HUMAN-SERUM AMYLOID-P COMPONENT, A CIRCULATING LECTIN WITH SPECIFICITY FOR THE CYCLIC 4,6-PYRUVATE ACETAL OF GALACTOSE - INTERACTIONS WITH VARIOUS BACTERIA

HUMAN-SERUM AMYLOID-P COMPONENT, A CIRCULATING LECTIN WITH SPECIFICITY FOR THE CYCLIC 4,6-PYRUVATE ACETAL OF GALACTOSE - INTERACTIONS WITH VARIOUS BACTERIA
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DOI:
10.1042/bj2250107
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发表时间:
1985-01-01
影响因子:
4.1
通讯作者:
PEPYS, MB
PEPYS, MB
中科院分区:
生物学3区
文献类型:
--
作者:
HIND, CRK;COLLINS, PM;PEPYS, MB

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血清淀粉样蛋白P组分(SAP)是一种正常的血浆糖蛋白,对甲基4,6-O-(1-羧基亚乙基)-β-葡萄糖具有Ca 2+依赖性结合特异性。D-吡喃半乳糖苷(MO β DG)。SAP被发现在体外结合克雷伯氏菌,其细胞壁已知含有这种特定的半乳糖环状丙酮酸缩醛。SAP也以类似的量结合(. apprx. 6000分子/生物体)对A组化脓性链球菌的吸收,但对含有甘露糖的4,6-环丙酮酸缩醛的野油菜黄单胞菌的吸收少得多。没有SAP结合到大肠杆菌(其含有葡萄糖的4,6-环状丙酮酸缩醛)或肺炎链球菌4型(其含有α-葡萄糖的2,3-环状丙酮酸缩醛)。而不是β-在一些实施方案中,所述化合物可与糖基化吡喃半乳糖苷或其他生物体(无乳链球菌、金黄色葡萄球菌和表皮葡萄球菌)结合,其碳水化合物结构的特征不太清楚。SAP与其识别的那些生物体的结合被毫摩尔浓度的游离MO β DG完全抑制或逆转。因此,SAP,一种人血浆蛋白,表现为凝集素,并且可能是细菌和其他生物体细胞壁中其特定特异性配体的有用探针。
Serum amyloid P component (SAP), a normal plasma glycoprotein, has Ca2+-dependent binding specificity for methyl 4,6-O-(1-carboxyethylidene)-.beta.-D-galactopyranoside (MO.beta.DG). SAP was found to bind in vitro to Klebsiella rhinoscleromatis, the cell wall of which is known to contain this particular cyclic pyruvate acetal of galactose. SAP also bound in similar amounts (.apprx. 6000 molecules/organism) to group A Streptococcus pyogenes, but very much less was taken up on Xanthomonas campestris, which contain the 4,6-cyclic pyruvate acetal of mannose. No SAP bound to Escherichia coli, which contains the 4,6-cyclic pyruvate acetal of glucose, or to Streptococcus pneumoniae type 4, which contains the 2,3-cyclic pyruvate acetal of .alpha.- rather than .beta.-galactopyranoside, or to other organisms (Streptococcus agalactiae, Staphylococcus aureus and Staphylococcus epidermidis), the carbohydrate structures of which are less well characterized. Binding of SAP to those organisms which it did recognize was completely inhibited or reversed by millimolar concentrations of free MO.beta.DG. SAP, a human plasma protein, thus, behaves as a lectin and may be a useful probe for its particular specific ligand in the cell walls of bacteria and other organisms.