BIOLOGICAL-ACTIVITY, BINDING-SITE AND AFFINITY OF MONOCLONAL-ANTIBODIES TO THE FUSION PROTEIN OF RESPIRATORY SYNCYTIAL VIRUS

west W., LOUNSBACH g., BOURGEOIS c., robinson j., carter m., crompton s., ...More

JOURNAL OF GENERAL VIROLOGY, vol.75, pp.2813-2819, 1994 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 75
  • Publication Date: 1994
  • Doi Number: 10.1099/0022-1317-75-10-2813
  • Journal Name: JOURNAL OF GENERAL VIROLOGY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.2813-2819
  • Recep Tayyip Erdoğan University Affiliated: No

Abstract

The neutralizing activity and fusion-inhibition activity per unit weight of immunoglobulin were determined for each of a panel of 20 monoclonal antibodies (MAbs) to the fusion (F) protein of respiratory syncytial (RS) virus. Neutralization did not correlate with fusion-inhibiting activity, suggesting that the F protein plays at least two independent, antibody-sensitive roles in viral infection. Antibodies with the highest biological activity against A2, a subgroup A strain of RS virus, neutralized a subgroup B strain (8/60) poorly, suggesting a degree of antigenic variation that may be important in human infection.