The body protein plays a vital role in our immune system and helps our body to resist infection. However, the precise way of interaction between these proteins and specific cell receptors has been the theme of scientific conspiracy for a long time. The new study clarifies how the body protein is combined with CR2, which is likely to pave the way for the improvement of immune -related diseases.
Recent research clarifies the fascinating insights on interaction between body protein and interaction with CR2. The study was studied by the IStituto Tecnologie Biomethe’s Giuseppe Barile of the Italian CNR, exploring the complex biochemical mechanism to control these interactions. This work was published in the “Biochemical and Biophysics Report” magazine.
Type 2 (CR2), also known as CD21, is a vital cross -membrane glycoprotein that is mainly expressed on B cells. CR2 acts as the receptor of C3D, C3D is a fragment of the body component C3, which plays an important role in the immune response. The study emphasized that RAJI cells (a CR2-positive cell line) can combine the endogenous and exogenous forms of I-C3, thereby forming an heterododerous cluster that links through the sulfur key. These findings have a profound impact on understanding immune cell activation and pathogen interaction.
Giuseppe Barile explained: “Our research shows that the fixed mechanism of I-C3 on CR2 involves a complex mechanism, which is affected by the hydrophobic performance of specific Fang residues in the I-C3 C3C structure.”
Barile uses a series of research and immunohic tract technologies to discover how specific monoclonal antibodies (such as OKB7 and HB5) existence significantly affects different cutting mechanisms.
The study found that Raj cells not only combine the exogenous I-C3, but also synthesize the protein similar to C3 internally, and Barile is called E-C3. This protein has a characteristic similar to the I-C3, which is essential to the immune function of the cells, and participates in the formation of a complex structure of CR2, which may work in the self-secretion signal transmission.
Interestingly, the study also emphasizes the role of low molecules in these interactions. “These molecules seem to strongly combine the immune complex unit through THIOESTER, thereby giving the CR2-C3 complex a significant stability.” “It is likely to pass the immunohic complex through multiple binding sites (at least three) through a specific ABS. (Or ABS matched) It may suffer a crack in its structure, so that H2O enters the hydrolyzed sulfur. As a result, the surface tumor antigen is no longer covered, so the immune system recognition that can physical kill tumor cells can be physical. Therefore, a similar mechanism should constitute the basis for the successful treatment of immunotherapy in certain tumors. “
Barile pointed out: “Our discovery shows that the hydrophobicity of certain residues in C3C is necessary for fixing the i-C3 to CR2.” “” “
The meaning of these findings is important. By understanding the molecular details of how CR2 interacts with body protein, researchers can better understand the potential mechanism of immune cell activation and regulation. This knowledge is essential for the development of targeted therapy for autoimmune diseases and improves immune response to infection.
Barile uses advanced technology, such as SDS-PAGE and immunization to visualize the interaction between CR2 and C3 fragments. His detailed methods enable him to identify a specific protein belt corresponding to these interactions, which further clarifies the structure of the CR2-C3 complex.
All in all, the study of Giuseppe Barile provides important insights for the biochemical interaction between CR2 and body protein. His work emphasizes the importance of specific molecular characteristics in these interactions, and has opened up new ways for the treatment intervention of immune -related diseases.
Journal reference
Barile, G. (2024). “The fixation of the body of the body of the CR2 is fixed.” Report on biochemistry and biophysics, 38,101657. Doi: https: //doi.org/10.1016/j.bbrep.2024.101657
About the author
Giuseppe Barile He was born on August 23, 1946 in Cercemaggiore, Meris, Italy, and graduated from biological science in 1971. In 1973, he was a recipient of the CNR scholarship. He studied the study of estrogen and progesterone receptors, and later expanded his focus to virus and immunology in 1982. Visiting researcher at the ICRF Hormon Biochemistry Laboratory, Dr. JRB King Director London and Dr. Gunnarähnstrom, Director of the Department of Radiology of the University of Stockholm. He received a scholarship from Airc (September 1983 /Ag.84). He took a vacation and was guided by Dr. J. Meneze to explore the immunology of S. Justine S. Justine S. Justine of Montreal, Canada. Tie. He contributed 37 works published in scientific journals with other researchers. In 2009, he retired as Digigente Di Ricerca on CNR’s ITBM and ended his outstanding occupation.
