process in which sugars (glycans) are added to proteins, as a key variable in comparisons between EIAV gp90 and HIV gp120.
- N-glycosylation plays a crucial role in protein folding, stability, and functionality. It was observed that vaccine strains of EIAV lose two N-glycosylation sites at these two regions.
Implications for HIV Vaccine Design
- A deduced implication of this study was that the conservative domain shared by EIAV gp90 and HIV gp120, along with their glycosylation properties, should be taken into consideration when designing an HIV vaccine.
- This finding could potentially guide the design of novel HIV therapeutic strategies, as these features could prove to be viable targets for vaccine development.
Cite This Article
APA
Li H, Zhang X, Fan X, Shen T, Tong X, Shen R, Shao Y.
(2005).
A conservative domain shared by HIV gp120 and EIAV gp90: implications for HIV vaccine design.
AIDS Res Hum Retroviruses, 21(12), 1057-1059.
https://doi.org/10.1089/aid.2005.21.1057 Publication
Researcher Affiliations
- Department of Virus and Immunology, Chinese Center for STD and HIV Control and Prevention, 27 Nanwei Road, Xuanwu District, Beijing, 100050, Peoples Republic of China.
MeSH Terms
- AIDS Vaccines
- Amino Acid Sequence
- Animals
- Conserved Sequence
- Drug Design
- Epitopes, B-Lymphocyte
- Glycoproteins / chemistry
- Glycoproteins / genetics
- Glycosylation
- HIV Envelope Protein gp120 / chemistry
- HIV Envelope Protein gp120 / genetics
- Horses
- Humans
- Molecular Sequence Data
- Viral Envelope Proteins / chemistry
- Viral Envelope Proteins / genetics
Citations
This article has been cited 6 times.- Shao Y, Liu Y, Hao Y, Xu J, Li T, Wu H, Zhang T, Wu L, Wang S, Li D, Ren L, Wu Y. China CDC's HIV/AIDS Vaccine Efforts, from Basic Research to Clinical Studies.. China CDC Wkly 2020 Nov 27;2(48):929-932.
- Wang XF, Lin YZ, Li Q, Liu Q, Zhao WW, Du C, Chen J, Wang X, Zhou JH. Genetic Evolution during the development of an attenuated EIAV vaccine.. Retrovirology 2016 Feb 3;13:9.
- Du J, Wang X, Ma J, Wang J, Qin Y, Zhu C, Liu F, Shao Y, Zhou J, Qiao W, Liu X. Structural and biochemical insights into the V/I505T mutation found in the EIAV gp45 vaccine strain.. Retrovirology 2014 Mar 21;11:26.
- Wang X, Wang S, Lin Y, Jiang C, Ma J, Zhao L, Lv X, Wang F, Shen R, Zhou J. Unique evolution characteristics of the envelope protein of EIAV(LN₄₀), a virulent strain of equine infectious anemia virus.. Virus Genes 2011 Apr;42(2):220-8.
- Liu L, Wan Y, Wu L, Sun J, Li H, Li H, Ma L, Shao Y. Broader HIV-1 neutralizing antibody responses induced by envelope glycoprotein mutants based on the EIAV attenuated vaccine.. Retrovirology 2010 Sep 1;7:71.
- Taylor SD, Leib SR, Carpenter S, Mealey RH. Selection of a rare neutralization-resistant variant following passive transfer of convalescent immune plasma in equine infectious anemia virus-challenged SCID horses.. J Virol 2010 Jul;84(13):6536-48.
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