Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical use

Tu, I-FanI-FanTuLin, Tzu-LungTzu-LungLinYang, Feng-LingFeng-LingYangLee, I-MingI-MingLeeTu, Wei-LinWei-LinTuLiao, Jiahn-HaurJiahn-HaurLiaoKo, Tzu-PingTzu-PingKoWu, Wen-JinWen-JinWuJan, Jia-TsrongJia-TsrongJanHo, Meng-RuMeng-RuHoChou, Ching-YiChing-YiChouWang, Andrew H-JAndrew H-JWangWu, Chung-YiChung-YiWuJIN-TOWN WANGHuang, Kai-FaKai-FaHuangWu, Shih-HsiungShih-HsiungWu2023-12-202023-12-202022-02-0710217770https://scholars.lib.ntu.edu.tw/handle/123456789/638011K1 capsular polysaccharide (CPS)-associated Klebsiella pneumoniae is the primary cause of pyogenic liver abscesses (PLA) in Asia. Patients with PLA often have serious complications, ultimately leading to a mortality of ~ 5%. This K1 CPS has been reported as a promising target for development of glycoconjugate vaccines against K. pneumoniae infection. The pyruvylation and O-acetylation modifications on the K1 CPS are essential to the immune response induced by the CPS. To date, however, obtaining the fragments of K1 CPS that contain the pyruvylation and O-acetylation for generating glycoconjugate vaccines still remains a challenge.enAcetylation; K1 capsular polysaccharide; Klebsiella pnuemoniae; Polysaccharide lyase; Pyruvylation; Tailspike protein; β-Helix[SDGs]SDG3Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical usejournal article10.1186/s12929-022-00792-4351308762-s2.0-85124442686https://api.elsevier.com/content/abstract/scopus_id/85124442686