Structure of the equine infectious anemia virus Tat protein.
Abstract: Trans-activator (Tat) proteins regulate the transcription of lentiviral DNA in the host cell genome. These RNA binding proteins participate in the life cycle of all known lentiviruses, such as the human immunodeficiency viruses (HIV) or the equine infectious anemia virus (EIAV). The consensus RNA binding motifs [the trans-activation responsive element (TAR)] of HIV-1 as well as EIAV Tat proteins are well characterized. The structure of the 75-amino acid EIAV Tat protein in solution was determined by two- and three-dimensional nuclear magnetic resonance methods and molecular dynamics calculations. The protein structure exhibits a well-defined hydrophobic core of 15 amino acids that serves as a scaffold for two flexible domains corresponding to the NH2- and COOH-terminal regions. The core region is a strictly conserved sequence region among the known Tat proteins. The structural data can be used to explain several of the observed features of Tat proteins.
Publication Date: 1994-06-10 PubMed ID: 7515512DOI: 10.1126/science.7515512Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The researchers studied the structure of a protein called Tat, involved in the life cycle of certain types of viruses, such as HIV and EIAV, using nuclear magnetic resonance techniques and molecular dynamics calculations. They found that it has a core scaffold composed of a highly conserved sequence of 15 amino acids, as well as two flexible regions.
Understanding Tat Proteins
- Trans-activator or Tat proteins play a crucial role in the regulation of lentiviral DNA transcription within the host cell genome. Essentially, these proteins help initiate the transcription process enabling the virus to replicate.
- These proteins are notable in all known lentiviruses including potentially lethal viruses like the human immunodeficiency viruses (HIV) and the equine infectious anemia virus (EIAV).
- The study particularly focuses on the structure of the Tat protein of EIAV, a lentivirus that affects horses.
Structural Insights Into EIAV Tat Protein
- Researchers leveraged advanced techniques – two and three-dimensional nuclear magnetic resonance methods, along with molecular dynamics calculations – to discern the structure of the 75-amino acid EIAV Tat protein.
- The EIAV Tat protein structure was found to have a ‘hydrophobic core’ of 15 amino acids which provides a scaffold for two flexible domains – the NH2 and COOH terminal regions.
- The ‘hydrophobic core’ was identified as a strictly conserved sequence region among the known Tat proteins. This indicates that this structural element is common and critical across various strains of lentiviruses.
Significance of the Research
- The structural data provided can help explain several observed features of Tat proteins.
- Discovering the role and structure of the Tat protein could aid in the development of targeted treatments and therapies for lentivirus-related diseases, including HIV and EIAV. By understanding how this protein functions in the viral life cycle, scientists may be able to disrupt its effects, hence preventing the virus from proliferating.
- Given that the ‘hydrophobic core’ constitutes a conserved sequence area, it could be exploited as a universal target for the development of broad-spectrum antiviral therapies.
Cite This Article
APA
Willbold D, Rosin-Arbesfeld R, Sticht H, Frank R, Rösch P.
(1994).
Structure of the equine infectious anemia virus Tat protein.
Science, 264(5165), 1584-1587.
https://doi.org/10.1126/science.7515512 Publication
Researcher Affiliations
- Lehrstuhl für Biopolymere, Universität Bayreuth, Germany.
MeSH Terms
- Amino Acid Sequence
- Gene Products, tat / chemistry
- Gene Products, tat / metabolism
- Infectious Anemia Virus, Equine / chemistry
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Protein Conformation
- Protein Structure, Secondary
- RNA / metabolism
- Sequence Alignment
Citations
This article has been cited 5 times.- Lonning SM, Zhang W, Leib SR, McGuire TC. Detection and induction of equine infectious anemia virus-specific cytotoxic T-lymphocyte responses by use of recombinant retroviral vectors. J Virol 1999 Apr;73(4):2762-9.
- Filikov AV, James TL. Structure-based design of ligands for protein basic domains: application to the HIV-1 Tat protein. J Comput Aided Mol Des 1998 May;12(3):229-40.
- Manival X, Yang Y, Strub MP, Kochoyan M, Steinmetz M, Aymerich S. From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins. EMBO J 1997 Aug 15;16(16):5019-29.
- Tan R, Frankel AD. Structural variety of arginine-rich RNA-binding peptides. Proc Natl Acad Sci U S A 1995 Jun 6;92(12):5282-6.
- Hoffman DW, White SW. NMR analysis of the trans-activation response (TAR) RNA element of equine infectious anemia virus. Nucleic Acids Res 1995 Oct 25;23(20):4058-65.
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