Human monoclonal Fab fragments derived from a combinatorial library bind to respiratory syncytial virus F glycoprotein and neutralize infectivity.

Barbas CF, Crowe JE, Cababa D, Jones TM, Zebedee SL, Murphy BR, Chanock RM, Burton DR
Proc Natl Acad Sci U S A. 1992 89 (21): 10164-8

PMID: 1279672 · PMCID: PMC50298 · DOI:10.1073/pnas.89.21.10164

Respiratory syncytial virus (RSV) is the most important cause, throughout the world, of severe viral lower respiratory tract illness in young children. Antibodies are known to mediate resistance to RSV infection and illness. We have isolated a number of human monoclonal Fab fragments to RSV F glycoprotein from a combinatorial antibody library expressed on the surface of phage. One of these neutralized a wide range of virus isolates, 10 subgroup A and 9 subgroup B isolates, with a titer (60% neutralization) of approximately 0.1-1.0 micrograms/ml. Another Fab neutralized diverse isolates at a concentration somewhat higher. These human Fab fragments show great promise for use in the prophylaxis or therapy of serious RSV lower respiratory tract disease. For intramuscular or intravenous administration, whole antibodies will be required, whereas for aerosol application, F(ab')2 or Fab fragments may suffice.

MeSH Terms (22)

Amino Acid Sequence Antibodies, Monoclonal Antigens, Viral Base Sequence Binding, Competitive Binding Sites, Antibody Enzyme-Linked Immunosorbent Assay Gene Library HIV Seropositivity HN Protein Humans Immunoglobulin Fab Fragments Immunoglobulin Variable Region Lymphocytes Molecular Sequence Data Neutralization Tests Oligodeoxyribonucleotides Respiratory Syncytial Viruses RNA Viral Envelope Proteins Viral Fusion Proteins Viral Proteins

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