Allele-specific sequencing confirms novel prion gene polymorphism in Creutzfeldt-Jakob disease.
We analyzed the prion protein coding sequence in a familial Creutzfeldt-Jakob disease patient who did not have any of the currently recognized prion protein mutations. Denaturing gradient gel electrophoresis indicated that the prion protein coding sequence was heterozygous at least one location. We isolated each allele by denaturing gradient gel electrophoresis and directly sequenced. We found a DNA polymorphism at codon 178 that predicted the amino acid substitution, aspartate----asparagine. Whether this represents a benign polymorphism or pathogenic mutation will depend on analysis of the functional consequences of this change. Denaturing gradient gel electrophoresis and allele-specific sequencing proved to be efficient means of analyzing sequence polymorphisms in this gene.
Department of Neurology, University of Michigan, Ann Arbor.
J K
JK
Fink
J T
JT
Warren
I
I
Drury
D
D
Murman
M L
ML
Peacock
D000328:Adult; D000483:Alleles; D000595:Amino Acid Sequence; D007562:Creutzfeldt-Jakob Syndrome / Q000235:genetics*; D004586:Electrophoresis; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D011110:Polymorphism, Genetic; D011328:Prions
D011328:Prions