Department of Microbiology and Immunology, Virginia Commonwealth University, School of Medicine, Richmond, VA 23298-0678, USA.
Microbiology (Reading). 2012 Mar;158(Pt 3):791-803. doi: 10.1099/mic.0.055020-0. Epub 2012 Jan 5.
Naegleria fowleri and Naegleria lovaniensis are closely related free-living amoebae found in the environment. N. fowleri causes primary amoebic meningoencephalitis (PAM), a rapidly fatal disease of the central nervous system, while N. lovaniensis is non-pathogenic. N. fowleri infection occurs when the amoebae access the nasal passages, attach to the nasal mucosa and its epithelial lining, and migrate to the brain. This process involves interaction with components of the host extracellular matrix (ECM). Since the ability to invade tissues can be a characteristic that distinguishes pathogenic from non-pathogenic amoebae, the objective of this study was to assess adhesion to, and invasion of, the ECM by these two related but distinct Naegleria species. N. fowleri exhibited a higher level of adhesion to the ECM components laminin-1, fibronectin and collagen I. Scanning electron microscopy revealed that N. fowleri attached on ECM substrata exhibited a spread-out appearance that included the presence of focal adhesion-like structures. Western immunoblotting revealed two integrin-like proteins for both species, but one of these, with a molecular mass of approximately 70 kDa, was detected at a higher level in N. fowleri. Confocal microscopy indicated that the integrin-like proteins co-localized to the focal adhesion-like structures. Furthermore, anti-integrin antibody decreased adhesion of N. fowleri to ECM components. Finally, N. fowleri disrupted 3D ECM scaffolds, while N. lovaniensis had a minimal effect. Collectively, these results indicate a distinction in adhesion to, and invasion of, ECM proteins between N. fowleri and N. lovaniensis.
福氏耐格里阿米巴和拉氏耐格里阿米巴是两种密切相关的自由生活阿米巴,存在于环境中。福氏耐格里阿米巴引起原发性阿米巴脑膜脑炎(PAM),这是一种迅速致命的中枢神经系统疾病,而拉氏耐格里阿米巴则没有致病性。当阿米巴进入鼻腔、附着在鼻腔黏膜及其上皮衬里并迁移到大脑时,就会发生福氏耐格里阿米巴感染。这个过程涉及到与宿主细胞外基质(ECM)成分的相互作用。由于侵袭组织的能力可能是区分致病性和非致病性阿米巴的一个特征,因此本研究的目的是评估这两种相关但不同的耐格里阿米巴对 ECM 的粘附和侵袭能力。福氏耐格里阿米巴对 ECM 成分层粘连蛋白-1、纤维连接蛋白和胶原 I 的粘附水平更高。扫描电子显微镜显示,福氏耐格里阿米巴附着在 ECM 基质上表现出伸展的外观,包括存在焦点附着样结构。Western 免疫印迹显示两种物种都存在两种整合素样蛋白,但其中一种分子量约为 70 kDa 的蛋白在福氏耐格里阿米巴中检测到更高水平。共聚焦显微镜表明,整合素样蛋白与焦点附着样结构共定位。此外,抗整合素抗体减少了福氏耐格里阿米巴对 ECM 成分的粘附。最后,福氏耐格里阿米巴破坏了 3D ECM 支架,而拉氏耐格里阿米巴的影响则较小。总的来说,这些结果表明福氏耐格里阿米巴和拉氏耐格里阿米巴在 ECM 蛋白的粘附和侵袭方面存在差异。