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Do, Yoonkyung
DC-based Immune System & Immunotherapy (DISNI) Lab
Research Interests
  • Study on various subsets of dendritic cells and their immunological functions
  • Vaccine development by targeting pathogenic antigens to distinct DC subsets via anti-DC-subset-specific-receptor monoclonal antibodies
  • Characterization of roles of DCs in tumor microenvironment and tumor metastasis
  • Studies on role of DCs in neuro-related diseases
  • Study DCs in collaboration with Biotechnology or Engineering field

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A dominant complement fixation pathway for pneumococcal polysaccharides initiated by SIGN-R1 interacting with C1q

Cited 108 times inthomson ciCited 102 times inthomson ci
Title
A dominant complement fixation pathway for pneumococcal polysaccharides initiated by SIGN-R1 interacting with C1q
Author
Kang, YSDo, YoonkyungLee, HKPark, SHCheong, CLynch, RMLoeffler, JMSteinman, RMPark, CG
Issue Date
2006-04
Publisher
CELL PRESS
Citation
CELL, v.125, no.1, pp.47 - 58
Abstract
The intricate system of serum complement proteins provides resistance to infection. A pivotal step in the complement pathway is the assembly of a C3 convertase, which digests the C3 complement component to form microbial binding C3 fragments recognized by leukocytes. The spleen and C3 provide resistance against blood-borne S. pneumoniae infection. To better understand the mechanisms involved, we studied SIGN-R1, a lectin that captures microbial polysaccharides in spleen. Surprisingly, conditional SIGN-R1 knockout mice developed deficits in C3 catabolism when given S. pneumoniae or its capsular polysaccharide intravenously. There were marked reductions in proteolysis of serum C3, deposition of C3 on organisms within SIGN-R1+ spleen macrophages, and formation of C3 ligands. We found that SIGN-R1 directly bound the complement C1 subcomponent, C1q, and assembled a C3 convertase, but without the traditional requirement for either antibody or factor B. The transmembrane lectin SIGN-R1 therefore contributes to innate resistance by an unusual C3 activation pathway.
URI
https://scholarworks.unist.ac.kr/handle/201301/7058
URL
https://www.sciencedirect.com/science/article/pii/S0092867406003084?via%3Dihub
DOI
10.1016/j.cell.2006.01.046
ISSN
0092-8674
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BME_Journal Papers
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