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Updated: Aug 19, 2026

Forward Genetic Approaches in Chlamydia trachomatis
Published on: October 23, 2013
Polymorphic outer-membrane proteins of Chlamydophila abortus are glycosylated
E Vretou1, P Giannikopoulou, E Psarrou
1Department of Microbiology, Hellenic Pasteur Institute, Vassilissis Sofias 127, Athens 11521, Greece. vretou@mail.pasteur.gr
Abstract:
Antigenic profiles of mono-, bi- and poly-specific monoclonal antibodies against 90 kDa polymorphic outer-membrane proteins (POMPs) and a 105 kDa POMP-related protein of Chlamydophila abortus ATCC VR 656(T), after one- and two-dimensional electrophoretic analysis, helped identify each one of the triplets POMP 90, 91A and 91B, and a POMP-related protein at 85 kDa. The lectin concanavalin A bound to the four POMPs and the POMP-related protein in a specific manner and the binding was sensitive to treatment with the amidase N-endoglycosidase F, suggesting the presence of small asparagine-linked oligosaccharide chains. The exposure of the five proteins on the chlamydial surface and the orientation of the attached oligosaccharide chains was examined by protease and endoglycosidase treatments of intact bacteria. The results were consistent with the concept that some of the oligosaccharides in the POMPs face outwards, possibly protecting the polypeptides from proteolytic enzymes, whereas the oligosaccharides in the 105 kDa POMP-related protein are oriented inwards, thereby rendering the polypeptide chain accessible to proteases. A possible role for the N-linked oligosaccharides in the POMPs might be the promotion of the proper folding and processing of these proteins.
Insights
Monoclonal antibodies identified polymorphic outer-membrane proteins (POMPs) and related proteins in Chlamydophila abortus. N-linked oligosaccharides on POMPs face outward, potentially aiding protein folding and protection.
Area of Science:
- Microbiology
- Protein Chemistry
- Glycobiology
Background:
- Chlamydophila abortus possesses polymorphic outer-membrane proteins (POMPs) and related proteins crucial for its structure and function.
- Understanding the antigenic profiles and glycosylation of these proteins is essential for characterizing Chlamydophila abortus.
Purpose of the Study:
- To characterize the antigenic profiles of Chlamydophila abortus POMPs and a related protein using monoclonal antibodies.
- To investigate the presence and orientation of N-linked oligosaccharide chains on these proteins and their potential roles.
Main Methods:
- Electrophoretic analysis (one- and two-dimensional) to identify protein components.
- Monoclonal antibody binding assays to determine antigenic profiles.
- Lectin binding (concanavalin A) and enzymatic treatments (N-endoglycosidase F, proteases) to analyze oligosaccharide presence and orientation.
Main Results:
- Identification of specific POMP triplets (90, 91A, 91B) and a POMP-related protein (85 kDa).
- Concanavalin A specifically bound to these proteins, sensitive to N-endoglycosidase F, indicating N-linked oligosaccharides.
- Protease and endoglycosidase treatments revealed outward-facing oligosaccharides on POMPs and inward-facing ones on the related protein.
Conclusions:
- Chlamydophila abortus POMPs and a related protein possess N-linked oligosaccharides.
- The orientation of these oligosaccharides differs, with POMP oligosaccharides potentially protecting the protein and facilitating folding, while the related protein's oligosaccharides are internally oriented.
- These findings contribute to understanding the surface structure and potential virulence factors of Chlamydophila abortus.
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