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

DOI Web Site 被引用文献6件
  • C F Barbas
    Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
  • J E Crowe
    Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
  • D Cababa
    Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
  • T M Jones
    Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
  • S L Zebedee
    Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
  • B R Murphy
    Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
  • R M Chanock
    Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
  • D R Burton
    Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.

抄録

<jats:p>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.</jats:p>

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