Lillie Brandon N, Hammermueller Jutta D, Macinnes Janet I, Jacques Mario, Hayes M Anthony
Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ontario Canada N1G 2W1.
Dev Comp Immunol. 2006;30(10):954-65. doi: 10.1016/j.dci.2005.12.008. Epub 2006 Jan 20.
Various collagenous lectins involved in innate immunity bind to surface oligosaccharides of bacteria and other microorganisms. We have been characterizing porcine plasma lectins that bind in a carbohydrate-dependent manner to surfaces of important bacterial pig pathogens including Actinobacillus suis (AS), A. pleuropneumoniae (APP), and Haemophilus parasuis (HP). A plasma protein with 32kDa subunits (pI 5.4 and 5.75) bound most isolates of HP, AS, and some APP. Partial amino acid sequences of this protein were similar to mammalian mannan-binding lectins (MBLs). The corresponding MBL-A cDNA sequences obtained by RT-PCR on liver tissue from pigs and cattle were homologous to the MBL1 gene of mice, rats and the MBL1P1 pseudogene of humans and chimpanzees. While human MBL-C, the product of the MBL2 gene, is known to bind various microorganisms, our studies in pigs provide the first direct evidence that MBL-A has bacteria-binding properties, and suggest it may have antibacterial functions in pigs.
多种参与固有免疫的胶原凝集素可与细菌及其他微生物的表面寡糖结合。我们一直在对猪血浆凝集素进行特性分析，这些凝集素以碳水化合物依赖的方式与重要的猪细菌性病原体表面结合，包括猪放线杆菌（AS）、胸膜肺炎放线杆菌（APP）和副猪嗜血杆菌（HP）。一种具有32kDa亚基（pI 5.4和5.75）的血浆蛋白可结合大多数HP、AS分离株以及一些APP。该蛋白的部分氨基酸序列与哺乳动物甘露聚糖结合凝集素（MBL）相似。通过对猪和牛肝脏组织进行RT-PCR获得的相应MBL-A cDNA序列与小鼠、大鼠的MBL1基因以及人类和黑猩猩的MBL1P1假基因同源。虽然已知MBL2基因的产物人MBL-C可结合多种微生物，但我们在猪身上的研究首次直接证明MBL-A具有细菌结合特性，并表明它可能在猪体内具有抗菌功能。
