口腔放线菌和链球菌凝集素对免疫球蛋白A1的识别。
Recognition of immunoglobulin A1 by oral actinomyces and streptococcal lectins.
作者信息
Ruhl S, Sandberg A L, Cole M F, Cisar J O
机构信息
Laboratory of Microbial Ecology, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892, USA.
出版信息
Infect Immun. 1996 Dec;64(12):5421-4. doi: 10.1128/iai.64.12.5421-5424.1996.
Abstract
Actinomyces naeslundii and Streptococcus gordonii, oral bacteria that possess Gal/GalNAc- and sialic acid-reactive lectins, respectively, were adherent to immobilized secretory immunoglobulin A (IgA) and two IgA1 myeloma proteins but not to two IgA2 myeloma proteins. Apparently, O-linked oligosaccharides at the hinge region of the IgA1 heavy chain are receptors for lectin-mediated adhesion of these bacteria.
摘要
内氏放线菌和戈登链球菌分别是具有半乳糖/ N - 乙酰半乳糖胺反应性凝集素和唾液酸反应性凝集素的口腔细菌，它们能黏附于固定化的分泌型免疫球蛋白A（IgA）和两种IgA1骨髓瘤蛋白，但不能黏附于两种IgA2骨髓瘤蛋白。显然，IgA1重链铰链区的O - 连接寡糖是这些细菌凝集素介导黏附的受体。
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