Facultad de Medicina Veterinaria y Zootecnia, Universidad Nacional Autónoma de México (UNAM), 04510, Coyoacán, CdMx, Mexico.
Departamento de Biología Celular, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV-IPN), Ave. Instituto Politécnico Nacional 2508, Zacatenco, 07360, CdMx, Mexico.
Vet Res. 2020 Mar 5;51(1):36. doi: 10.1186/s13567-020-00759-z.
Mannheimia haemolytica serotype A2 is the principal cause of pneumonic mannheimiosis in ovine and caprine livestock; this disease is a consequence of immune suppression caused by stress and associated viruses and is responsible for significant economic losses in farm production worldwide. Gram-negative bacteria such as M. haemolytica produce outer membrane (OM)-derived spherical structures named outer membrane vesicles (OMVs) that contain leukotoxin and other biologically active virulence factors. In the present study, the relationship between M. haemolytica A2 and bovine lactoferrin (BLf) was studied. BLf is an 80 kDa glycoprotein that possesses bacteriostatic and bactericidal properties and is part of the mammalian innate immune system. Apo-BLf (iron-free) showed a bactericidal effect against M. haemolytica A2, with an observed minimal inhibitory concentration (MIC) of 16 µM. Sublethal doses (2-8 µM) of apo-BLf increased the release of OMVs, which were quantified by flow cytometry. Apo-BLf modified the normal structure of the OM and OMVs, as observed through transmission electron microscopy. Apo-BLf also induced lipopolysaccharide (LPS) release from bacteria, disrupting OM permeability and functionality, as measured by silver staining and SDS and polymyxin B cell permeability assays. Western blot results showed that apo-BLf increased the secretion of leukotoxin in M. haemolytica A2 culture supernatants, possibly through its iron-chelating activity. In contrast, holo-BLf (with iron) did not have this effect, possibly due to differences in the tertiary structure between these proteins. In summary, apo-BLf affected the levels of several M. haemolytica virulence factors and could be evaluated for use in animals as an adjuvant in the treatment of ovine mannheimiosis.
产单核细胞李氏杆菌 A2 血清型是绵羊和山羊肺部支原体病的主要病原体;这种疾病是由应激和相关病毒引起的免疫抑制引起的,是全球农场生产中重大经济损失的原因。产单核细胞李氏杆菌等革兰氏阴性菌产生的外膜(OM)衍生的球形结构称为外膜囊泡(OMVs),其中包含白细胞毒素和其他具有生物活性的毒力因子。在本研究中,研究了产单核细胞李氏杆菌 A2 与牛乳铁蛋白(BLf)的关系。BLf 是一种 80 kDa 的糖蛋白,具有抑菌和杀菌作用,是哺乳动物先天免疫系统的一部分。脱铁 BLf(无铁)对产单核细胞李氏杆菌 A2 表现出杀菌作用,观察到的最小抑菌浓度(MIC)为 16 µM。亚致死剂量(2-8 µM)的脱铁 BLf 增加了 OMVs 的释放,通过流式细胞术进行了定量。透射电子显微镜观察到,脱铁 BLf 改变了 OM 和 OMVs 的正常结构。脱铁 BLf 还通过银染和 SDS 及多粘菌素 B 细胞通透性测定法诱导细菌释放脂多糖(LPS),破坏 OM 的通透性和功能。Western blot 结果表明,脱铁 BLf 增加了产单核细胞李氏杆菌 A2 培养上清液中白细胞毒素的分泌,可能是通过其铁螯合活性。相比之下,全铁 BLf(含铁)没有这种作用,可能是由于这两种蛋白质的三级结构不同。总之,脱铁 BLf 影响了几种产单核细胞李氏杆菌毒力因子的水平,可作为绵羊支原体病治疗的佐剂在动物中进行评估。