INTERACTION OF A SALIVARY MUCIN-SECRETORY IMMUNOGLOBULIN-A COMPLEX WITH MUCOSAL PATHOGENS
INTERACTION OF A SALIVARY MUCIN-SECRETORY IMMUNOGLOBULIN-A COMPLEX WITH MUCOSAL PATHOGENS
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DOI：
10.1128/iai.59.10.3492-3497.1991
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发表时间：
1991-10-01
影响因子：
3.1
通讯作者：
LEVINE, MJ
中科院分区：
文献类型：
--
作者：
BIESBROCK, AR;REDDY, MS;LEVINE, MJ
本研究采用液相、固相和固相测定法研究了人唾液低分子量粘蛋白（MG 2）与金黄色葡萄球菌和铜绿假单胞菌的相互作用。 在溶液相中，人下颌下舌下唾液（HSMSL）中的MG 2与细菌表面结合;然而，高度纯化的粘蛋白亚型（MG 2a和MG 2b）不与细菌表面结合。 粘蛋白结合似乎依赖于MG 2和分泌型免疫球蛋白A（伊加）之间的异型复合，虽然其他唾液分子也可能参与。 相反，在固相测定中，其中HSMSL、具有分泌型伊加的含MG 2的级分和纯化的MG 2被固定到固体表面上，存在最小的S.金黄色。 这些结果表明粘蛋白与S.金黄色葡萄球菌和铜绿假单胞菌的感染可以基于MG 2分泌型伊加复合物的形成。 这种相互作用可能有助于微生物从口腔中清除，并在防止潜在病原体在口腔和呼吸道定植方面发挥重要作用。
This study examined the interaction of a human salivary low-molecular-weight mucin (MG2) with Staphylococcus aureus and Pseudomonas aeruginosa by using both solution-phase and solid-phase and solid-phase assays. In solution phase, MG2 in human submandibular-sublingual saliva (HSMSL) bound to the bacterial surface; however, the highly purified mucin isoforms (MG2a and MG2b) did not. Mucin binding appeared to be dependent on heterotypic complexing between MG2 and secretory immunoglobulin A (IgA), although other salivary molecules may also be involved. In contrast, in a solid-phase assay in which HSMSL, MG2-containing fractions with secretory IgA, and purified MG2 were immobilized onto a solid surface, there was minimal adherence of S. aureus. The collective results suggest that mucin binding to S. aureus and P. aeruginosa may be predicated on the formation of an MG2-secretory IgA complex. Such interactions may facilitate microbial clearance from the oral cavity and play an important role in preventing colonization of the oral cavity and the respiratory tract by potential pathogens.