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Home / Equine Research Bank / Virology / Exposing cryptic epitopes on the Venezuelan equine encephali...
Virology2021; 565; 13-21; doi: 10.1016/j.virol.2021.09.007

Exposing cryptic epitopes on the Venezuelan equine encephalitis virus E1 glycoprotein prior to treatment with alphavirus cross-reactive monoclonal antibody allows blockage of replication early in infection.

Abstract: Eastern equine encephalitis virus (EEEV), western equine encephalitis virus (WEEV) and Venezuelan equine encephalitis virus (VEEV) can cause fatal encephalitis in humans and equids. Some MAbs to the E1 glycoprotein are known to be cross-reactive, weakly neutralizing in vitro but can protect from disease in animal models. We investigated the mechanism of neutralization of VEEV infection by the broadly cross-reactive E1-specific MAb 1A4B-6. 1A4B-6 protected 3-week-old Swiss Webster mice prophylactically from lethal VEEV challenge. Likewise, 1A4B-6 inhibited virus growth in vitro at a pre-attachment step after virions were incubated at 37 °C and inhibited virus-mediated cell fusion. Amino acid residue N100 in the fusion loop of E1 protein was identified as critical for binding. The potential to elicit broadly cross-reactive MAbs with limited virus neutralizing activity in vitro but that can inhibit virus entry and protect animals from infection merits further exploration for vaccine and therapeutic developmental research.
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
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Publication Date: 2021-09-28 PubMed ID: 34626907PubMed Central: PMC8765347DOI: 10.1016/j.virol.2021.09.007Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • N.I.H.
  • Extramural
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  • Non-U.S. Gov't

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.

This research investigated the ability of the E1-specific MAb 1A4B-6 antibody to block the replication of the Venezuelan equine encephalitis virus (VEEV) at an early stage of infection. It suggests that the antibody, which can bind to the virus’s E1 glycoprotein, can offer protection from disease in animals, despite having limited in vitro neutralizing activity.

Understanding the Research

  • This study aimed to understand the function and effectiveness of MAb 1A4B-6, an antibody that reacts to the E1 glycoprotein on the VEEV. The immune system’s ability to recognize and neutralize any foreign material, such as bacteria, viruses, or tumor cells, is often due to antibodies, which bind specifically to these pathogens.
  • The VEEV, along with the Eastern equine encephalitis virus (EEEV) and the Western equine encephalitis virus (WEEV), can lead to fatal encephalitis in both humans and equids (a family of animals that includes horses and related species).
  • Previous research indicated that some monoclonal antibodies (MAbs) known to react to the E1 glycoprotein exhibited limited effectiveness in neutralizing the virus in vitro (laboratory conditions outside a living organism). However, these antibodies were able to protect animals from the disease in laboratory tests, showing some therapeutic potential.

Research Methodology and Outcomes

  • In this research, the scientists investigated how MAb 1A4B-6 combats VEEV infection. They discovered that the antibody could protect against lethal VEEV challenge prophylactically in 3-week-old Swiss Webster mice, suggesting a preventive use.
  • MAb 1A4B-6 was also able to impede the growth of the virus at a stage before it attached to host cells. The investigation revealed that this was accomplished after the virus particles, referred to as virions, were incubated at a certain temperature (37 °C).
  • The researchers also found that MAb 1A4B-6 could inhibit the fusion of the VEEV with host cells, a crucial step for the virus to replicate and spread within the host.
  • Through their investigation, the researchers identified the N100 amino acid residue found in the fusion loop of the E1 protein as an essential binding site for MAb, providing a potential target for future vaccine or therapeutic developments.

Implications

  • The research suggested that despite their limited in vitro neutralizing activity, antibodies like MAb 1A4B-6 could potentially be used as a preventive measure against VEEV infection.
  • The identification of the N100 amino acid residue as a critical binding site for the antibody provides a specific target for future research aiming to develop vaccines and therapeutics against VEEV.
  • The ability of MAb 1A4B-6 to inhibit virus entry and protect animals from infection in the study highlights a pathway for further exploration and development in the domain of vaccine and therapeutic research.

Cite This Article

APA
Calvert AE, Bennett SL, Hunt AR, Fong RH, Doranz BJ, Roehrig JT, Blair CD. (2021). Exposing cryptic epitopes on the Venezuelan equine encephalitis virus E1 glycoprotein prior to treatment with alphavirus cross-reactive monoclonal antibody allows blockage of replication early in infection. Virology, 565, 13-21. https://doi.org/10.1016/j.virol.2021.09.007

Publication

Virology
ISSN: 1096-0341
NlmUniqueID: 0110674
Country: United States
Language: English
Volume: 565
Pages: 13-21
PII: S0042-6822(21)00198-7

Researcher Affiliations

Calvert, Amanda E
  • Arboviral Diseases Branch, Division of Vector-Borne Diseases, Centers for Disease Control and Prevention, Fort Collins, CO 80521, USA. Electronic address: zpz0@cdc.gov.
Bennett, Susan L
  • Center for Vector-borne Infectious Diseases, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523, USA.
Hunt, Ann R
  • Center for Vector-borne Infectious Diseases, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523, USA.
Fong, Rachel H
  • Integral Molecular, Philadelphia, PA 19104, USA.
Doranz, Benjamin J
  • Integral Molecular, Philadelphia, PA 19104, USA.
Roehrig, John T
  • Center for Vector-borne Infectious Diseases, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523, USA.
Blair, Carol D
  • Center for Vector-borne Infectious Diseases, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523, USA.

MeSH Terms

  • Alphavirus / immunology
  • Alphavirus Infections / immunology
  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / immunology
  • Antibodies, Neutralizing / immunology
  • Antibodies, Viral / immunology
  • Cell Line
  • Chlorocebus aethiops
  • Cross Reactions
  • Encephalitis Virus, Venezuelan Equine / immunology
  • Encephalitis Virus, Venezuelan Equine / metabolism
  • Encephalomyelitis, Venezuelan Equine / immunology
  • Encephalomyelitis, Venezuelan Equine / therapy
  • Encephalomyelitis, Venezuelan Equine / virology
  • Glycoproteins / immunology
  • Immunotherapy
  • Mice
  • Protein Binding
  • Vero Cells
  • Viral Envelope Proteins / immunology
  • Viral Envelope Proteins / metabolism
  • Virion / immunology
  • Virion / metabolism
  • Virus Replication / drug effects

Grant Funding

  • HHSN272201400058C / NIAID NIH HHS

Conflict of Interest Statement

Declaration of competing interest. The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: B.J.D. and R.H.F. are shareholders of Integral Molecular.

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Citations

This article has been cited 1 times.
  1. Kim AS, Diamond MS. A molecular understanding of alphavirus entry and antibody protection.. Nat Rev Microbiol 2023 Jun;21(6):396-407.
    doi: 10.1038/s41579-022-00825-7pubmed: 36474012google scholar: lookup
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