Purification and partial characterization of a type-specific antigen of Rickettsia tsutsugamushi.
A type-specific antigen (54- to 56-kilodalton polypeptide) in the envelope of Rickettsia tsutsugamushi was purified from each of three prototype strains (Gilliam, Karp, and Kato) by a combination of mild anionic detergent treatment, gel filtration, and reverse-phase high-performance liquid chromatography. The purified antigens from the three strains were shown to have similar amino acid compositions: primarily aspartic acid, glutamic acid, and glycine, with lesser amounts of cysteine, methionine, and tyrosine. The N-terminal amino acid sequences of the antigens were 74.3% homologous among the three strains.
Ohashi
N
N
Department of Microbiology, Niigata College of Pharmacy, Japan.
Tamura
A
A
Ohta
M
M
Hayashi
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000942:Antigens, Bacterial / Q000302:isolation & purification*; D000954:Antigens, Surface / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012285:Orientia tsutsugamushi / Q000032:analysis / Q000276:immunology*
D000596:Amino Acids; D000942:Antigens, Bacterial; D000954:Antigens, Surface