- Mucus coats the internal surfaces of the body, where it serves as a barrier against pathogens and a food source for friendly bacteria. Mucus is produced by the body’s immune system.
- One of its most important parts are mucins, which are proteins that are studded with sugar molecules in a variety of patterns, which govern how the mucus interacts with both beneficial and pathogenic microbes, respectively.
- Currently, scientists are working on developing a cell-based platform for customising the production of mucins with unique qualities to meet specific needs.
- It is possible that mucin-based therapies for viral and bacterial infections will be developed using this platform.
When it comes to the body-to-environment interface, mucus is a sticky substance that serves a variety of critical roles in the body and outside world.
It coats the cells that border the lungs, intestines, and genital tract, where it acts as a barrier against unpleasant chemicals as well as a lubricant for the organs in these areas.
Mucus has a similar role in the gut as it does on the other body surfaces, keeping pathogens out while allowing beneficial microbes in.
Mucins are the primary ingredients of mucus, and they are proteins that have been decorated with different patterns of sugar molecules.
These not only serve as a food supply for bacteria, but they can also act as anchors to keep them in place when they bind to adhesins, which are molecules found in bacterial cell walls that act as anchors to hold bacteria in place.
Mucins produced into bodily fluids such as saliva and tears have the ability to attach to the adhesins of pathogens, preventing them from clumping together and spreading. Mucins are also capable of dissolving the infections’ “biofilms.”
Essentially, a biofilm is an aggregation of bacteria that has collaborated to build thin coatings on the surfaces of teeth and other tissues. Biofilms can have a harmful impact on one’s health in some circumstances.
Because of this, sugar molecule patterns on mucins are critical in defining how the body interacts with bacteria and how they are eliminated.
Mucins, on the other hand, are difficult to separate and investigate, which has resulted in a limited understanding of how they function.
An international team of researchers has now discovered a method for producing human mucins that include specific patterns of sugar molecules.
Research led by scientists at the Copenhagen Center for Glycomics has now demonstrated that they can genetically control laboratory cultures of human embryonic kidney cells to make mucins that bind to specific bacterial adhesion molecules.
Their research was published in the journal Nature Communications.
Mucins on prescription
It is possible, according to the scientists, that doctors will be able to prescribe mucins that either encourage the growth of helpful species or prevent the growth of disease-causing species in the future.
We currently know relatively little about how to control the intestinal flora in the treatment of diseases, despite the fact that an unbelievable number of diseases are linked to intestinal flora.” Synthetic mucins have the potential to offer up new therapy options in this situation,” says Yoshiki Narimatsu, an associate professor of glycobiology at the University of Copenhagen and one of the study’s lead authors, in a statement.
“In the long run, it is possible to envision employing mucins as a prebiotic material, that is, as chemicals that aid the growth of beneficial bacteria in the body,” he says.
Artificial mucins, according to the researchers, might potentially be employed in place of antibiotics to treat bacterial infections in the future.
Using synthetic versions of the mucins found in saliva and tears, for example, doctors may flush away bacteria that would otherwise build toxic biofilms and cause infection.
For example, Dr. Narimatsu suggests that instead of using antibiotics, you may create eye drops that contain the mucin that is generally used to eliminate bacteria from infections, such as those caused by bacterial infections in the eyes.
Competition for the flu virus
Mucins could even be used to compete with the common flu virus and prevent it from entering the cells that lining the nose, windpipe, and lungs, according to some researchers.
In order to infect cells in the respiratory tract, the virus attaches itself to sugar molecules known as sialic acids found in the cell membranes of the infected cells.
However, in order for the virus to release newly produced viral particles and hence perpetuate the infection, it must use an enzyme to remove its connection to the sialic acids.
Prof. Henrik Clausen, one of the study’s co-lead authors, told Medical News Today that mucins contain large amounts of sialic acids.
Besides binding to free virus particles and preventing them from attaching themselves to host cells in the nose, lungs or on both sides of the body, these acids also compete with one another for the utilisation of the enzyme that releases new viral particles.
According to Prof. Clausen, “In this paper, we solely investigate the effect on [the] release of the virus, and we discover that particular mucins containing sialic acids inhibit [the] release of the influenza virus and, as a result, its ability to proliferate and disseminate the infection.”
