Nontypeable Haemophilus influenzae-binding gangliosides of human respiratory (HEp-2) cells have a requisite lacto/neolacto core structure.
Nontypeable Haemophilus influenzae-binding gangliosides of human respiratory (HEp-2) cells have a requisite lacto/neolacto core structure.
复制标题
人类呼吸道 (HEp-2) 细胞的不可分型流感嗜血杆菌结合神经节苷脂具有必需的乳/新乳核心结构。
DOI：
10.1016/j.femsim.2005.03.007
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发表时间：
2005
影响因子：
--
通讯作者：
Yohe,HerbertC
中科院分区：
文献类型：
--
作者：
Berenson,CharlesS;Sayles,KellyB;Huang,Jing;Reinhold,VernonN;Garlipp,MaryAlice;Yohe,HerbertC
NontypeableHaemophilus influenzae(NTHI) are a major cause of human infections. We previously demonstrated high affinity and high specificity binding of NTHI to minor gangliosides of human respiratory (HEp-2) cells and macrophages, but not to brain gangliosides. We further identified the NTHI-binding ganglioside of human macrophages as α2,3-sialylosylparagloboside (IV3NeuAc-nLcOse4Cer, nLM1), which possesses a neolacto core structure that is absent in brain gangliosides. This supported a hypothesis that lacto/neolacto core carbohydrates are critical for NTHI-ganglioside binding. To investigate, we determined the core carbohydrate structure of NTHI-binding gangliosides of HEp-2 cells, through multiple approaches, including specific enzymatic degradation, mass spectral analysis and gas–liquid chromatography. Our analyses denote the following critical structural attributes of NTHI-binding gangliosides: (1) a conserved lacto/neolacto core structure; (2) requisite sialylation, which may be either internal or external, with α2,3 (human macrophages) or α2,6 (HEp-2 cells) anomeric linkages; (3) internalized galactose residues. Mass spectral and gas chromatographic analyses confirm that NTHI-binding gangliosides of HEp-2 cells possess lacto/neolacto carbohydrate cores and identify the structure of the major peak as NeuAcα2–6Galβ1–4GlcNAcβ1–3Galβ1–4Glcβ1–1Cer (α2,6-sialosylparagloboside, nLM1). Collectively, our studies denote NTHI-binding gangliosides as lacto/neolacto series structures.
