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Prevention of Respiratory Syncytial Virus Infection: From Vaccine to Antibody

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  • Authors: Kelly Huang1, Herren Wu
  • Editors: James E. Crowe Jr.3, Diana Boraschi4, Rino Rappuoli5
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Department of Infectious Disease, MedImmune, LLC., One MedImmune Way, Gaithersburg, MD 20878; 2: Department of Antibody Discovery and Protein Engineering, MedImmune, LLC., One MedImmune Way, Gaithersburg, MD 20878; 3: Vanderbilt University School of Medicine, Nashville, TN; 4: National Research Council, Pisa, Italy; 5: Novartis Vaccines, Siena, Italy
    • Source: microbiolspec August 2014 vol. 2 no. 4 doi:10.1128/microbiolspec.AID-0014-2014
  • Received 06 January 2014 Accepted 31 March 2014 Published 08 August 2014
  • : Herren Wu, [email protected]mune.com
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  • Abstract:

    Respiratory syncytial virus (RSV) is the leading cause of lower respiratory tract disease in infants and young children. Initial efforts to develop a vaccine to prevent RSV lower respiratory tract disease in children were halted because of serious adverse events that occurred when children were infected with RSV following vaccination, including vaccine-related deaths. Subsequently, a major focus for researchers was to understand what led to these adverse events. Investment in a vaccine for RSV continues, and new strategies are under development. Success to prevent RSV disease was met by the development of immunoprophylaxis, first with intravenous immunoglobulin and then with recombinant monoclonal antibody. The story of immunoprophylaxis for RSV includes the first-in-class use of antibody technology for infectious disease, and palivizumab currently remains the only way to prevent serious lower respiratory tract disease due to RSV infection.

  • Citation: Huang K, Wu H. 2014. Prevention of Respiratory Syncytial Virus Infection: From Vaccine to Antibody. Microbiol Spectrum 2(4):AID-0014-2014. doi:10.1128/microbiolspec.AID-0014-2014.

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2014-08-08
2020-08-03

Abstract:

Respiratory syncytial virus (RSV) is the leading cause of lower respiratory tract disease in infants and young children. Initial efforts to develop a vaccine to prevent RSV lower respiratory tract disease in children were halted because of serious adverse events that occurred when children were infected with RSV following vaccination, including vaccine-related deaths. Subsequently, a major focus for researchers was to understand what led to these adverse events. Investment in a vaccine for RSV continues, and new strategies are under development. Success to prevent RSV disease was met by the development of immunoprophylaxis, first with intravenous immunoglobulin and then with recombinant monoclonal antibody. The story of immunoprophylaxis for RSV includes the first-in-class use of antibody technology for infectious disease, and palivizumab currently remains the only way to prevent serious lower respiratory tract disease due to RSV infection.

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Prevention of Respiratory Syncytial Virus Infection: From Vaccine to Antibody
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Citation: Huang K, Wu H. 2014. Prevention of respiratory syncytial virus infection: from vaccine to antibody. microbiolspec 2(4): doi:10.1128/microbiolspec.AID-0014-2014
/content/microbiolspec/10.1128/microbiolspec.AID-0014-2014.fig1
FIGURE 1
The illustration depicts the mechanism of action of RSV-neutralizing mAbs, palivizumab and motavizumab. An RSV virion is illustrated at the top left corner showing that the F and G proteins are located on the surface of the virion and the drawing below depicts G-protein-mediated attachment to cells followed by F protein mediated virus-cell fusion. The steps of fusion are shown on the top right. F protein also mediates cell-to-cell fusion resulting in syncytium formation, depicted in the middle drawing. In the final drawing on the bottom, an RSV-neutralizing antibody, either palivizumab or motavizumab, binds to F protein and blocks virus replication. It was determined that palivizumab and motavizumab do not inhibit RSV attachment, but rather F-protein-mediated virus-cell fusion and syncytia formation as reported recently ( 99 ).
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FIGURE 1

The illustration depicts the mechanism of action of RSV-neutralizing mAbs, palivizumab and motavizumab. An RSV virion is illustrated at the top left corner showing that the F and G proteins are located on the surface of the virion and the drawing below depicts G-protein-mediated attachment to cells followed by F protein mediated virus-cell fusion. The steps of fusion are shown on the top right. F protein also mediates cell-to-cell fusion resulting in syncytium formation, depicted in the middle drawing. In the final drawing on the bottom, an RSV-neutralizing antibody, either palivizumab or motavizumab, binds to F protein and blocks virus replication. It was determined that palivizumab and motavizumab do not inhibit RSV attachment, but rather F-protein-mediated virus-cell fusion and syncytia formation as reported recently ( 99 ).

Source: microbiolspec August 2014 vol. 2 no. 4 doi:10.1128/microbiolspec.AID-0014-2014
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FIGURE 2a
(A) Palivizumab was generated by CDR-grafting humanization of murine mAb 1129. Murine CDR regions are depicted in ball structure. The remaining regions are human origin. (B) Top view of the six murine CDRs that were grafted to human frameworks.
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FIGURE 2a

(A) Palivizumab was generated by CDR-grafting humanization of murine mAb 1129. Murine CDR regions are depicted in ball structure. The remaining regions are human origin. (B) Top view of the six murine CDRs that were grafted to human frameworks.

Source: microbiolspec August 2014 vol. 2 no. 4 doi:10.1128/microbiolspec.AID-0014-2014
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FIGURE 2b
(A) Palivizumab was generated by CDR-grafting humanization of murine mAb 1129. Murine CDR regions are depicted in ball structure. The remaining regions are human origin. (B) Top view of the six murine CDRs that were grafted to human frameworks.
microbiolspec/2/4/AID-0014-2014-fig2b_thmb.gif
microbiolspec/2/4/AID-0014-2014-fig2b.gif
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FIGURE 2b

(A) Palivizumab was generated by CDR-grafting humanization of murine mAb 1129. Murine CDR regions are depicted in ball structure. The remaining regions are human origin. (B) Top view of the six murine CDRs that were grafted to human frameworks.

Source: microbiolspec August 2014 vol. 2 no. 4 doi:10.1128/microbiolspec.AID-0014-2014
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