Duchenne muscular dystrophy (DMD) is caused by mutations in
the dystrophin gene that often introduce frame shifts, resulting in the absence
of functional dystrophin and severe muscle degeneration. In contrast,
individuals with Becker muscular dystrophy produce a shorter but partially
functional dystrophin protein and experience a milder disease phenotype.

Antisense oligonucleotide therapies have been developed to
shift the DMD phenotype toward a Becker-like outcome. Which mechanism best
explains how antisense oligonucleotides achieve this effect?

Question

Duchenne muscular dystrophy (DMD) is caused by mutations in
the dystrophin gene that often introduce frame shifts, resulting in the absence
of functional dystrophin and severe muscle degeneration. In contrast,
individuals with Becker muscular dystrophy produce a shorter but partially
functional dystrophin protein and experience a milder disease phenotype.

Antisense oligonucleotide therapies have been developed to
shift the DMD phenotype toward a Becker-like outcome. Which mechanism best
explains how antisense oligonucleotides achieve this effect?

Accepted Answer

Inducing
exon skipping to restore the reading frame and allow production of a truncated,
functional dystrophin protein

Answer

Promoting
RNase H–mediated degradation of dystrophin mRNA to prevent toxic protein
production

Answer

Increasing
dystrophin gene transcription to compensate for the mutated allele

Answer

Blocking
ribosome binding to dystrophin mRNA to reduce translation of the mutant protein

Crowdly

Duchenne muscular dystrophy (DMD) is caused by mutations in the dystrophin gene...

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