Life Science Seminar

 

▶ Subject : Recognition mechanism and functions of bacterial pattern molecules by host defense proteins

▶ Speaker:  Prof. Lee Bok Luel (College of Pharmacy, Pusan National University)

▶ Date :  4:00PM/ Jun. 8(Fri)/2012

▶ Place :  Auditorium(1F), Postech Biotech Center

 

*Abstract
Wall teichoic acid (WTA) of Staphylococcus aureus is a major cell envelope-associated glycopolymer that is a key molecule in promoting colonization during S. aureus infection. The complement system plays a key role in the opsonization and clearance of pathogens. We recently reported that S. aureus WTA functions as a ligand of human serum mannose-binding lectin (MBL), a recognition molecule of the lectin complement pathway. Intriguingly, serum MBL in adults does not bind to WTA because of an inhibitory effect of serum anti-WTA-immunoglobulin (IgG). Here, to examine the biological function of human anti-WTA-IgG, serum anti-WTA-IgG was purified to homogeneity using a purified S. aureus WTA-coupled affinity column. The purified anti-WTA-IgG contained the IgG2 subclass as a major component and specifically induced C4 and C3 deposition on the S. aureus surface in the anti-WTA-IgG-depleted serum, but not in C1q-deficient serum. Furthermore, the anti-WTA-IgG-dependent C3 deposition induced phagocytosis of S. aureus cells by human polymorphonuclear leukocytes. These results demonstrate that serum anti-WTA-IgG is a real trigger for the induction of classical complement-dependent opsonophagocytosis against S. aureus. Our results also support the fact that a lack of the lectin complement pathway in MBL-deficient adults is compensated by antigen-specific antibody-mediated adaptive immunity.

 

☎ Inquiry : Prof. Kim You-Me(279-0689)

 

*This Seminar will be given in English