Partial characterization of an 89-kDa highly immunoreactive protein from Chlamydia psittaci A/22 causing ovine abortion.
An 89-kDa immunogen from Chlamydia psittaci A/22 causing ovine abortion was partially characterized. The 89-kDa protein, localized on the outer membrane complex of chlamydiae, was synthesized relatively early in the developmental cycle. The protein contained cysteine but was not extensively cross-linked by disulfide bonds. Treatment with proteases apparently did not cleave the protein. The infectivity of strain A/22 was partially (60%) reduced by treatment of chlamydial elementary bodies with monoclonal antibody BS/89 specifically reacting with the 89-kDa antigen. Species-specific as well as strain-specific antigenic determinants were present on the 89-kDa protein.
Cevenini
R
R
Instituto di Microbiologia, University of Bologna, Italy.
Donati
M
M
Brocchi
E
E
De Simone
F
F
La Placa
M
M
D000034:Abortion, Veterinary / Q000209:etiology*; D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D002691:Chlamydophila psittaci / Q000032:analysis* / Q000472:pathogenicity; D003545:Cysteine / Q000032:analysis; D010450:Endopeptidases / Q000494:pharmacology; D000939:Epitopes / Q000032:analysis; D005260:Female; D008623:Mercaptoethanol / Q000494:pharmacology; D011247:Pregnancy; D012521:Sarcosine / Q000031:analogs & derivatives / Q000494:pharmacology; D012756:Sheep; D012757:Sheep Diseases / Q000209:etiology*
D001425:Bacterial Outer Membrane Proteins; D000939:Epitopes; D008623:Mercaptoethanol; C025231:sarkosyl; D010450:Endopeptidases; D003545:Cysteine; D012521:Sarcosine