Critical site differences of fusion protein between wildtype and vaccine measles virus strains in Indonesia
Background Measles virus can cause high morbidity andÂ mortality in infants and children. Fusion glycoprotein (F protein)Â found in the viral envelope is important for the host cell infectionÂ mechanism. F protein is immunogenic and may cause specificÂ immune responses in the host. High variability is found in the FÂ protein gene of vaccine viral strains compared to 'Wild type strains.Â This amino add sequence variability may result in a less specificÂ immune response against other strains, possibly rendering the
vaccine to be less effective.
Objective To detennine the amino add sequence differences inÂ critical sites of F protein in Mld type and vaccine measles virusÂ strains in Indonesia.
Methods We compared amino acid sequences of three genotypesÂ of Mld type measles virus (02, 03 and D9) to those of theÂ vaccine strains, CAMô€€¸ 70, Schwarz, and Edmonstonô€€¸wt typeÂ measles virus.
Resul ts Analysis showed that there were differences at Flô€€¸F2Â cleavage site, B cell epitopes, and H protein binding site betweenÂ the CAMô€€¸70 vaccine viral strains and Mld type strains. SchwarzÂ vaccine strain differed from the wild type strains at the H proteinÂ binding site. A 03 wild type strain potential glycosylation site wasÂ also different from all other strains studied.
Conclusion There were differences in the critical sites of F proteinÂ between Mld type strains and the CAMô€€¸70 and Schwarz vaccineÂ strains.Â
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