Developed a New Way to Block Cancer Immunosuppression
In a new study, Belgian researchers have elucidated the three-dimensional structure of a protein complex on the surface of cells that inhibits immune responses. They also discovered how antibodies can block this protein complex and its downstream induced immunosuppression. Such antibodies may be used to activate an immune response against tumor cells in cancer patients, triggering them to destroy the tumor. Related research results on October 25, 2018, published online in the journal Science, the paper entitled "Structural basis of latent TGF - beta 1 presentation and activation by GARP on human regulatory T cells".
Immunosuppression through a series of interactions
Regulatory T cells are immunosuppressive cells that, under normal conditions, resist excessive immune responses in the body to prevent autoimmune diseases. But in cancer patients, they play a detrimental role by inhibiting the immune response against tumor cells. Treg cells do their job by producing a messenger protein called TGF- beta. The messenger protein sends inhibitory signals to nearby immune cells, especially those that should destroy tumors in cancer patients.
Elucidating molecular mechanisms
To solve these problems, several teams worked together to resolve the three-dimensional structure of a protein complex assembled by GARP and TGF- beta.
The researchers used X-ray crystallography. The method has been used to study molecular structures for more than a century, and scientists are still refining it to study biomolecules at atomic resolution.
Immunosuppression through a series of interactions
Regulatory T cells are immunosuppressive cells that, under normal conditions, resist excessive immune responses in the body to prevent autoimmune diseases. But in cancer patients, they play a detrimental role by inhibiting the immune response against tumor cells. Treg cells do their job by producing a messenger protein called TGF- beta. The messenger protein sends inhibitory signals to nearby immune cells, especially those that should destroy tumors in cancer patients.
Elucidating molecular mechanisms
To solve these problems, several teams worked together to resolve the three-dimensional structure of a protein complex assembled by GARP and TGF- beta.
The researchers used X-ray crystallography. The method has been used to study molecular structures for more than a century, and scientists are still refining it to study biomolecules at atomic resolution.
