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Journal of virology1985; 55(3); 840-842; doi: 10.1128/JVI.55.3.840-842.1985

Properties of monoclonal antibodies against glycoproteins of western equine encephalitis virus.

Abstract: To analyze the biological activities of the alphavirus glycoproteins, eight different monoclonal antibodies against the two glycoproteins of western equine encephalitis virus were isolated. Five of the eight monoclonal antibodies were shown to be specific for E1 and three for E2 protein by an enzyme-linked immunosorbent assay and by radioimmunoprecipitation. Three of the five anti-E1 and all of the anti-E2 monoclonal antibodies inhibited hemagglutination by purified virions. One anti-E1 and two anti-E2 monoclonal antibodies possessed high virus-neutralizing activity.
Publication Date: 1985-09-01 PubMed ID: 4020970PubMed Central: PMC255071DOI: 10.1128/JVI.55.3.840-842.1985Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This research studied eight different monoclonal antibodies against two types of glycoproteins found in the western equine encephalitis virus, analyzed their specificity and assessed their ability to neutralize the virus and inhibit hemagglutination.

Selection and characterization of monoclonal antibodies

  • The study isolated eight monoclonal antibodies that are specifically directed against the glycoproteins of the western equine encephalitis virus.
  • An enzyme-linked immunosorbent assay (ELISA) and radioimmunoprecipitation techniques were used to test these antibodies for specificity against two different types of viral glycoproteins, E1 and E2.
  • Five of the eight antibodies were found to be specific to E1 glycoprotein, while the remaining three showed specificity towards E2 glycoprotein.

Evaluating inhibition of hemagglutination and virus-neutralizing activity

  • The researchers then tested these antibodies for their ability to inhibit hemagglutination caused by the virus.
  • Out of the five E1-specific antibodies, three were able to inhibit hemagglutination, and all three E2-specific antibodies showed this capability.
  • Hemagglutination inhibition is vital as it shows the ability of the antibodies to prevent the virus from clumping red blood cells together, which is a strategy often used by the virus to evade the immune system.
  • The researchers also interestingly found that one of the E1-specific antibodies and both E2-specific antibodies possess high virus-neutralizing activity.
  • Virus-neutralizing activity describes the ability of these antibodies to neutralize the virus, making it incapable of infecting host cells and thus stopping the progression of the disease.

Implications of the research

  • The identification and characterization of these monoclonal antibodies provide deeper insights into the biology of the western equine encephalitis virus and can lead to the development of effective therapeutic strategies.
  • The neutralizing ability of these antibodies makes them promising candidates for the development of potential vaccines or treatments for western equine encephalitis.
  • Finally, these findings may also contribute to the development of diagnostic kits based on these specific antibodies.

Cite This Article

APA
Yamamoto K, Hashimoto K, Chiba J, Simizu B. (1985). Properties of monoclonal antibodies against glycoproteins of western equine encephalitis virus. J Virol, 55(3), 840-842. https://doi.org/10.1128/JVI.55.3.840-842.1985

Publication

ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 55
Issue: 3
Pages: 840-842

Researcher Affiliations

Yamamoto, K
    Hashimoto, K
      Chiba, J
        Simizu, B

          MeSH Terms

          • Antibodies, Monoclonal
          • Encephalitis Virus, Western Equine / metabolism
          • Hemagglutination
          • Viral Envelope Proteins / immunology
          • Viral Envelope Proteins / metabolism

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          Citations

          This article has been cited 2 times.
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          2. Strauss EG, Stec DS, Schmaljohn AL, Strauss JH. Identification of antigenically important domains in the glycoproteins of Sindbis virus by analysis of antibody escape variants.. J Virol 1991 Sep;65(9):4654-64.