Human monoclonal antibodies isolated from spontaneous Epstein-Barr virus-transformed tumors of Hu-SPL-SCID mice and specific for fusion protein display broad neutralizing activity toward respiratory syncytial virus
S. Chamat et al., Human monoclonal antibodies isolated from spontaneous Epstein-Barr virus-transformed tumors of Hu-SPL-SCID mice and specific for fusion protein display broad neutralizing activity toward respiratory syncytial virus, J INFEC DIS, 180(2), 1999, pp. 268-277
Two human monoclonal antibodies, RF-1 and RF-2, specifically recognize the
fusion protein of the human respiratory syncytial virus (RSV), These were i
solated from spontaneous tumors in SCID mice reconstituted with human splen
ocytes and boosted with fusion protein. The tumors consisted of Epstein-Bar
r virus-transformed human B cells in animals with antigen-specific antibody
titers >10(5). The binding affinity of RF-1 and RF-2 to the fusion protein
is 10(10) and 10(9) M-1, respectively. The antibodies bind specifically to
a conformational epitope of the fusion protein on RSV-infected HEp-2 cells
, Both antibodies display virus-neutralizing properties in vitro at concent
rations varying between 8 and 1000 ng/mL, Virus neutralization applies to a
broad variety of wild and laboratory-adapted virus strains belonging to bo
th virus types A and B, These antibodies are potential candidates for passi
ve immunotherapy of severe RSV infections.