Identification and structural determination of the capsular polysaccharides from two Acinetobacter baumannii clinical isolates, MG1 and SMAL
Identification and structural determination of the capsular polysaccharides from two Acinetobacter baumannii clinical isolates, MG1 and SMAL
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DOI：
10.1016/j.carres.2011.03.024
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发表时间：
2011-05-15
影响因子：
3.1
通讯作者：
De Castro, Cristina
中科院分区：
文献类型：
--
作者：
Fregolino, Eleonora;Gargiulo, Valentina;De Castro, Cristina
阐明了两种临床分离鲍曼不动杆菌 SMAL 和 MG1 的荚膜多糖 (CPS) 的结构。对干燥生物质进行热苯酚/水提取，然后进行酶消化和反复超速离心，从而分离出多糖，这些多糖在使用抗脂质 A 抗体的蛋白质印迹分析中呈阴性，从而证明它们不是 LPS O 抗原，而是 CPS。它们的结构是在核磁共振波谱和GC-MS分析的基础上确定的。鲍曼不动杆菌 MG1 CPS 由 QuipN4N:4)-alpha-D-GlcpNAc-(1 -> 4)-alpha-L-GalpNAcA-(1 -> 3)-beta-D-QuipNAc4NR-(1 -> R = -3-羟基丁酰基或乙酰基) 的 N-4 氨基处具有酰基取代异质性的线性氨基多糖组成。产生的 CPS 的重复单元SMAL 是一种五糖，已报道鲍曼不动杆菌 ATCC 17961 菌株的 O 抗原部分：beta-D-GlcpNAc3NAcA-(1 向下箭头 4) 6)-beta-D-Glcp-(1 -> 3)-beta-D-GalpNAc-(1 -> 3)-alpha-D-Galp-(1 -> 6)向上箭头beta-D-GlcpNAc-(1(C) 2011 Elsevier Ltd. 保留所有权利。
The structures of the capsular polysaccharides (CPSs) of the two clinical isolates Acinetobacter baumannii SMAL and MG1 were elucidated. Hot phenol/water extractions of the dry biomasses, followed by enzymatic digestions and repeated ultracentrifugations led to the isolation of polysaccharides that were negative in Western blot analysis utilizing an anti-lipid A antibody, thus proving that they were not the LPS O-antigens but CPSs. Their structures were established on the basis of NMR spectroscopy and GC-MS analyses. The A. baumannii MG1 CPS consisted of a linear aminopolysaccharide with acyl substitution heterogeneity at the N-4 amino group of QuipN4N:4)-alpha-D-GlcpNAc-(1 -> 4)-alpha-L-GalpNAcA-(1 -> 3)-beta-D-QuipNAc4NR-(1 -> R = -3-hydroxybutyrryl or acetyl.The repeating unit of the CPS produced by strain SMAL is a pentasaccharide, already reported for the O-antigen moiety from A. baumannii strain ATCC 17961:beta-D-GlcpNAc3NAcA-(1 down arrow 4) 6)-beta-D-Glcp-(1 -> 3)-beta-D-GalpNAc-(1 -> 3)-alpha-D-Galp-(1 -> 6)up arrow beta-D-GlcpNAc-(1(C) 2011 Elsevier Ltd. All rights reserved.