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A frameshift variant in the COL5A1 gene in a cat with Ehlers-Danlos syndrome. 2018

M Spycher, and A Bauer, and V Jagannathan, and M Frizzi, and M De Lucia, and T Leeb
Institute of Genetics, Vetsuisse Faculty, University of Bern, 3001, Bern, Switzerland.

Ehlers-Danlos syndrome (EDS) is a group of heritable connective tissue disorders caused by defective collagen synthesis or incorrect assembly of the collagen triple helical structure. EDS is characterised by joint hypermobility, skin hyperextensibility, abnormal scarring, poor wound healing and tissue friability. Human EDS may be caused by variants in several different genes including COL5A1, which encodes the collagen type V alpha 1 chain. For the present study we investigated a 1.5-year-old, spayed female, domestic shorthair cat with EDS. The affected cat showed multiple recurrent skin tears, hyperextensibility of the skin and joint abnormalities. We obtained whole genome sequencing data from the affected cat and searched for variants in candidate genes known to cause EDS. We detected a heterozygous single base-pair deletion in exon 43 of the COL5A1 gene, namely c.3420delG. The deletion was predicted to result in a frameshift and premature stop codon: p.(Leu1141SerfsTer134). Sanger sequencing confirmed that the variant was present in the affected cat and absent from 103 unaffected cats from different breeds. The variant was also absent from a Burmese cat with EDS. Based on knowledge about the functional impact of COL5A1 variants in other species, COL5A1:c.3420delG represents a compelling candidate causative variant for the observed EDS in the affected cat.

