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
中科院分区:
文献类型:
--
作者:
HIND, CRK;COLLINS, PM;PEPYS, MB
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.