Dietrich Deborah E, Martin Aaron D, Brogden Kim A
Dows Institute for Dental Research, College of Dentistry, The University of Iowa, Iowa City, IA 52242, USA.
SensíQ Technologies Inc., 800 Research Parkway, Suite 100, Oklahoma City, OK 73104, USA.
Peptides. 2014 Mar;53:265-9. doi: 10.1016/j.peptides.2014.01.017. Epub 2014 Feb 2.
Human β-defensin 3 (HBD3) is a small, well-characterized peptide in mucosal secretions with broad antimicrobial activities and diverse innate immune functions. Among these functions is the ability of HBD3 to bind to antigens. In this study, we hypothesize that HBD3 binds to the allergen Bla g2 from the German cockroach (Blattella germanica). The ability of HBD1 (used as a control β-defensin) and HBD3 to bind to Bla g2 and human serum albumin (HSA, used as a control ligand) was assessed using the SensíQ Pioneer surface plasmon resonance (SPR) spectroscopy biosensor system. HBD1 was observed to bind weakly to Bla g2, while HBD3 demonstrated a stronger affinity for the allergen. HBD3 was assessed under two buffer conditions using 0.15 M and 0.3 M NaCl to control the electrostatic attraction of the peptide to the chip surface. The apparent K(D) of HBD3 binding Bla g2 was 5.9±2.1 μM and for binding HSA was 4.2±0.7 μM, respectively. Thus, HBD3, found in mucosal secretions has the ability to bind to allergens like Bla g2 possibly by electrostatic interaction, and may alter the ability of Bla g2 to induce localized allergic and/or inflammatory mucosal responses.
人β-防御素3(HBD3)是一种在黏膜分泌物中已被充分表征的小分子肽,具有广泛的抗菌活性和多种固有免疫功能。这些功能之一是HBD3与抗原结合的能力。在本研究中,我们假设HBD3与德国小蠊(Blattella germanica)的变应原Bla g2结合。使用SensíQ Pioneer表面等离子体共振(SPR)光谱生物传感器系统评估了HBD1(用作对照β-防御素)和HBD3与Bla g2及人血清白蛋白(HSA,用作对照配体)结合的能力。观察到HBD1与Bla g2的结合较弱,而HBD3对该变应原表现出更强的亲和力。在两种缓冲条件下,使用0.15 M和0.3 M NaCl评估HBD3,以控制肽与芯片表面的静电吸引力。HBD3与Bla g2结合的表观解离常数(K(D))为5.9±2.1 μM,与HSA结合的表观解离常数为4.2±0.7 μM。因此,在黏膜分泌物中发现的HBD3可能通过静电相互作用与诸如Bla g2之类的变应原结合,并可能改变Bla g2诱导局部过敏和/或炎症性黏膜反应的能力。