129-Prnptm1Canc/H

Status

Available to order

EMMA IDEM:11451
Citation informationRRID:IMSR_EM:11451 

Research Resource Identifiers (RRID) are persistent unique ID numbers assigned to help researchers cite key resources (e.g. antibodies, model organisms and software projects) in the biomedical literature to improve transparency and reproducibility in research. See https://www.rrids.org/ for more information.

 
International strain name129-Prnptm1Canc/H
Alternative nameG1
Strain typeTargeted Mutant Strains : Point mutation
Allele/Transgene symbolPrnptm1Canc
Gene/Transgene symbolPrnp

Information from provider

ProviderJean Manson
Provider affiliationThe Roslin Institute
Genetic informationTargeted mutant mice carrying the Prnp substitution threonine for asparagine at position 180 which eliminates the first Prnp N-glycosylation site.
Phenotypic informationHomozygous:
Appear to develop normally with no overt phenotype

Heterozygous:
Appear to develop normally with no overt phenotype
References
  • Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties.;Cancellotti Enrico, Wiseman Frances, Tuzi Nadia L, Baybutt Herbert, Monaghan Paul, Aitchison Lorraine, Simpson Jennifer, Manson Jean C, ;2005;The Journal of biological chemistry;280;42909-18; 16219759
  • Host PrP glycosylation: a major factor determining the outcome of prion infection.;Tuzi Nadia L, Cancellotti Enrico, Baybutt Herbert, Blackford Lorraine, Bradford Barry, Plinston Chris, Coghill Anne, Hart Patricia, Piccardo Pedro, Barron Rona M, Manson Jean C, ;2008;PLoS biology;6;e100; 18416605
  • Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties.;Cancellotti Enrico, Mahal Sukhvir P, Somerville Robert, Diack Abigail, Brown Deborah, Piccardo Pedro, Weissmann Charles, Manson Jean C, ;2013;The EMBO journal;32;756-69; 23395905
  • The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species.;Wiseman Frances K, Cancellotti Enrico, Piccardo Pedro, Iremonger Kayleigh, Boyle Aileen, Brown Deborah, Ironside James W, Manson Jean C, Diack Abigail B, ;2015;Journal of virology;89;4738-47; 25673720
Homozygous fertileyes
Homozygous viableyes
Homozygous matings requiredyes
Immunocompromisedno

Information from EMMA

Archiving centreMary Lyon Centre at MRC Harwell, Oxford, United Kingdom

Disease and phenotype information

Orphanet associated rare diseases, based on orthologous gene matching

MGI phenotypes (gene matching)
  • impaired fertilization / MGI
  • abnormal spleen morphology / MGI
  • tremors / MGI
  • abnormal cerebral cortex morphology / MGI
  • abnormal hippocampus morphology / MGI
  • abnormal olfactory bulb morphology / MGI
  • abnormal thalamus morphology / MGI
  • abnormal cerebellum morphology / MGI
  • Purkinje cell degeneration / MGI
  • decreased Purkinje cell number / MGI
  • abnormal cerebellar molecular layer / MGI
  • thin cerebellar molecular layer / MGI
  • abnormal retina morphology / MGI
  • ataxia / MGI
  • hypoactivity / MGI
  • impaired coordination / MGI
  • reduced long term potentiation / MGI
  • abnormal sleep pattern / MGI
  • abnormal body temperature homeostasis / MGI
  • male infertility / MGI
  • premature death / MGI
  • abnormal muscle physiology / MGI
  • abnormal brain morphology / MGI
  • no abnormal phenotype detected / MGI
  • gliosis / MGI
  • abnormal CNS synaptic transmission / MGI
  • neurodegeneration / MGI
  • spongiform encephalopathy / MGI
  • decreased vertical activity / MGI
  • abnormal inhibitory postsynaptic potential / MGI
  • abnormal inhibitory postsynaptic currents / MGI
  • no phenotypic analysis / MGI
  • increased neuron apoptosis / MGI
  • neuron degeneration / MGI
  • astrocytosis / MGI
  • abnormal voluntary movement / MGI
  • nervous system phenotype / MGI
  • abnormal nervous system morphology / MGI
  • impaired acrosome reaction / MGI
  • abnormal behavior / MGI
  • abnormal neuronal precursor proliferation / MGI
  • decreased susceptibility to prion infection / MGI
  • increased susceptibility to prion infection / MGI
  • behavior/neurological phenotype / MGI
  • immune system phenotype / MGI
  • teratozoospermia / MGI
  • brain vacuoles / MGI
  • abnormal brain white matter morphology / MGI
  • abnormal hippocampus CA1 region morphology / MGI
  • decreased neuron number / MGI
  • abnormal neuron differentiation / MGI
  • abnormal neuron proliferation / MGI
  • decreased brain copper level / MGI
  • enlarged brain ventricles / MGI
  • cerebellum atrophy / MGI
  • altered susceptibility to prion infection / MGI

Literature references

  • Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties.;Cancellotti Enrico, Wiseman Frances, Tuzi Nadia L, Baybutt Herbert, Monaghan Paul, Aitchison Lorraine, Simpson Jennifer, Manson Jean C, ;2005;The Journal of biological chemistry;280;42909-18; 16219759
  • Host PrP glycosylation: a major factor determining the outcome of prion infection.;Tuzi Nadia L, Cancellotti Enrico, Baybutt Herbert, Blackford Lorraine, Bradford Barry, Plinston Chris, Coghill Anne, Hart Patricia, Piccardo Pedro, Barron Rona M, Manson Jean C, ;2008;PLoS biology;6;e100; 18416605
  • Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties.;Cancellotti Enrico, Mahal Sukhvir P, Somerville Robert, Diack Abigail, Brown Deborah, Piccardo Pedro, Weissmann Charles, Manson Jean C, ;2013;The EMBO journal;32;756-69; 23395905
  • The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species.;Wiseman Frances K, Cancellotti Enrico, Piccardo Pedro, Iremonger Kayleigh, Boyle Aileen, Brown Deborah, Ironside James W, Manson Jean C, Diack Abigail B, ;2015;Journal of virology;89;4738-47; 25673720

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