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Isolation of Fidelity Variants of RNA Viruses and Characterization of Virus Mutation Frequency
Published on: June 16, 2011
Genetic variability of the glycoprotein genes of current wild-type measles isolates
J S Rota1, K B Hummel, P A Rota
1National Center for Infectious Diseases, Centers for Disease Control, Atlanta, Georgia 30333.
Abstract:
The glycoprotein coding sequences from three wild-type measles viruses isolated in the United States during 1988-1989 were examined by mRNA templated sequencing to determine whether contemporary strains have undergone genetic changes relative to the vaccine strain, Moraten. These studies revealed variation in the hemagglutinin (HA) gene and, to a far lesser degree, the fusion (F) gene. The F protein coding region was highly conserved with only three predicted amino acid changes. Among the predicted amino acid changes identified in the HA was a new potential glycosylation site at residue 416, located toward the carboxy-terminal end of the HA peptide. Eighty percent of the predicted amino acid changes in the HA shared by the three wild-type isolates were clustered near the five previously identified potential glycosylation sites. A linear pattern of evolutionary change was observed after comparing the predicted amino acid HA changes from the 1988-1989 viruses to those predicted in the HA protein from U.S. wild types isolated in 1977 and 1983.
Insights
Measles virus (MeV) glycoprotein genes were sequenced to detect genetic changes. Contemporary MeV strains show variations in hemagglutinin (HA) and fusion (F) genes compared to the vaccine strain.
Area of Science:
- Virology
- Molecular Biology
- Genetics
Background:
- Measles virus (MeV) poses a significant public health threat.
- Understanding genetic variations in wild-type MeV is crucial for vaccine efficacy and disease control.
- The Moraten vaccine strain serves as a reference for contemporary MeV genetic analysis.
Purpose of the Study:
- To investigate genetic alterations in glycoprotein coding sequences of wild-type measles viruses isolated in the U.S. (1988-1989).
- To compare contemporary wild-type MeV strains with the established Moraten vaccine strain.
- To identify evolutionary patterns in measles virus genes.
Main Methods:
- mRNA-templated sequencing was employed to analyze glycoprotein genes.
- Specific focus on hemagglutinin (HA) and fusion (F) genes.
- Comparative analysis of predicted amino acid changes in HA and F proteins.
Main Results:
- Significant variations were observed in the hemagglutinin (HA) gene.
- The fusion (F) gene exhibited high conservation with minimal predicted amino acid changes.
- A novel potential glycosylation site was identified in the HA protein (residue 416).
- Eighty percent of HA amino acid changes clustered near previously known glycosylation sites.
- A linear evolutionary pattern was detected in HA protein changes from 1977 to 1989.
Conclusions:
- Contemporary wild-type measles viruses display genetic divergence from the Moraten vaccine strain, particularly in the HA gene.
- The identified variations, including a new glycosylation site, may influence viral properties.
- Evolutionary analysis reveals a consistent pattern of genetic change in the HA gene over time.
