Ledermann, K. Burki et al. Shi, C. Kam, J. Powers, R. Aebersold, and A. Kagi, F. Vignaux, B. Ledermann et al. View at: Google Scholar A. Kupfer, S. Singer, and G. View at: Google Scholar T. Lyubchenko, G. Wurth, and A. Stinchcombe, G. Bossi, S. Booth, and G.
Froelich, K. Orth, J. Turbov et al. Trapani, K. Browne, M. Smyth, and D. View at: Google Scholar S. Odake, C. Kam, L. Narasimhan et al. Spaner, K. Raju, L. Radvanyi, Y. Lin, and R. Ober, R. Narayanan, and P. Raju, B. Rabinovich, and R. Odermatt, and T. Matloubian, M. Suresh, A. Glass et al. View at: Google Scholar V. Badovinac, A. Tvinnereim, and J. Badovinac, S. Hamilton, and J. Stepp, P. Mathew, M. Bennett, G. De Saint Basile, and V. Stepp, R. Dufourcq-Lagelouse, F.
Le Deist et al. Walden and H. Hanon, J. Stinchcombe, M. Saito et al. Huang, Y. Yang, H. Sepulveda et al. Chen, M. Woo, R. Hakem, and R. Isaaz, K. Baetz, K. Olsen, E. Podack, and G.
Ida, T. Nakashima, N. Kedersha et al. Hirst, M. Buzza, C. Bird et al. Phillips, J. Opferman, R. Shah, N. Liu, C. Froelich, and P. Zhang, S. Park, Y. Wang et al. Byrne, N. Wang, A. Oxenius, and P. Cannarile, N. Lind, R. Rivera et al. Godfrey, H.
MacDonald, M. Kronenberg, M. Smyth, and L. Bendelac, P. Savage, and L. Ansari, J. Temblay, S. Alyahya, and P. Jacob and D. Kaech, S. Hemby, E. Kersh, and R. Liu, T. Phillips, M. Zhang et al. Forsyth, A. Horvath, and P. Byrne, A. Aucher, S. Alyahya et al. Joshi, W. Cui, A. Chandele et al. Jung, D.
Unutmaz, P. Wong et al. Zammit, L. Cauley, Q. Pham, and L. Belz, C. Smith, D. Eichner et al. View at: Google Scholar W. Heath, G. Belz, G. Behrens et al. Hermans, D. Ritchie, J. Yang, J. Roberts, and F. Yang, S. Huck, R. McHugh, I. Hermans, and F. Wakim, J. Waithman, N. Van Rooijen, W. Heath, and F. Wong and E. Medema, J. De Jong, L. Peltenburg et al.
Lovo, M. Zhang, L. Graubert, J. DiPersio, J. Russell, and T. View at: Google Scholar Y. Miura, C. Thoburn, E. Bright, and A. Goldbach-Mansky, S. Suson, R. Wesley, C. Hack, H. El-Gabalawy, and P. Kraan, J. Haringman, H. Weedon et al. Choy, R. Cruz, A. Garrett, M. Identification and analysis of serpin-family genes by homology and synteny across the 12 sequenced Drosophilid genomes.
BMC Genomics 10 , Evans, J. Immune pathways and defence mechanisms in honey bees Apis mellifera. Insect Mol. Comparative analysis of serine protease-related genes in the honey bee genome: possible involvement in embryonic development and innate immunity. Comparative genomic analysis of the Tribolium immune system. Genome Biol. A comparative analysis of serpin genes in the silkworm genome. Genomics 93 , — Lin, H.
Characterization and expression profiling of serine protease inhibitors in the diamondback moth, Plutella xylostella Lepidoptera: Plutellidae. BMC Genomics 18 , Zhao, P. Genome-wide identification and immune response analysis of serine protease inhibitor genes in the silkworm, Bombyx mori. PLoS One 7 , e Yang, L. The genomic and transcriptomic analyses of serine proteases and their homologs in an endoparasitoid.
Pteromalus puparum. Li, J. The structure of active serpin 1K from Manduca sexta. Elliott, P. Wild-type alpha 1 -antitrypsin is in the canonical inhibitory conformation. Wu, C. An insect TEP in a crustacean is specific for cuticular tissues and involved in intestinal defense.
Yan, Z. Insights into the venom composition and evolution of an endoparasitoid wasp by combining proteomic and transcriptomic analyses. Meekins, D. Serpins in arthropod biology. Cell Dev. Jiang, H. Organization of serpin gene-1 from Manduca sexta - Evolution of a family of alternate exons encoding the reactive site loop.
Liu, H. Alternative splicing of the antitrypsin gene in the silkworm. Bombyx mori. A venom serpin splicing isoform of the endoparasitoid wasp Pteromalus puparum suppresses host Prophenoloxidase cascade by forming complexes with host hemolymph proteinases. Simonet, G. Characterization of two novel pacifastin-like peptide precursor isoforms in the desert locust Schistocerca gregaria : cDNA cloning, functional analysis and real-time RT-PCR gene expression studies.
