作者: Albert Mulenga , Chihiro Sugimoto , Geoffrey Ingram , Kazuhiko Ohashi , Misao Onuma
DOI: 10.1292/JVMS.61.497
关键词:
摘要: Immunological protection of mammalian hosts against tick infestation has been proposed as the most sustainable alternative control method to current use acaricides which several limitations. The success this is dependent on identification key molecules for vaccine antigens. Proteolytic enzymes are involved in a wide range cellular processes eukaryotes such development regulation and nutrition, thus they can be considered good target antigens vaccine. In present study we used primers designed based consensus amino acid motifs flanking conserved active sites C25 N175 all papain-like cysteine proteinases amplify by polymerase chain reaction, sequence characterize two Haemaphysalis longicornis proteinase genes. Based nucleotide deduced sequences, both genes were identified members gene family presence their sequences C25, H150 that proteinases. Both about 1.2 kb size show high homology predominantly invertebrate cathepsin L-like