Dysferlin (DYSF) is a calcium dependent membrane associated protein implicated in membrane repair, vesicle trafficking and T-tubule function. Mutations in DYSF encoding the dysferlin protein cause primary dysferlinopathies; autosomal recessive diseases that present clinically as Limb Girdle Muscular Dystrophy type 2 B (LGMD2B), Myoshi myopathy and distal myopathy. More than 350 pathogenic mutations in DYSF have been reported within exons or near intron-exon boundaries. Due to the large size of the DYSF mRNA, AAV vector mediated gene transfer may be challenging. In recent studies, CRISPR Cas9 was used to correct DYSF mutations in vitro, however the efficiency was low, and therefore, alternative methods are required. We hypothesize that antisense mediated exon skipping strategies could be used for some dysferlinopathy patients to restore dysferlin function by inframe exon skipping. 2´O Methyl antisense oligomers on a Phosphorothioate backbone (2OMeAOs) were designed to skip exons 2, 25, 30, 32, 34, 35, 36 and 37 and transfected into normal human myoblasts. The 2OMeAOs targeting in-frame exons 30 and 32 induced almost 100% skipping at 400 nM The most effective exon 32 skipping AO was resynthesised as a phosphordiamidate morpholino oligomer and induced up to 90% exon 32 skipping in the patient myotubes. The loss of DYSF exon 32 has been shown by others to be associated with a milder presentation of LGMD2B. Antisense oligomer induced skipping of exon 32 seems to be viable method to correct DYSF function for amenable mutations, and we will now explore the redundancy