Abstract
Monoclonal antibody resistant (MAR) mutants (which escaped antibody-mediated neutralization) were selected from simian (W 3) and human (LN) isolates of simian virus 5 (SV 5), using monoclonal antibodies (MAbs) specific for antigenic sites 4 and 5 on the HN glycoprotein. Resistance correlated with an inability of the selecting antibody to bind with the respective MAR mutants. Sequence comparisons between parental and mutant HN proteins revealed multiple non-adjacent amino acid substitutions in the majority of MAR mutants. The same multiple substitutions were identified in mutants selected from both the LN and W 3 isolates of SV 5. Furthermore, different mutations on the primary sequence of the HN protein conferred resistance to the same MAb.
| Original language | English |
|---|---|
| Pages (from-to) | 217-24 |
| Number of pages | 8 |
| Journal | Archives of Virology |
| Volume | 131 |
| Issue number | 02-Jan |
| Publication status | Published - 1993 |
Keywords
- HEMAGGLUTININ NEURAMINIDASE GLYCOPROTEIN
- PARAINFLUENZA VIRUS TYPE-2
- SEQUENCE-ANALYSIS
- SIMIAN VIRUS-5
- NUCLEOTIDE-SEQUENCE
- MESSENGER-RNA
- SENDAI VIRUS
- PATHOGENICITY