Sunday, October 20, 2019

Study discovers enzyme that may prevent streptococci infection

Researchers have found an enzyme that could prevent a deadly streptococci infection that causes around 500,000 deaths worldwide each year.

Group A streptococcus can lead to illnesses such a s strep throat, scarlet fever, sepsis, and toxic shock syndrome as well as several long-term autoimmune diseases with high mortality rates.


Working with colleagues, the researchers found an enzyme that is required to produce a carbohydrate on the surface of the streptococcal bacterium which enables it to infect humans and animals.


Their research reveals new opportunities to inhibit this enzyme and ultimately, fight Group A Streptococcus infections.


The fact this enzyme works through a novel mechanism of action that can also be found in other streptococcal species increases the impact and relevance of this finding.


Strep throat is the most common Group A Streptococcus infection and can often be fought by the body's immune system. Unfortunately, the very same bacterium also causes a plethora of severe and potentially fatal illnesses, such as sepsis and toxic shock syndrome, said one of the researcher.


We knew that the carbohydrate coating was an essential component of Group A Strep, but we wanted to find out more about how this worked. What we've shown is that the enzyme initiates the synthesis of the bacterial coating, continued the Dr.


Surprisingly, we also found that this enzyme fulfills the same function in many other types of streptococci. This includes Group B Streptococci, that can cause severe infections in newborns, and Group C and G Streptococci that cause similar disease as Group A, including bacteraemia and endocarditis, in humans and animals, added the Dr.

The newly discovered enzyme is not present in humans or animals, therefore providing a novel,opportunity for drug discovery programmes, reported the study published recently.

Antimicrobial resistance is a global problem and existing antibiotics fail to work in around 20 % of cases of strep throat. The long term aim of the Dundee team is to aid the development of a new class of antimicrobial drugs that could completely inhibit or reduce the enzyme's activity.


The next step towards this goal will see them work with others to develop compounds that could target this enzyme.


The research was jointly led by PhD student and another researcher explained, in our study, we show how this protein initiates the production of this carbohydrate through a mechanism never described before.


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Wednesday, July 17, 2019

IIT-Kharagpur Trio Used Curd To Make Low-Cost Gel That Enhances Wound Healing!

Usually small cuts, bruises or wounds are harmless as the body has a system for repairing them. Often, antibiotic ointment is applied over them to prevent the growth of infection-causing microbes and to promote speedy healing. However, with the increasing presence of antibiotic-resistant bacteria in the environment, there is a danger that the ointments might not be able to stop the infections and a minor bruise could turn out to be a major health issue.

To address this concern, a team of scientists from IIT-Kharagpur has synthesized a low-cost gel from curd which not only retards the growth of antibiotic-resistant bacteria but also enhances wound healing.

“From ancient times, curd has been used for skin and hair care. Drainage water from curd, which is usually discarded, contains a good amount of bioactive peptides which we have utilized for this therapeutic application,” says one of the researchers.

For their study, scientists made curd by inoculating three strains of bacteria – Streptococcus thermophilus, Lactobacillus casei, and Bifidobacterium bifidum, which they obtained from National Collection of Dairy Cultures. They then collected the drainage water from the curd and purified it for bioactive peptides. They added ten micrograms of the peptide to 0.1% trifluoroacetic acid and zinc nitrate to form a hydrogel. Scientists tested the efficacy of the hydrogel against two antibiotic-resistant strains. One of Staphylococcus aureus and another of Pseudomonas aeruginosa. The hydrogel killed both the strains. Pseudomonas, however, required a higher dose of hydrogel/peptide than Staphylococcus.

Often, a group of bacteria reside in a colony by synthesizing mucilage around them called bio-film. These bio-films protect the bacteria from antibiotics. Biofilm formation is dependent on the ability of bacteria to move. Scientists found that hydrogel retarded movement of the bacteria and thus prevented bio-film formation.

To evaluate the wound healing activity of hydrogel, scientist used laboratory-grown skin cell lines. Scientists scratched the surface containing the skin cells and applied hydrogel over there. After 24 hours, cells were observed at the scratched surface. This confirmed that hydrogel can enhance the proliferation capacity of damaged cells and therefore has property of wound healing also.

“The cost of the hydrogel is very low and it is easy to prepare without the need of any harsh chemicals. It, therefore, has the potential to be used for therapeutic application in wound healing. We intend to test this hydrogel on small animals,” added the Dr.

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