Structures of respiratory syncytial virus G antigen bound to broadly neutralizing antibodies

See allHide authors and affiliations

Science Immunology  09 Mar 2018:
Vol. 3, Issue 21, eaar3534
DOI: 10.1126/sciimmunol.aar3534

You are currently viewing the editor's summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

Structural insights

Respiratory syncytial virus (RSV) causes respiratory infections associated with severe morbidity and mortality in infants, young children, and the elderly, and currently, no licensed vaccine exists. Fedechkin et al. now describe cocrystal structures of the RSV G glycoprotein conserved central domain (CCD) bound by two different broadly neutralizing monoclonal antibodies (mAbs). Both mAbs bind to conformational epitopes on this highly conserved region. The RSV G CCD can activate CX3CR1, and this activity can be blocked by binding of these mAbs. These findings provide structural insights into how neutralizing mAbs interact with the RSV G glycoprotein and may advance the development of new RSV vaccines and therapeutics.