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J Gen Virol 88 (2007), 2719-2723; DOI 10.1099/vir.0.82753-0

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Short Communication

Characterization of the epitope for anti-human respiratory syncytial virus F protein monoclonal antibody 101F using synthetic peptides and genetic approaches

Sheng-Jiun Wu1, Albert Schmidt1, Eric J. Beil1, Nicole D. Day2, Patrick J. Branigan2, Changbao Liu2, Lester L. Gutshall2, Concepción Palomo3, Julie Furze4, Geraldine Taylor4, José A. Melero3, Ping Tsui5, Alfred M. Del Vecchio2 and Marian Kruszynski1

1 Protein Engineering, Centocor R&D Inc., 145 King of Prussia Road, Radnor, PA 19087, USA
2 Immunobiology, Centocor R&D Inc., 145 King of Prussia Road, Radnor, PA 19087, USA
3 Centro Nacional de Microbiología, Instituto de Salud Carlos III, Majadahonda, 28220 Madrid, Spain
4 Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, UK
5 Molecular Discovery Technologies, Centocor R&D Inc., 145 King of Prussia Road, Radnor, PA 19087, USA

Correspondence
Marian Kruszynski
mkruszy2{at}cntus.jnj.com

Chimeric 101F (ch101F) is a mouse–human chimeric anti-human respiratory syncytial virus (HRSV) neutralizing antibody that recognizes residues within antigenic site IV, V, VI of the fusion (F) glycoprotein. The binding of ch101F to a series of peptides overlapping aa 422–438 spanning antigenic site IV, V, VI was analysed. Residues 423–436 comprise the minimal peptide sequence for ch101F binding. Substitution analysis revealed that R429 and K433 are critical for ch101F binding, whilst K427 makes a minor contribution. Binding of ch101F to a series of single mutations at positions 427, 429 and 433 in the F protein expressed recombinantly on the cell surface confirmed the peptide results. Sequence analysis of viruses selected for resistance to neutralization by ch101F indicated that a single change (K433T) in the F protein allowed ch101F escape. The results confirm that ch101F and palivizumab have different epitope specificity and define key residues for ch101F recognition.






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