UI MeSH Term Description Entries
D002371 Cat Diseases Diseases of the domestic cat (Felis catus or F. domesticus). This term does not include diseases of the so-called big cats such as CHEETAHS; LIONS; tigers, cougars, panthers, leopards, and other Felidae for which the heading CARNIVORA is used. Feline Diseases,Cat Disease,Disease, Cat,Disease, Feline,Diseases, Cat,Diseases, Feline,Feline Disease
D002415 Cats The domestic cat, Felis catus, of the carnivore family FELIDAE, comprising over 30 different breeds. The domestic cat is descended primarily from the wild cat of Africa and extreme southwestern Asia. Though probably present in towns in Palestine as long ago as 7000 years, actual domestication occurred in Egypt about 4000 years ago. (From Walker's Mammals of the World, 6th ed, p801) Felis catus,Felis domesticus,Domestic Cats,Felis domestica,Felis sylvestris catus,Cat,Cat, Domestic,Cats, Domestic,Domestic Cat
D004535 Ehlers-Danlos Syndrome A heterogeneous group of autosomally inherited COLLAGEN DISEASES caused by defects in the synthesis or structure of FIBRILLAR COLLAGEN. There are numerous subtypes: classical, hypermobility, vascular, and others. Common clinical features include hyperextensible skin and joints, skin fragility and reduced wound healing capability. Cutis Elastica,Ehlers Danlos Disease,Ehlers-Danlos Disease,Danlos Disease, Ehlers,Disease, Ehlers Danlos,Disease, Ehlers-Danlos,Ehlers Danlos Syndrome,Syndrome, Ehlers-Danlos
D005091 Exons The parts of a transcript of a split GENE remaining after the INTRONS are removed. They are spliced together to become a MESSENGER RNA or other functional RNA. Mini-Exon,Exon,Mini Exon,Mini-Exons
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012868 Skin Abnormalities Congenital structural abnormalities of the skin. Abnormalities, Skin,Abnormality, Skin,Skin Abnormality
D016368 Frameshift Mutation A type of mutation in which a number of NUCLEOTIDES deleted from or inserted into a protein coding sequence is not divisible by three, thereby causing an alteration in the READING FRAMES of the entire coding sequence downstream of the mutation. These mutations may be induced by certain types of MUTAGENS or may occur spontaneously. Mutation, Frameshift,Frame Shift Mutation,Out-of-Frame Deletion,Out-of-Frame Insertion,Out-of-Frame Mutation,Deletion, Out-of-Frame,Deletions, Out-of-Frame,Frame Shift Mutations,Frameshift Mutations,Insertion, Out-of-Frame,Insertions, Out-of-Frame,Mutation, Frame Shift,Mutation, Out-of-Frame,Mutations, Frame Shift,Mutations, Frameshift,Mutations, Out-of-Frame,Out of Frame Deletion,Out of Frame Insertion,Out of Frame Mutation,Out-of-Frame Deletions,Out-of-Frame Insertions,Out-of-Frame Mutations
D017384 Sequence Deletion Deletion of sequences of nucleic acids from the genetic material of an individual. Deletion Mutation,Deletion Mutations,Deletion, Sequence,Deletions, Sequence,Mutation, Deletion,Mutations, Deletion,Sequence Deletions
D018389 Codon, Nonsense An amino acid-specifying codon that has been converted to a stop codon (CODON, TERMINATOR) by mutation. Its occurance is abnormal causing premature termination of protein translation and results in production of truncated and non-functional proteins. A nonsense mutation is one that converts an amino acid-specific codon to a stop codon. Codon, Termination, Premature,Codon, Unassigned,Mutation, Nonsense,Nonsense Codon,Nonsense Mutation,Premature Stop Codon,Unassigned Codon,Amber Nonsense Codon,Amber Nonsense Mutation,Nonsense Codon, Amber,Ochre Nonsense Codon,Ochre Nonsense Mutation,Opal Nonsense Codon,Opal Nonsense Mutation,Premature Termination Codon,Amber Nonsense Codons,Amber Nonsense Mutations,Codon, Amber Nonsense,Codon, Ochre Nonsense,Codon, Opal Nonsense,Codon, Premature Stop,Codon, Premature Termination,Codons, Amber Nonsense,Codons, Nonsense,Codons, Ochre Nonsense,Codons, Opal Nonsense,Codons, Premature Stop,Codons, Premature Termination,Codons, Unassigned,Mutation, Amber Nonsense,Mutation, Ochre Nonsense,Mutation, Opal Nonsense,Mutations, Amber Nonsense,Mutations, Nonsense,Mutations, Ochre Nonsense,Mutations, Opal Nonsense,Nonsense Codon, Ochre,Nonsense Codon, Opal,Nonsense Codons,Nonsense Codons, Amber,Nonsense Codons, Ochre,Nonsense Codons, Opal,Nonsense Mutation, Amber,Nonsense Mutation, Ochre,Nonsense Mutation, Opal,Nonsense Mutations,Nonsense Mutations, Amber,Nonsense Mutations, Ochre,Nonsense Mutations, Opal,Ochre Nonsense Codons,Ochre Nonsense Mutations,Opal Nonsense Codons,Opal Nonsense Mutations,Premature Stop Codons,Premature Termination Codons,Stop Codon, Premature,Stop Codons, Premature,Termination Codon, Premature,Termination Codons, Premature,Unassigned Codons
D024062 Collagen Type V A fibrillar collagen found widely distributed as a minor component in tissues that contain COLLAGEN TYPE I and COLLAGEN TYPE III. It is a heterotrimeric molecule composed of alpha1(V), alpha2(V) and alpha3(V) subunits. Several forms of collagen type V exist depending upon the composition of the subunits that form the trimer. Collagen Type V, alpha1 Chain,Collagen Type V, alpha1 Subunit,Collagen Type V, alpha2 Chain,Collagen Type V, alpha2 Subunit,Collagen Type V, alpha3 Chain,Collagen Type V, alpha3 Subunit,Collagen alpha1(V),Collagen alpha2(V),Collagen alpha3(V),Procollagen Type V,Type V Collagen,Type V Procollagen,Collagen, Type V,Procollagen, Type V,V Procollagen, Type

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