1.Life Cycle of Dermacentor everestianus Hirst, 1926 (Acari: Ixodidae) under Laboratory Conditions.
Shang JIN ; Tianhong WANG ; Tuo LI ; Ming LIU ; Qingying JIA ; Xiaolong YANG ; Hui WANG ; Zhijun YU ; Jingze LIU
The Korean Journal of Parasitology 2017;55(2):193-196
This study investigated the development characteristics of Dermacentor everestianus under laboratory conditions. The time taken for D. everestianus to complete the whole life cycle was 110.2 days on average, and the average developmental durations of larvae and nymphs were 17.1 days and 29.5 days, respectively. The summation of the prefeeding, feeding, and preoviposition periods of females was 17.8 days, and the oviposition and egg incubation lasted for 18.1 days and 27.7 days, respectively. A highly positive correlation was observed between the weight of engorged female and the number of egg mass laid (r=0.947). The reproductive efficiency index and the reproductive fitness index were 7.1 and 6.1, respectively.
Dermacentor*
;
Female
;
Genetic Fitness
;
Humans
;
Larva
;
Life Cycle Stages*
;
Nymph
;
Oviposition
;
Ovum
3.Gene Cloning, Expression and Immunogenicity of the Protective Antigen Subolesin in Dermacentor silvarum.
Yonghong HU ; Hua ZENG ; Jincheng ZHANG ; Duo WANG ; Dongming LI ; Tiantian ZHANG ; Shujie YANG ; Jingze LIU
The Korean Journal of Parasitology 2014;52(1):93-97
Subolesin (4D8), the ortholog of insect akirins, is a highly conserved protective antigen and thus has the potential for development of a broad-spectrum vaccine against ticks and mosquitoes. To date, no protective antigens have been characterized nor tested as candidate vaccines against Dermacentor silvarum bites and transmission of associated pathogens. In this study, we cloned the open reading frame (ORF) of D. silvarum 4D8 cDNA (Ds4D8), which consisted of 498 bp encoding 165 amino acid residues. The results of sequence alignments and phylogenetic analysis demonstrated that D. silvarum 4D8 (Ds4D8) is highly conserved showing more than 81% identity of amino acid sequences with those of other hard ticks. Additionally, Ds4D8 containing restriction sites was ligated into the pET-32(a+) expression vector and the recombinant plasmid was transformed into Escherichia coli rosetta. The recombinant Ds4D8 (rDs4D8) was induced by isopropyl beta-D-thiogalactopyranoside (IPTG) and purified using Ni affinity chromatography. The SDS-PAGE results showed that the molecular weight of rDs4D8 was 40 kDa, which was consistent with the expected molecular mass considering 22 kDa histidine-tagged thioredoxin (TRX) protein from the expression vector. Western blot results showed that rabbit anti-D. silvarum serum recognized the expressed rDs4D8, suggesting an immune response against rDs4D8. These results provided the basis for developing a candidate vaccine against D. silvarum ticks and transmission of associated pathogens.
Animals
;
Antigens/chemistry/genetics/*immunology/isolation & purification
;
Arthropod Proteins/chemistry/genetics/*immunology/isolation & purification
;
Chromatography, Affinity
;
Cloning, Molecular
;
Cluster Analysis
;
Conserved Sequence
;
Dermacentor/*genetics
;
Electrophoresis, Polyacrylamide Gel
;
Escherichia coli/genetics
;
Gene Expression
;
Humans
;
Molecular Sequence Data
;
Molecular Weight
;
Phylogeny
;
Recombinant Proteins/chemistry/genetics/immunology/isolation & purification
;
Sequence Analysis, DNA
;
Sequence Homology, Amino Acid