Recent studies have revealed the central role of bacterial adhesion factors during bacterial infection, especially FimH in E. coli. These bacterial adhesion factors do more than just attach themselves to bacteria; they also play an important role in manipulating our immune system. This article will deeply explore the structure, function and potential of FimH in the development of anti-infectious vaccines.
Bacterial adhesion factors are bacterial surface components that help them attach to host cells or surfaces. These factors are important factors in the pathogenic ability of bacteria. In bacterial etiology, adhesion is an essential step in infecting a new host. Bacteria often face frequent shear forces during their life cycle, and adhesion factors act as anchors to help stabilize bacteria in ideal environments, such as plant roots or mammal tear duct tissue.
FimH is one of the most representative bacterial adhesion factors, which is responsible for "D-mannose-sensitive" attachment. Simply put, FimH is a protein composed of 279 amino acids, which is displayed on the surface of bacteria and becomes part of the first type of bacterial filament organization. According to research in 1999, the structure of FimH was analyzed through X-ray crystallography and found to consist of two main regions. The N-terminal adhesion region is responsible for surface recognition, while the C-terminal is responsible for integration with bacterial filaments.
Most bacterial pathogens utilize specific adhesion as their main virulence factor. Many studies have shown that inhibiting the expression of a single adhesion factor is enough to make pathogenic bacteria lose their pathogenicity.
Research shows that adhesion factors have great potential in vaccine development, especially anti-adhesion vaccines for urinary tract infections. Because these factors play an important role in bacterial infection, their surface location makes them accessible targets for antibodies. Studies targeting the FimH adhesion factor of uropathogenic Escherichia coli (UPEC) have shown that anti-adhesion antibodies can significantly reduce bacterial colonization in animal models.
Dr family adhesion factors bind to the Dr blood antigen of the Deceleration accelerating factor (DAF) component to mediate the attachment of uropathogenic Escherichia coli in the urethra. This adhesion factor not only induces cells to expand to encapsulate bacteria, but also initiates multiple signaling cascades.
Multivalent adhesion molecule is an adhesion factor widely present in Gram-negative bacteria, including Escherichia coli. Studies have shown that blockers targeting these adhesion factors can significantly reduce the colonization of multidrug-resistant bacteria, providing new ideas for clinical treatment.
Neisseria is almost exclusive to humans, and relevant studies have shown that its type 4 bacterial filament adhesion factor is an important factor in its pathogenicity. By manipulating the behavior of white blood cells, Neisseria is able to remain invisible under the protection of the immune system.
For pathogenic E. coli, such as the strains that cause diarrhea, they use K88 and CFA1 to attach to the intestine. UPEC causes up to 90% of urinary tract infections, and 95% of Wilcox strains express type I bacterial filaments. The FimH of these bacteria can effectively switch their adhesion state to avoid antibody immune responses. Researchers hope to use this understanding to develop vaccines targeting specific adhesion factors as a reference against viruses.
With the deepening of research, the understanding of bacterial adhesion factors has become more thorough. Can effective vaccines be developed in the future to prevent the attachment and infection of pathogenic bacteria?