Purification, partial characterization, and seroreactivity of a genuswide 60-kilodalton Legionella protein antigen.
A genuswide protein antigen extracted from Legionella pneumophila serogroup 1 (strain Philadelphia 1) cells was enriched by differential pelleting and ammonium sulfate precipitation and subsequently purified with a combination of high-performance size-exclusion and ion-exchange chromatography. The protein has an apparent molecular weight of 650,000 before and 63,000 after urea (5 M) treatment, as determined by size-exclusion chromatography. These proteins resolved to a single band of 60,000 after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The urea-treated protein had an isoelectric point of 5.8. This purified 60-kilodalton protein reacted with a convalescent-phase serum sample from a patient with legionellosis and rabbit immune sera prepared against each of 23 Legionella species. The 60-kilodalton protein may be useful in developing diagnostic tests for legionellosis.
Pau
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CP
Department of Chemistry, Emory University, Atlanta, Georgia 30332.
Plikaytis
B B
BB
Carlone
G M
GM
Warner
I M
IM
D000818:Animals; D000907:Antibodies, Bacterial / Q000276:immunology; D000942:Antigens, Bacterial / Q000276:immunology / Q000302:isolation & purification*; D001426:Bacterial Proteins / Q000276:immunology / Q000302:isolation & purification*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007526:Isoelectric Point; D007875:Legionella / Q000145:classification / Q000276:immunology*; D008970:Molecular Weight; D011817:Rabbits
D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D001426:Bacterial Proteins