ABSTRACT
The potential resolving power of molecular epidemiological studies has enhanced the precision and reliability of poliovirus (PV) surveillance. PV has an error prone RNA polymerase responsible for rapid evolution of genome (approximately 10(-2) nt substitution/site/year), during inter and intra-human passages. The present study included a serotyped panel of 60 PV (42 PV type-1, 13 PV type-2 and 5 PV type-3) isolated during 1997. They were differentiated into vaccine (Sabin) and wild strains by two methods viz., genotype specific RNA probe hybridization (Rpro-Hy) based on genotypic variability; and ELISA that uses cross-absorbed antiserum (Pab-E) based on phenotypic variability. For obtaining information on molecular epidemiology, partial nucleotide sequencing (VP1/2A region) of five clinical PV isolates was also done. Three of the 60 isolates (two PV type-1 and one PV type-3) intratyped, could not be differentiated correctly by either method. Genotypic characterization of PV isolates was done for confirmation of intratyping results. All five wild PV1 sequenced belonged to the same genotype (> 85% homology) and sequence divergence among the strains was < or = 4.5 per cent. This indicated circulation of a single genetic lineage in the area.
Subject(s)
Base Sequence , Child , Child, Preschool , Genome, Viral , Humans , India/epidemiology , Infant , Molecular Sequence Data , Poliomyelitis/epidemiology , Poliovirus/genetics , RNA, Viral/genetics , Sequence AnalysisABSTRACT
The nucleotide sequences encoding the capsid protein VP1 were determined for the wild polioviruses of serotypes 1 and 3 endemic to the northeastern region of Brazil. Compared with the corresponding Sabin vaccine strain sequences, the wild isolates differed at 20%(type 1) and 22%(type 3) of their nucleotide positions, and in 7%(type 1) and 11%(type 3) of their amino acid residues. The highest degree of amino acid heterogeneity occurred within the amino-terminal residues of the VP1 proteins. Intratypic amino acid differences also occurred in VP1 surface residues that form parts of antigenic sites for neutralizing antibodies