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Human antibody recognition of antigenic site IV on Pneumovirus fusion proteins

Jarrod J Mousa1, Elad Binshtein2, Stacey Human3,4

  • 1Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, Tennessee, United States of America.

Plos Pathogens
|February 23, 2018
PubMed

Insights

Researchers identified new human antibodies targeting the Respiratory Syncytial Virus (RSV) fusion protein's antigenic site IV. These antibodies offer insights into RSV and human metapneumovirus (hMPV) cross-reactivity, potentially aiding pan-Pneumovirus vaccine development.

Area of Science:

  • Virology and Immunology
  • Vaccine Development

Background:

  • Respiratory Syncytial Virus (RSV) is a significant human pathogen, particularly affecting young children.
  • The RSV fusion (F) protein is a key target for neutralizing antibodies, with antigenic site IV being conserved across different F protein conformations.
  • Previous studies indicate that antibodies targeting antigenic site IV can neutralize both RSV and human metapneumovirus (hMPV).

Purpose of the Study:

  • To explore the diverse binding mechanisms of antibodies at antigenic site IV of the RSV F protein.
  • To investigate the basis of cross-reactivity between antibodies targeting RSV and hMPV F proteins.
  • To inform the design of novel vaccines, potentially a pan-Pneumovirus vaccine.

Main Methods:

  • Generation and characterization of a panel of human monoclonal antibodies (mAbs) against RSV F protein.
  • Competition-binding assays and site-directed mutagenesis to identify antibody binding sites and key residues (e.g., R429).
  • Neutralization assays against wild-type and mutant RSV strains, including cross-reactivity testing with hMPV.
  • Electron microscopy and peptide binding experiments to elucidate antibody-antigen interactions and binding poses.

Main Results:

  • Four new human mAbs targeting antigenic site IV were generated; two (3M3, 6F18) required R429 for binding and neutralization.
  • Two novel mAbs (17E10, 2N6) were identified that bind independently of R429 and neutralize an R429A mutant.
  • One mAb (17E10) demonstrated cross-neutralization of both RSV and hMPV, with a binding pose similar to the 101F antibody.
  • Binding pose of mAb 17E10 to RSV F protein was determined to be a potential indicator of hMPV cross-reactivity.

Conclusions:

  • Antibody binding pose at antigenic site IV is a critical factor influencing cross-reactivity between RSV and hMPV.
  • The characterization of site IV epitopes recognized by human antibodies provides valuable insights for RSV vaccine design.
  • These findings support the development of a pan-Pneumovirus vaccine targeting conserved epitopes across related viruses.

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