Department of Biological Sciences, Texas Tech University, Lubbock, TX, United States.
Department of Surgery, Texas Tech University Health Sciences Center, Lubbock, TX, United States.
Front Cell Infect Microbiol. 2022 Jul 13;12:898796. doi: 10.3389/fcimb.2022.898796. eCollection 2022.
Calprotectin is a transition metal chelating protein of the innate immune response known to exert nutritional immunity upon microbial infection. It is abundantly released during inflammation and is therefore found at sites occupied by pathogens such as and . The metal limitation induced by this protein has previously been shown to mediate and co-culture. In addition to the transition metal sequestration role of calprotectin, it has also been shown to have metal-independent antimicrobial activity direct cell contact. Therefore, we sought to assess the impact of this protein on the biofilm architecture of and in monomicrobial and polymicrobial culture. The experiments described in this report reveal novel aspects of calprotectin's interaction with biofilm communities of and discovered using scanning electron microscopy and confocal laser scanning microscopy. Our results indicate that calprotectin can interact with microbial cells by stimulating encapsulation in mesh-like structures. This physical interaction leads to compositional changes in the biofilm extracellular polymeric substance (EPS) in both and .
钙卫蛋白是先天免疫反应中的一种过渡金属螯合蛋白，已知其在微生物感染时发挥营养免疫作用。它在炎症期间大量释放，因此在病原体占据的部位如 和 中被发现。先前已经表明，这种蛋白质诱导的金属限制可以介导 和 共培养。除了钙卫蛋白的过渡金属螯合作用外，它还具有独立于金属的抗菌活性 通过直接细胞接触。因此，我们试图评估这种蛋白质对 单微生物和多微生物培养物中 和 生物膜结构的影响。本报告中描述的实验使用扫描电子显微镜和共聚焦激光扫描显微镜揭示了钙卫蛋白与 和 生物膜群落相互作用的新方面。我们的结果表明，钙卫蛋白可以通过刺激网格状结构的包裹与微生物细胞相互作用。这种物理相互作用导致 和 生物膜细胞外聚合物物质 (EPS) 的组成发生变化。