Genomics, evolution and biological functions of the pacifastin peptide family: a conserved serine protease inhibitor family in arthropods. Peptides 24 , — Xu, G. Identification and expression profiles of neuropeptides and their G protein-coupled receptors in the rice stem borer Chilo suppressalis.
Jiang, R. Ligoxygakis, P. A serpin regulates dorsal-ventral axis formation in the Drosophila embryo. Coleman, S. A Drosophila male accessory-gland protein that is a member of the serpin superfamily of proteinase-inhibitors is transferred to females during mating. Abraham, E. An immune-responsive serpin, SRPN6, mediates mosquito defense against malaria parasites.
USA , — Kramerova, I. Alternative splicing of papilin and the diversity of Drosophila extracellular matrix during embryonic morphogenesis. Tzarfati-Majar, V. F-spondin is a contact-repellent molecule for embryonic motor neurons.
USA 98 , — Vanleuven, F. Human alphamacroglobulin - structure and function. Sekiguchi, R. Evolution of the thioester-containing protein genes in the arthropoda. Immunobiology , — Colinet, D. Identification of the main venom protein components of Aphidius ervi , a parasitoid wasp of the aphid model Acyrthosiphon pisum. BMC Genomics 15 , Martinson, E. The evolution of venom by co-option of single-copy genes.
Laterally transferred gene recruited as a venom in parasitoid wasps. Werren, J. Functional and evolutionary insights from the genomes of three parasitoid Nasonia species.
Thompson, J. Nucleic Acids Res. Tamura, K. MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Untergasser, A. Primer3-new capabilities and interfaces. Livak, K. Methods 25 , — Wang, L.
Bioinformatics 26 , — Download references. You can also search for this author in PubMed Google Scholar. All authors contributed to the final paper. Correspondence to Gongyin Ye. Publisher's note: Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
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Sorry, a shareable link is not currently available for this article. Trichinella and Trichinosis. Castillo Alvarez, A. A prime-boost vaccination of mice with attenuated Salmonella expressing a mer peptide from the Trichinella spiralis gp43 antigen. Cui, J. Survey of Trichinella infections in domestic pigs from northern and eastern Henan, China. Vaccine 31, — Biochemical and functional characterization of the glutathione S-transferase from Trichinella spiralis.
Characterization of a Trichinella spiralis 31 kDa protein and its potential application for the serodiagnosis of trichinellosis. Acta Trop. An epidemiological overview of swine trichinellosis in China. The epidemiology of human trichinellosis in China during Deville, S. Influence of adjuvant formulation on the induced protection of mice immunized with total soluble antigen of Trichinella spiralis.
Duggan, B. Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2. Dupouy-Camet, J. Opinion on the diagnosis and treatment of human trichinellosis. Expert Opin. Dzik, J.
Molecules released by helminth parasites involved in host colonization. Acta Biochim. PubMed Abstract Google Scholar. Gajadhar, A. Trichinella diagnostics and control: mandatory and best practices for ensuring food safety. Gamble, H. International commission on Trichinellosis: recommendations on methods for the control of Trichinella in domestic and wild animals intended for human consumption. Gettins, P. Serpin structure, mechanism, and function. Gu, Y. Vaccination with a paramyosin-based multi-epitope vaccine elicits significant protective immunity against Trichinella spiralis infection in mice.
Jiang, P. Survey of Trichinella infection from domestic pigs in the historical endemic areas of Henan province, central China. Jin, X. Identification and characterization of a serine protease inhibitor with two trypsin inhibitor-like domains from the human hookworm Ancylostoma duodenale.
Larkin, M. Clustal W and Clustal X version 2. Bioinformatics 23, — Li, F. Sensitivity and optimization of artificial digestion in the inspection of meat for Trichinella spiralis. Foodborne Pathog. Li, L. Trichinella spiralis : low vaccine potential of glutathione S-transferase against infections in mice. Liu, C. Characterization of a putative glutathione S-transferase from the parasitic nematode Trichinella spiralis. Cloning and expression of a Trichinella spiralis putative glutathione S-transferase and its elicited protective immunity against challenge infections.
Vectors Liu, P. Oral vaccination of mice with Trichinella spiralis nudix hydrolase DNA vaccine delivered by attenuated Salmonella elicited protective immunity.
Liu, R. Comparative proteomic analysis of surface proteins of Trichinella spiralis muscle larvae and intestinal infective larvae. Screening and characterization of early diagnostic antigens in excretory-secretory proteins from Trichinella spiralis intestinal infective larvae by immunoproteomics. Proteomic analysis of Trichinella spiralis adult worm excretory-secretory proteins recognized by early infection sera.
Analysis of differentially expressed genes of Trichinella spiralis larvae activated by bile and cultured with intestinal epithelial cells using real-time PCR. Long, S. Characterization and functional analysis of Trichinella spiralis Nudix hydrolase.
Maizels, R. Susceptibility and immunity to helminth parasites. Martzen, M. Ascaris suum : localization by immunochemical and fluorescent probes of host proteases and parasite proteinase inhibitors in cross-sections. McGuire, C. Nasal immunization with homogenate and peptide antigens induces protective immunity against Trichinella spiralis. McVay, C. Antibodies to tyvelose exhibit multiple modes of interference with the epithelial niche of Trichinella spiralis. Participation of parasite surface glycoproteins in antibody-mediated protection of epithelial cells against Trichinella spiralis.
