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Molecular Characterization of Hamster-Adapted Yellow Fever Virus
Monica A McArthur1,2, Shuliu L Zhang3, Li Li3,4
1Center for Vaccine Development and Global Health, University of Maryland School of Medicine, Baltimore, Maryland.
Abstract:
We previously reported two hamster models for viscerotropic yellow fever virus (YFV) infection: one using a YFV strain (Jiménez), isolated from a fatal human case in Panama in 1974, and the other using the prototype YFV strain (Asibi). Asibi hamster passage 7 (P7) was associated with accumulation of seven amino acid substitutions, including five in the envelope protein. In this study we report the genome sequences of the hamster Jiménez P0 and P10 viruses in which we identified only two amino acid substitutions during passage, one each in the nonstructural proteins NS3 and NS5, indicating a role for the nonstructural proteins in increased YFV viscerotropism in the Jiménez hamster model. Thus, there are multiple molecular mechanisms involved in viscerotropism of YFV in the hamster model. Neither Asibi P7 nor Jiménez P10 viruses were viscerotropic in mice or guinea pigs. Thus, the hamster viscerotropic phenotype did not translate to other laboratory rodent species.
Insights
Researchers identified distinct genetic changes in yellow fever virus (YFV) strains adapted to hamsters. Nonstructural proteins play a key role in YFV viscerotropism, but this hamster adaptation doesn't extend to other rodent models.
Area of Science:
- Virology
- Molecular Biology
- Infectious Diseases
Background:
- Two hamster models for viscerotropic yellow fever virus (YFV) infection were previously established using the Jiménez and Asibi strains.
- The Asibi strain (passage 7) showed seven amino acid substitutions, five in the envelope protein, upon adaptation to hamsters.
Purpose of the Study:
- To determine the genome sequences and identify genetic changes in the Jiménez YFV strain after adaptation to hamsters.
- To elucidate the molecular mechanisms underlying YFV viscerotropism in the Jiménez hamster model.
- To assess the cross-species applicability of the YFV hamster viscerotropic phenotype in other rodent models.
Main Methods:
- Whole-genome sequencing of the Jiménez YFV strain at passage 0 (P0) and passage 10 (P10) in hamsters.
- Amino acid substitution analysis in viral proteins.
- Inoculation of mice and guinea pigs with adapted YFV strains (Asibi P7 and Jiménez P10) to evaluate viscerotropism.
Main Results:
- The Jiménez YFV strain acquired only two amino acid substitutions by passage 10 in hamsters, located in the nonstructural proteins NS3 and NS5.
- These findings suggest a significant role for nonstructural proteins in enhancing YFV viscerotropism in the Jiménez hamster model.
- Neither the Asibi P7 nor the Jiménez P10 YFV strains exhibited viscerotropism in mice or guinea pigs, indicating a lack of cross-species translation of the hamster-adapted phenotype.
Conclusions:
- Multiple distinct molecular mechanisms contribute to YFV viscerotropism in hamster models.
- Nonstructural protein modifications are critical for YFV viscerotropism in the Jiménez hamster model.
- The YFV viscerotropic phenotype observed in hamsters is not transferable to other common laboratory rodent species such as mice and guinea pigs.
