Premature stop codons in the G glycoprotein of human respiratory syncytial viruses resistant to neutralization by monoclonal antibodies.
AUTOR(ES)
Rueda, P
RESUMO
Mutants of human respiratory syncytial (RS) virus which escaped neutralization by monoclonal antibodies directed against the G glycoprotein were selected from the Long strain. Most mutants showed drastic antigenic changes, reflected in the lack of reactivity with several anti-G antibodies, including the one used for selection. Sequence analysis revealed the presence of in-frame premature stop codons in the mutated G genes which shortened the G polypeptide by between 11 and 42 amino acids. In contrast, two mutants selected with monoclonal antibody 25G contained two amino acid substitutions (Phe-265----Leu and Leu-274----Pro) and had lost only the capacity to bind the antibody used in their selection. These results demonstrate that the carboxy-terminal end of the G molecule is dispensable for infectivity in tissue culture and indicate the importance of this part of the G protein in determining its antigenicity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=241000Documentos Relacionados
- Neutralization of respiratory syncytial virus by individual and mixtures of F and G protein monoclonal antibodies.
- Isolation and characterization of a chimpanzee monoclonal antibody to the G glycoprotein of human respiratory syncytial virus.
- Protection from respiratory syncytial virus infection in cotton rats by passive transfer of monoclonal antibodies.
- Synergistic neutralization of human immunodeficiency virus type 1 by combinations of human monoclonal antibodies.
- Neutralizing and enhancing activities of human respiratory syncytial virus-specific antibodies.