Mitreva, M. The IL1 excretory-secretory ES proteins were prepared [ 25 ]. The primary IECs were prepared from fetal mouse intestines and susceptible to T. The mouse striated muscle myoblast C2C12 was unsusceptible to the larval invasion and utilized as negative control [ 26 ]. The IEC lysates were prepared with the help of grinding, sonicating and centrifuging as described [ 27 ]. The TsSPI was induced with 0. Anti-rTsSPI immune serum were collected at two weeks following the fourth immunization, and pre-immune normal serum was used as negative control [ 32 ].
Catalytic substrate reaction occurs every minute, and the enzyme required for every 0. Each sample had three replicates. The absorbance at nm was measured by a spectrophotometer Mapada, Shanghai, China. The inhibition rate was calculated as follows:. The rTsSPI 1. Aliquots 1. The absorbance at nm was measured as above described.
The monolayer cell nuclei were dyed with propidium iodide PI. After being washed again, the cells were observed with the aid of fluorescent microscopy Olympus, Tokyo, Japan [ 43 ]. The IIF was performed as reported with some modifications [ 39 , 44 ]. The intestinal epithelium cell nuclei were stained with PI.
Finally, the sections were observed using fluorescent microscopy Olympus [ 45 ]. The media were supplemented with anti-rTsSPI serum to , or infection serum or pre-immune serum diluted at [ 26 ]. The larvae invaded and migrated into the monolayer were counted as invaded larvae, whereas the larvae suspended in the media were counted as non-invaded larvae [ 47 , 48 ].
Three independent tests for three groups of serum samples were carried out and three repeats were used to determine the larval invasion for each kind of serum. Infection serum and pre-immune serum were utilized as positive and negative control, respectively. Peritoneal exudates cells PECs were collected from peritoneal exudate of normal mice after intraperitoneal injection with 4.
After five days, peritoneal cavity was washed with RPMI The number of PECs was estimated in a cell counter. The cell suspensions contained 2. Each assay was performed in triplicate. The larval viability treated by ADCC was estimated on the basis of their morphology and activity under microscope. The living NBL are mobile and show wriggling motion, while the dead worms are straight, inactive or disintegrated [ 45 , 51 ].
The data were statistically analyzed using the SPSS Chi-square tests or one-way ANOVAs were utilized to analyze the differences between different groups. The proteolytic activity of trypsin was also inhibited by natural inhibitor phenylmethylsulfonyl fluoride PMSF Fig.
The results revealed that the trypsin enzymatic activity was inhibited with rTsSPI. The inhibition rate was The titration curve graph of trypsin activity inhibited by rTsSPI.
The absorbance at nm was measured by spectrophotometry with the substrate BAEE, and the inhibition rate of trypsin enzymatic activity was calculated as described in method section. Each point is the mean of triplicates. The residual enzymatic activity of trypsin was determined with BAEE as a substrate. The results showed about 29 protein bands with a molecular weight of Propidium iodide PI dyed cell nuclei in red.
The results of IIF with intestinal and liver sections revealed that after incubation with rTsSPI, immunostaining on intestinal epithelium was detected by using anti-rTsSPI serum; weak staining was also detected with infection serum Fig.
These sections were examined by fluorescent microscopy. When the IEC monolayer was covered by semisolid media containing the larvae, and cultured for 2 h, the larvae invaded and migrated in the IEC monolayer Fig. When dilution of anti-rTsSPI serum, infection serum and pre-immune serum were added into the media and cultured for 2 h, the invaded larvae in the monolayer represented The in vitro inhibition of T.
The dilutions of infection serum IS and pre-immune serum PI were utilized as control sera. The results are shown as the percent of the larvae invaded the monolayer out of all larvae added into the media.
ADCC killing T. Infection serum e and pre-immune serum f were utilized as control sera. SDS-PAGE analysis and spectrophotometry showed that the rTsSPI reacted strongly with porcine trypsin, had inhibitory activities against porcine trypsin, and the inhibition was rTsSPI dose-dependent, demonstrating that trypsin may be the possible target of the inhibitor [ 16 ]. However, the precise role that the inhibitor might play in T.
A hookworm Ancylostoma duodenale adult serpin AduTIL-1 has been expressed, being distributed in cuticle surface, oesophagus and intestines of adult worms; this rAduTIL-1 was found to show inhibitory activity against human neutrophil elastase and pancreatic trypsin. AduTIL-1 may participate in Ancylostoma survival in host by targeting relative digestive enzymes and elastase [ 52 ].
A Schistosoma haematobium serpin was located on the surface of this schistosome and can interact with host cells and proteases [ 53 ]. The protection mechanism could be similar to the one described for Ascaris suum [ 55 ]. Anti-TsSPI antibodies could inhibit the anti-proteolytic activity of serpins in a way similar to that observed for serpins originating from other parasites, such as S.
Anti- Trichinella antibodies could bind to T.
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