Recombinant A. caninum NIF antigen, was expressed in Mouse myeloma cell line, NS0. Asn18-Leu274, with a C-terminal 6-His tag (Accession # AAA27789)
> 95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Lyophilized from a 0.2 μm filtered solution in PBS, NaCl, and DTT
2-8°C short term, -20°C long term
Ancylostoma caninum, commonly Dog hookworm, is a parasitic nematode hookworm that infects dogs. The larval stage penetrates the skin and makes it way through the circulatory system into the digestive tract, where adult forms lay eggs that are passed through the feces. Common symptoms include anemia and diarrhea. Newborn pups can die of hemorrhaging from their intestines caused by massive numbers of feeding hookworms. A. braziliense and Uncinaria stenocephala are different species of hookworm which can infect dogs and cause similar symptoms
Neutrophil inhibitory factor (NIF) of the dog hookworm, Ancylostoma caninum, is a 41 kDa secreted glycoprotein that is thought to allow the hookworm to evade the innate immune defenses of the host. NIF interacts with the leukocyte integrin αMβ2 (CD11b/CD18, also called Mac-1), thus inhibiting mammalian neutrophil adhesion to endothelium. The A. caninum NIF cDNA encodes 257 amino acids (aa) including a 17 aa signal sequence and a 240 aa mature protein with 10 cysteine residues and 7 potential N-linked glycosylation sites. Incubation of mammalian neutrophils with NIF does not appear to be toxic, but does result in rapid, cation-dependent, reversible inhibition of αMβ2-mediated adhesion and degranulation. The NIF binding site within the αMβ2 I-domain interferes with activation-dependent adhesion sites of ligands including ICAM-1/CD54, complement component C3b, and fibrinogen. In mouse or guinea pig inflammatory lung injury models, administration of NIF prevented neutrophil-dependent vascular injury.
Ancylostoma caninum; A. caninum; caninum; A. caninum NIF; Neutrophil inhibitory factor; Ancylostoma caninum Neutrophil inhibitory factor protein