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Updated: Feb 3, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
Published on: November 25, 2017
Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors
David Aparicio1, Sergi Torres-Puig2, Mercè Ratera1
1Instituto de Biología Molecular de Barcelona (IBMB-CSIC) and Maria de Maeztu Unit of Excellence, Parc Científic de Barcelona, Baldiri Reixac 10, 08028, Barcelona, Spain.
Abstract:
Adhesion of pathogenic bacteria to target cells is a prerequisite for colonization and further infection. The main adhesins of the emerging sexually transmitted pathogen Mycoplasma genitalium, P140 and P110, interact to form a Nap complex anchored to the cell membrane. Herein, we present the crystal structures of the extracellular region of the virulence factor P110 (916 residues) unliganded and in complex with sialic acid oligosaccharides. P110 interacts only with the neuraminic acid moiety of the oligosaccharides and experiments with human cells demonstrate that these interactions are essential for mycoplasma cytadherence. Additionally, structural information provides a deep insight of the P110 antigenic regions undergoing programmed variation to evade the host immune response. These results enlighten the interplay of M. genitalium with human target cells, offering new strategies to control mycoplasma infections.
Insights
Mycoplasma genitalium uses its P110 adhesin to bind sialic acid on human cells, enabling infection. Understanding this interaction offers new strategies to combat this sexually transmitted pathogen.
Area of Science:
- Microbiology
- Structural Biology
- Pathogen-Host Interactions
Background:
- Adhesion to host cells is crucial for pathogenic bacteria, including Mycoplasma genitalium.
- The P140 and P110 proteins form a complex essential for Mycoplasma genitalium adhesion.
Purpose of the Study:
- To determine the crystal structures of the Mycoplasma genitalium P110 adhesin.
- To investigate the interaction between P110 and sialic acid oligosaccharides.
- To elucidate the role of P110-sialic acid interactions in mycoplasma cytadherence and immune evasion.
Main Methods:
- X-ray crystallography was used to obtain the structures of P110.
- Biochemical assays were performed to study the binding of P110 to sialic acid.
- Experiments with human cells were conducted to assess the role of P110 in cytadherence.
Main Results:
- The crystal structures of unliganded P110 and P110 complexed with sialic acid oligosaccharides were determined.
- P110 specifically binds to the neuraminic acid component of sialic acid oligosaccharides.
- These interactions are essential for Mycoplasma genitalium's ability to adhere to human cells.
- Structural insights into P110's variable antigenic regions suggest mechanisms for immune evasion.
Conclusions:
- The P110 adhesin plays a critical role in Mycoplasma genitalium's attachment to host cells via sialic acid binding.
- Understanding these molecular interactions provides a basis for developing novel therapeutic strategies against Mycoplasma genitalium infections.
- The study highlights P110's role in both cytadherence and immune evasion, crucial aspects of this emerging pathogen.
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