Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0851341 (infestation)
 10,121 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We investigated the induction of resistance to Haemaphysalis longicornis infestation in rabbits that had been immunized with recombinant H. longicornis P27/30 protein. The success of immunological control methods is dependent upon the use of potential key antigens as tick vaccine candidates. Previously, we cloned a gene encoding 27 kDa and 30 kDa proteins (P27/30) of H. longicornis, and identified P27/30 as a troponin I-like protein. In this study, rabbits that were immunized with recombinant P27/30 expressed in Escherichia coli showed the statistically significant longer feeding duration for larval and adult ticks (P<0.05), low engorgement rates in larval ticks (64.4%), and an apparent reduction in egg weights, which suggest that H. longicornis P27/30 protein is a potential candidate antigen for a tick vaccine. These results demonstrated that the recombinant P27/30 protein might be a useful vaccine candidate antigen for biological control of H. longicornis.
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PMID:Immunization effect of recombinant P27/30 protein expressed in Escherichia coli against the hard tick Haemaphysalis longicornis (Acari: Ixodidae) in rabbits. 1559 37

The success of immunological control methods is dependent upon the use of potential key antigens as tick vaccine candidates. Previously, we cloned a gene encoding 27 kDa and 30 kDa proteins (P27/30) of Haemaphysalis longicornis, and identified the P27/30 is a troponin I-like protein. In this study, the recombinant P27/30 (rP27/30) expressed in Escherichia coli was used to immunize mice and the mice were challenge-infested with ticks at different developmental stages of the same species. The rP27/30 protein stimulated a specific protective anti-tick immune response in mice, evidenced by the statistically significant longer pre-feeding periods in adult ticks. Furthermore, significantly longer feeding periods were noted in both larval and adult ticks. On the other hand, only larval ticks exhibited low attachment rates (31.1%). Immunization of mice with rP27/30 protein confers protection against hard tick Haemaphysalis longicornis infestation. These results demonstrated that the rP27/30 protein might be a useful vaccine candidate antigen for biological control of ticks.
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PMID:Immunization of mice with recombinant P27/30 protein confers protection against hard tick Haemaphysalis longicornis (Acari: Ixodidae) infestation. 1578 23

Troponin T (TnT) is a key protein for Ca(2+)-sensitive molecular switching of muscle contraction. The entire cDNA sequence of Haemaphysalis qinghaiensis troponin T gene (HqTnT) from the hard tick was cloned here. The cDNA sequence of HqTnT possesses an ORF of 1170 bp coding for a mature protein with 389 amino acid residues and a molecular mass of 46.5 kDa. Search of the cloned sequence in GenBank revealed that HqTnT gene shared some homology with TnT genes of other organisms. By sequence comparison, two conserved domains were identified in the middle (residues 54-78) and close to the carboxyl-terminal end (residues 181-229) of the amino acid sequence of HqTnT. These conserved domains might be responsible for the interaction with tick tropomyosin and troponin I subunit, respectively. Reverse transcription-polymerase chain reaction showed a ubiquitous expression of HqTnT gene at different developmental stages and in different tissues of the tick. The HqTnT was expressed as glutathione S-transferase fused protein in a prokaryotic system. Though rHqTnT could induce specific antibodies in sheep, the antibodies could not protect sheep from the infestation of ticks. Therefore, recombinantly produced HqTnT could not be a candidate antigen for developing anti-tick vaccine. To our knowledge, this is the first report of tick TnT gene.
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PMID:Cloning and characterization of a cDNA clone encoding troponin T from tick Haemaphysalis qinghaiensis (Acari: Ixodidae). 1872 46