| Literature DB >> 33667709 |
Naijing Hu1, Chunxia Qiao2, Jing Wang3, Zhihong Wang4, Xinying Li5, Liuzhong Zhou6, Jiaguo Wu7, Dingmu Zhang8, Jiannan Feng9, Beifen Shen10, Jinghai Zhang11, Longlong Luo12.
Abstract
Staphylococcal enterotoxin B (SEB), one of the exotoxins produced by Staphylococcus aureus, is the key toxin that causes poisoning reactions and toxic shock syndrome. In the current research work, a novel human antibody named LXY8 was screened from a human phage display antibody library, and LXY8 blocked the interaction between SEB and the T cell receptor (TCR). The binding activity between LXY8 and SEB was 0.525 nM. Furthermore, LXY8 could effectively inhibit the SEB-induced activation of peripheral blood mononuclear cells and release of cytokines. In the BALB/c mouse model, LXY8 effectively neutralized SEB toxicity in vivo. Finally, based on computer-guided molecular modeling, we designed a series of SEB mutation sites; these sites facilitated the determination of the key residues (i.e.176EFNN179) of SEB recognized by LXY8. The research revealed that the 176EFNN179 residues of SEB are important for specific antibody-antigen recognition. The results may be helpful for the development of antibody-based therapy for SEB-induced toxic shock syndrome.Entities:
Keywords: Neutralizing antibody; Staphylococcal enterotoxin B; Treatment
Year: 2021 PMID: 33667709 DOI: 10.1016/j.bbrc.2021.02.057
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575