Thin pilus PilV adhesins of plasmid R64 recognize specific structures of the lipopolysaccharide molecules of recipient cells
Thin pilus PilV adhesins of plasmid R64 recognize specific structures of the lipopolysaccharide molecules of recipient cells
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DOI：
10.1128/jb.185.17.5192-5199.2003
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发表时间：
2003-09-01
影响因子：
3.2
通讯作者：
Komano, T
中科院分区：
文献类型：
--
作者：
Ishiwa, A;Komano, T
Inc 11质粒R64编码IV型菌毛，称为薄菌毛，其中包括Pi 1V粘附素。PilV粘附素的C-末端区段的七种不同序列可通过改组DNA重排产生。七种PilV粘附素的表达决定了质粒R64的液体交配中的受体特异性。肠道沙门氏菌血清型鼠伤寒LT 2被PilVA'和PiIVB'粘附素识别，而大肠杆菌K-12被PilVA '、PilVC和PiIVC'粘附素识别。受体细胞表面的脂多糖（LPS）先前被证明是七种PilV粘附素的特异性受体。为了鉴定LPS对各种PiIV粘附素的特异性受体结构，用由各种S.肠道血清型鼠伤寒沙门氏菌LT 2和E.大肠杆菌K-12 waa突变体及其衍生物携带不同来源的各种waa基因。通过交配实验，包括抑制实验，我们推测S.肠伤寒血清型LT 2分别作为PiIVB ′和PiIVC ′粘附素的受体，而野生型LT 2 LPS核心中的PiIVC ′受体可能被掩蔽。我们进一步提出，大肠杆菌LPS核心的GlcNAc（β 1 -7）Hep和Glc（α 1 -2）Glc结构可能与大肠杆菌LPS核心的GlcNAc结构有关。coli K-12分别作为PilVC和PilVC'粘附素的受体发挥功能。
Inc1l plasmid R64 encodes a type IV pilus called a thin pilus, which includes Pi1V adhesins. Seven different sequences for the C-terminal segments of PilV adhesins can be produced by shufflon DNA rearrangement. The expression of the seven PilV adhesins determines the recipient specificity in liquid matings of plasmid R64. Salmonella enterica serovar Typhimurium LT2 was recognized by the PilVA' and PiIVB' adhesins, while Escherichia coli K-12 was recognized by the PilVA', PilVC, and PiIVC' adhesins. Lipopolysaccharide (LPS) on the surfaces of recipient cells was previously shown to be the specific receptor for the seven PilV adhesins. To identify the specific receptor structures of LPS for various PiIV adhesins, R64 liquid matings were carried out with recipient cells consisting of various S. enterica serovar Typhimurium LT2 and E. coli K-12 waa mutants and their derivatives carrying various waa genes of different origins. From the mating experiments, including inhibition experiments, we propose that the GlcNAc(alpha1-2)Glc and Glc(alpha1-2)Gal structures of the LPS core of S. enterica serovar Typhimurimn LT2 function as receptors for the PiIVB' and PiIVC' adhesins, respectively, while the PiIVC' receptor in the wild-type LT2 LPS core may be masked. We further propose that the GlcNAc(beta1-7)Hep and Glc(alpha1-2)Glc structures of the LPS core of E. coli K-12 function as receptors for the PilVC and PilVC' adhesins, respectively.