Phage Lytic Enzyme Specifically Attacks MRSA

Due to the highly specific action, the natural microflora is maintained, and HY-133 could therefore be used for the prophylactic treatment of nasal colonization, counteracting the spread of MRSA and thus preventing infections.

HY-133 was developed using proprietary phage-ligand technology, which exploit the principles of bacteriophage biology for diagnostic, antimicrobial, and research applications. The technology enables the production of advanced molecules for effective binding of bacteria, bacterial components, and lysis. Other applications of the molecules developed using the technology include food preservation, and decolonization of acne Propionibacterium germs and other bacterium, such as Clostridium difficile. HY 133 was presented at the BIO World Congress on Industrial Biotechnology, held during June 2015 in Montreal (Canada).

“We do like to describe it as a MRSA-killing protein, even if it sounds somewhat sensational,” said Wolfgang Mutter, PhD, MBA, of Hyglos. “In fact, all Staphylococcus aureus cells, whether resistant or not resistant, will be killed by this new active substance within a very short time. And this without the natural microflora in the nose being destroyed, nor does resistance develop.”

“A rapid detection and effective elimination of MRSA colonization in the nose prior to a hospital stay is a crucial step in combating these hospital germs,” added Prof. Karsten Becker, MD, of University Hospital Münster (Germany), a researcher at the DZIF. “The bacteria in the nose are increasingly resistant to the currently used antibiotic mupirocin and the duration of the decolonization and follow-up control is around one week. Under such circumstances, no effective MRSA prevention is possible for patients immediately in need of surgery.”

Bacteriophages recognize their host via proteins that bind to carbohydrate or protein structures on the surface of the bacteria. These phage proteins are very stable; some of them require heating at temperatures above 90 °C to destroy their three-dimensional structure. Phage proteins also have binding affinities comparable to monoclonal antibodies. Both properties provide durability in harsh environmental conditions, and allow bacteriophages to wait for the next opportunity to infect new host bacteria.

Related Links:
German Center for Infection Research
Hyglos