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Proceedings of the National Academy of Sciences of the United States of America1992; 89(21); 10041-10045; doi: 10.1073/pnas.89.21.10041

Extended x-ray absorption fine structure studies of a retrovirus: equine infectious anemia virus cysteine arrays are coordinated to zinc.

Abstract: Zinc finger arrays have been established as a critical structural feature of proteins involved in DNA recognition. Retroviral nucleocapsid proteins, which are involved in the binding of viral RNA, contain conserved cysteine-rich arrays that have been suggested to coordinate zinc. We provide metalloprotein structural data from an intact virus preparation that validate this hypothesis. Extended x-ray absorption fine structure (EXAFS) spectroscopy of well-characterized and active preparations of equine infectious anemia virus, compared with a peptide with known coordination and in combination with available biochemical and genetic data, defines a Cys3His1 coordination environment for zinc. The average of the Zn-S distances is 2.30(1) A and that of the Zn-N distance (to histidine) is 2.01(3) A.
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Publication Date: 1992-11-11 PubMed ID: 1332027PubMed Central: PMC50273DOI: 10.1073/pnas.89.21.10041Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.
  • Research Support
  • U.S. Gov't
  • P.H.S.

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 verifying the theory that protein features in a retroviral nucleocapsid, specifically cysteine-rich arrays, coordinate with zinc. The study, done with the use of extended x-ray absorption fine structures (EXAFS) spectroscopy, contributes affirmative data from an active, intact virus experiment, equine infectious anemia virus.

Understanding the Research

To understand what the researchers set out to do and what they were able to achieve, it’s important to break down their focus points:

  • Zinc finger arrays and protein structures: Proteins involved in DNA recognition often feature zinc finger arrays which are recognized as critical structural elements. These arrays normally bind to DNA, RNA, protein, or small molecules. However, the researchers are focusing on a quality of retroviral nucleocapsid proteins that are involved in binding viral RNA.
  • Retroviral nucleocapsid proteins: A defining characteristic of these proteins are conserved cysteine-rich arrays which have been theorized to have an association with zinc in a coordination capacity. The researchers’ objective is to confirm or refute this theory with concrete structural data.
  • Use of EXAFS spectroscopy: EXAFS spectroscopy is a technique used to investigate materials on an atomic level. This was used to study the equine infectious anemia virus, an active and verified preparation, to determine the level of zinc coordination within the protein structure. Along with genetic and biochemical data, this study aimed at defining a Cys3His1 coordination environment for zinc.
  • Evidence of coordination environment: The data collected provided measurements for the Zn-S distances (2.30(1) A) and the Zn-N distance (2.01(3) A), both demonstrating the association and coordination of the cysteine-rich arrays with zinc.

Significance of the Study

The verification of this theory can have a major impact in the realm of virology. By understanding how these proteins function at a structural level, it allows scientists to gain more in-depth knowledge about how retroviruses operate. Future studies might interpret these findings to forge better therapeutic strategies for conditions caused by retroviruses such as HIV and cancer. Furthermore, understanding the structural design of biological proteins enhances the application of bioengineering in medicine.

Cite This Article

APA
Chance MR, Sagi I, Wirt MD, Frisbie SM, Scheuring E, Chen E, Bess JW, Henderson LE, Arthur LO, South TL. (1992). Extended x-ray absorption fine structure studies of a retrovirus: equine infectious anemia virus cysteine arrays are coordinated to zinc. Proc Natl Acad Sci U S A, 89(21), 10041-10045. https://doi.org/10.1073/pnas.89.21.10041

Publication

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
NlmUniqueID: 7505876
Country: United States
Language: English
Volume: 89
Issue: 21
Pages: 10041-10045

Researcher Affiliations

Chance, M R
  • Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461.
Sagi, I
    Wirt, M D
      Frisbie, S M
        Scheuring, E
          Chen, E
            Bess, J W
              Henderson, L E
                Arthur, L O
                  South, T L

                    MeSH Terms

                    • Absorptiometry, Photon / methods
                    • Centrifugation, Density Gradient
                    • Cysteine
                    • Fourier Analysis
                    • HIV-1 / ultrastructure
                    • Infectious Anemia Virus, Equine / ultrastructure
                    • Viral Proteins / ultrastructure
                    • Zinc / analysis
                    • Zinc Fingers

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