Open AccessStructure, serological specificity, and synthesis of artificial glycoconjugates representing the genus-specific lipopolysaccharide epitope of Chlamydia spp
Author(s) -
Otto Holst,
Lore Brade,
Paul Kosma,
Helmut Brade
Publication year - 1991
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.173.6.1862-1866.1991
Subject(s) - epitope , biology , glycoconjugate , antigen , alpha (finance) , lipopolysaccharide , monoclonal antibody , biochemistry , microbiology and biotechnology , antibody , immunology , medicine , construct validity , nursing , patient satisfaction
The human bacterial pathogens Chlamydia spp. possess a genus-specific lipopolysaccharide as a major surface antigen, the structure of which has been determined by analytical chemistry as Kdop alpha 2-8-Kdop alpha 2-4-Kdop alpha 2-6GlcNp beta 1-6-GlcNol (Kdo, 3-deoxy-D-manno-2-octulosonic acid). Immunochemical studies on this pentasaccharide and the chemically synthesized partial structures Kdop alpha 2-8-Kdop alpha 2-4-Kdop alpha 2-6GlcNp beta, Kdop alpha 2-8-Kdop alpha 2-4-Kdop alpha, Kdop alpha 2-4-Kdop alpha, Kdop alpha 2-8-Kdop alpha, and Kdop alpha using artificial glycoconjugate antigens and monoclonal antibodies showed that fatty acids and phosphoryl groups (as present in native lipopolysaccharide) are dispensable for constitution of the genus-specific epitope and that the minimal structure to exhibit chlamydia specificity is the Kdo trisaccharide moiety.