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人血清IgA抗甘露聚糖抗体对酵母的调理作用以及人多形核白细胞的吞噬作用。

Opsonization of yeast by human serum IgA anti-mannan antibodies and phagocytosis by human polymorphonuclear leucocytes.

作者信息

Yeaman G R, Kerr M A

机构信息

Department of Pathology, University of Dundee, Ninewells Hospital Medical School, UK.

出版信息

Clin Exp Immunol. 1987 Apr;68(1):200-8.

PMID:3308208
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1542678/
Abstract

The ability of sera from 72 patients with liver disease to opsonize yeast for phagocytosis by normal polymorphonuclear leucocytes has been studied. Seven showed defective opsonization. The opsonic activity of all but two sera was decreased markedly by heating at 56 degrees C for 1 h. When the two sera with heat stable opsonic activity were fractionated by gel filtration and by ion exchange chromatography, the activity copurified with IgA, not with IgG. The purified IgA, radiolabelled with 125I was shown to bind in a saturable manner to the yeast. Both sera had high levels of anti-yeast mannan IgA detected by an ELISA. In one case most of the anti-mannan activity was due to monomeric IgA, in the other it was dimeric. This was consistent with the observation of an apparent molecular weight of the opsonin of approximately 180 kD in one serum and 300-400 kD in the other.

摘要

研究了72例肝病患者血清对酵母进行调理作用以便被正常多形核白细胞吞噬的能力。7例显示调理作用缺陷。除两份血清外,所有血清的调理活性在56℃加热1小时后均显著降低。当通过凝胶过滤和离子交换色谱法对两份具有热稳定调理活性的血清进行分级分离时,活性与IgA共纯化,而非与IgG。用125I放射性标记的纯化IgA显示以可饱和方式与酵母结合。通过ELISA检测,两份血清均有高水平的抗酵母甘露聚糖IgA。在1例中,大部分抗甘露聚糖活性归因于单体IgA,在另1例中则为二聚体。这与观察到的一种血清中调理素的表观分子量约为180kD,另一种血清中为300 - 400kD相一致。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/341c/1542678/2918a5bbf574/clinexpimmunol00109-0213-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/341c/1542678/2918a5bbf574/clinexpimmunol00109-0213-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/341c/1542678/2918a5bbf574/clinexpimmunol00109-0213-a.jpg

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