Journal of Endotoxin Research

 

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Journal of Endotoxin Research, Vol. 6, No. 5, 361-368 (2000)
DOI: 10.1177/09680519000060050601
© 2000 SAGE Publications

A monoclonal antibody recognizing the 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) trisaccharide {alpha}Kdo(2->4){alpha}Kdo(2->4){alpha}Kdo of Chlamydophila spacepsittaci 6BC lipopolysaccharide

Lore Brade

Division of Medical and Biochemical Microbiology, Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany, hbrade{at}fz-borstel.de

Antoni Rozalski

Division of Medical and Biochemical Microbiology, Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany

Paul Kosma

Institute of Chemistry, University of Agriculture, Vienna, Austria

Helmut Brade

Division of Medical and Biochemical Microbiology, Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany

A monoclonal antibody (mAb) S45-18 was generated against a synthetic neoglycoconjugate containing the trisaccharide {alpha}Kdo(2->4){alpha}Kdo(2->4){alpha}Kdo (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 {alpha}Kdo(2->8){alpha}Kdo(2->4){alpha}Kdo trisaccharide which represents an epitope shared by all species of the family. MAb S45-18 bound to an epitope of the structure {alpha}Kdo(2->4){alpha}Kdo(2->4){alpha}Kdo, 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.


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