Features of the Human Antibody Response against the Respiratory Syncytial Virus Surface Glycoprotein G

Kristina Borochova, Katarzyna Niespodziana, Katarina Stenberg Hammar, Marianne van Hage, Gunilla Hedlin, Cilla Söderhäll, Margarete Focke-Tejkl, Rudolf Valenta

Research output: Journal article (peer-reviewed)Journal article

5 Citations (Scopus)


Respiratory syncytial virus (RSV) infections are a major cause of serious respiratory disease in infants. RSV occurs as two major subgroups A and B, which mainly differ regarding the surface glycoprotein G. The G protein is important for virus attachment and G-specific antibodies can protect against infection. We expressed the surface-exposed part of A2 strain-derived G (A2-G) in baculovirus-infected insect cells and synthesized overlapping peptides spanning complete A2-G. The investigation of the natural IgG response of adult subjects during a period of one year showed that IgG antibodies (i) recognize G significantly stronger than the fusion protein F0, (ii) target mainly non-conformational, sequential peptide epitopes from the exposed conserved region but also buried peptides, and (iii) exhibit a scattered but constant recognition profile during the observation period. The IgG subclass reactivity profile (IgG1 > IgG2 > IgG4 = IgG3) was indicative of a mixed Th1/Th2 response. Two strongly RSV-neutralizing sera including the 1st WHO standard contained high IgG anti-G levels. G-specific IgG increased strongly in children after wheezing attacks suggesting RSV as trigger factor. Our study shows that RSV G and G-derived peptides are useful for serological diagnosis of RSV-triggered exacerbations of respiratory diseases and underlines the importance of G for development of RSV-neutralizing vaccines.

Original languageEnglish
Article number337
Pages (from-to)1-21
Number of pages21
Issue number2
Publication statusPublished - 25 Jun 2020


Dive into the research topics of 'Features of the Human Antibody Response against the Respiratory Syncytial Virus Surface Glycoprotein G'. Together they form a unique fingerprint.

Cite this