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August 1, 1989Journal of VirologyOpen Access

Sindbis virus ts103 has a mutation in glycoprotein E2 that leads to defective assembly of virions

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Key result

A mutation in glycoprotein E2 (Ala-344 to Val) of Sindbis virus mutant ts103 leads to defective assembly of virions due to weakened interactions during budding.

Population

Sindbis virus mutant ts103 and parental strain

Comparison

Mutation in glycoprotein E2 (Ala-344 to Val) vs Parental strain of the virus

Design

Preclinical

Authors

CHChang S. HahnLeipzig UniversityCharles M. RiceCharles M. RiceUniversity of Notre DameESEllen G. StraussCalifornia Institute of Technology

Discussion

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Implication

Hypothesis-generating for E2-targeted antivirals; leaves open translation beyond this Sindbis model.

Structured PICO

P
Population
Sindbis virus mutant ts103 and parental strain
E
Exposure
Mutation in glycoprotein E2 (Ala-344 to Val)
C
Comparator
Parental strain of the virus
O
Outcome
Virus particle assembly and yield

The study identifies specific glycoprotein mutations responsible for defective virion assembly in Sindbis virus mutant ts103.

Cite This Study

Hahn et al. (1989) studied Sindbis virus. Sindbis virus mutant ts103 vs. Parental strain was evaluated on Virus assembly and budding. A mutation in glycoprotein E2 (Ala-344 to Val) of Sindbis virus mutant ts103 leads to defective assembly of virions due to weakened interactions during budding.

synapsesocial.com/papers/6a9d7bd79f8b6241c867f7e6https://doi.org/10.1128/jvi.63.8.3459-3465.1989
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