Hokkaido University · 의학
Katsumi Maenaka 교수의 연구실은 면역학적 상호작용의 분자 기반을 해독하는 데 초점을 맞추고 있습니다. 주로 MHC 분자, Fc 수용체, 항체-항원 상호작용의 고해상도 구조와 결합 메커니즘을 구조생물학적·생화학적 접근으로 연구합니다. 특히 항체의 보편적 중화 기전, 면역세포 수용체의 결합 특성, 그리고 바이러스 표면 단백질과의 상호작용에서의 구조 기반 기전을 규명하고자 합니다. 이는 새로운 면역치료제 개발과 감염병 예방 전략 수립에 기여합니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
HLA-G is a nonclassical major histocompatibility complex class I (MHCI) molecule, which is expressed in trophoblasts and confers immunological tolerance in the maternal-fetal interface by binding to leukocyte Ig-like receptors (LILRs, also called as LIR/ILT/CD85) and CD8. HLA-G is expressed in disulfide-linked dimer form both in solution and at the cell surface. Interestingly, MHCI dimer formations have been involved in pathogenesis and T cell activation. The structure and receptor binding chara
Fcgamma receptors (FcgammaRs) are expressed on all immunologically active cells. They bind the Fc portion of IgG, thereby triggering a range of immunological functions. We have used surface plasmon resonance to analyze the kinetic and thermodynamic properties of the interactions between the ectodomains of human low affinity FcgammaRs (FcgammaRIIa, FcgammaRIIb, and FcgammaRIIIb-NA2) and IgG1 or the Fc fragment of IgG1. All three receptors bind Fc or IgG with similarly low affinities (K(D) approxi
Potent neutralizing SARS-CoV-2 antibodies often target the spike protein receptor-binding site (RBS), but the variability of RBS epitopes hampers broad neutralization of multiple sarbecoviruses and drifted viruses. Here, using humanized mice, we identified an RBS antibody with a germline V<sub>H</sub> gene that potently neutralized SARS-related coronaviruses, including SARS-CoV and SARS-CoV-2 variants. X-ray crystallography revealed coordinated recognition by the heavy chain of non-RBS conserved
The crystal structures of the human MHC class I allele HLA-B*5101 in complex with 8-mer, TAFTIPSI, and 9-mer, LPPVVAKEI, immunodominant peptide epitopes from HIV-1 have been determined by x-ray crystallography. In both complexes, the hydrogen-bonding network in the N-terminal anchor (P1) pocket is rearranged as a result of the replacement of the standard tyrosine with histidine at position 171. This results in a nonstandard positioning of the peptide N terminus, which is recognized by B*5101-res
In order to elucidate the role of the aromatic ring in recognition of the sugar ring, Trp-62 of hen egg white lysozyme, which is proposed on the basis of x-ray crystallography data to make contact with a sugar ring through van der Waals interaction, was replaced with aliphatic amino acids (Leu, Ile, Val, and Ala) and Gly by site-directed mutagenesis. In spite of the loss of the aromatic effect, these mutant lysozymes, except for the Trp-62-->Gly mutant, showed higher bacteriolytic activity than
