A monoclonal antibody (mAb) S45-18 was generated against a synthetic neoglycoconjugate containing the trisaccharide αXKdop(2→4)αXKdop(2→4)αKdo (Kdo, 3-deoxy-D-manno-oct-2-ulopyranosonic acid) which represents a structure of the lipopolysaccharide (LPS) from Chlamydophila psittaci 6BC. The antibody was characterized by binding and inhibition assays in ELISA using: (i) the immunizing antigen and chemically synthesized derivatives thereof; (ii) chlamydial elementary bodies (EB); and (iii) LPS of Chl. psittaci 6BC and Chlamydia trachomatis L2. The specificity was determined in comparison to that of mAb S25-23 recognizing the αXKdop(2→8)αXKdop(2→4)αKdo trisaccharide which represents an epitope shared by all species of the family. MAb S45-18 bound to an epitope of the structure αXKdop(2→4)αXKdop(2→4)αKdo, with lower reactivity with the (2→8)-(2→4)-linked analog. Using chlamydial EB or LPS, mAb S45-18 bound preferentially to LPS and EB of Chl. psittaci. Therefore, Chl. psittaci LPS contains, in addition to the known genus-specific epitope, a species-specific epitope
lipopolysaccharides, 3-deoxy-D-manno-oct-2-ulosonic acid, antibody specificity, Chlamydia, Chlamydia trachomatis, Chlamydophila psittaci, epitopes, glycoconjugates, MAb
NCBI PubMed ID: 11521056Journal NLM ID: 9433350Publisher: Maney Publishing
Correspondence: hbrade@fz-borstel.de
Institutions: Division of Medical and Biochemical Microbiology, Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany
Methods: ELISA
Found