• Cystic echinococcosis
• Diagnosis
• ELISA
• Human
• Recombinant fusion protein

• ELISA
• Echinococcus vogeli
• antigen B
• immunodiagnosis
• polycystic echinococcosis
• recombinant antigens

Echinococcoses, caused by metacestodes of Echinococcus granulosus (cystic echinococcosis; CE) and E. multilocularis (alveolar echinococcosis; AE), represent major emerging parasitic diseases. These enzootic helminthiases invoke significant public health concerns and social burdens in endemic areas. The diseases are prevalent in the Qinghai-Tibetan Plateau, China, while community-based epidemiological studies have been scarcely reported. We surveyed echinococcosis patients in the southeastern Qinghai Province, China, to better understand the concurrent epidemiological situation in this area.

During July and August of 2013 and 2014, we screened echinococcosis patients at Yushu and Golog Prefectures, Qinghai Province, China, in a diagnostic campaign. A total of 2856 people (male:female ratio, 1:1.12; mean age, 34.6 years; age range, 6–88 years) were ultrasonographically examined for the presence of hepatic echinococcal cysts. We also collected serum samples from patients and analyzed antibody reactivity against recombinant forms of diverse E. granulosus antigen Bs (rEgAgB1-5) by enzyme-linked immunosorbent assay.

We detected 134 patients whose imaging scans were compatible with CE (115 cases) and AE (20 patients). One patient might have been infected with both CE and AE. The overall incidence was 4.7% (CE, 4.0%; AE, 0.7%). A large proportion (67.5%) of CE patients was diagnosed at active and transitional CE1-CE3 stages in their late 30s. The AE cases were generally detected at advanced stage in patients at early 20s (60%). Analysis of the receiver operating characteristic curve and Youden’s index indicated that rEgAgB2 was the most promising biomarker, followed by rEgAgB3 and rEgAgB1. Overall, sensitivity and specificity of rEgAgB1-3 were 84.5–92.7% and 91.9–94.6%, respectively. rEgAgB4 and 5 showed low sensitivity with high cross-reactivity.

Our results strongly suggest that disability-adjusted life years related to echinococcoses in Qinghai-Tibetan areas might be more serious than previously considered. Control and prevention strategy against CE and AE are highly required in these areas. In addition to ultrasonography, serological tests might provide supportive data. However, serological data should be carefully interpreted for differential diagnosis, especially in areas where both CE and AE are co-endemic.

The online version of this article (10.1186/s13071-019-3569-6) contains supplementary material, which is available to authorized users.

• Antigen B isoforms
• E. multilocularis
• Echinococcoses
• Echinococcus granulosus
• Immunoreactivity
• Qinghai-Tibetan Plateau
• Ultrasonography

Hydatidosis is a zoonotic infection and endemic in Iran. Due to the serological cross-reactivity (of sera) with other parasitic infection, diagnosis of hydatid cyst is considered to be problematic. In this regard, application of recombinant antigens improves serological diagnosis for human hydatidosis. Here, we present an ELISA test based on B8/2 recombinant antigen of Echinococcus granulosus with particular regard to its capability to diagnose human hydatidosis.

The synthesized E. granulosus B8/2 (EgB8/2) gene was sub-cloned into pET28b (+) plasmid. Nde1 and Hind3 restriction enzymes were used to confirm the recombinant plasmid extraction. Cloning was verified by colony PCR, digestion enzymes, and sequence determination methods. To express rtEgB8/2, strains of Escherichia coli BL21 (DE3) pLysS and Rosetta (DE3) were induced with isopropyl β-D-1-thiogalactopyranoside (IPTG). A Ni-NTA column was used for purification, and the expressed protein was analyzed by SDS-PAGE as well as western blotting. ELISA test was used to identify the antigenicity of produced protein.

The presence of EgB8/2 gene fragment in the recombinant plasmid was confirmed. SDS-PAGE showed that the BL21 (DE3) pLysS strain had the highest level of expression and a protein band of 11 kDa was observed in induced bacteria. Western blotting approved the purity of rtEgB8/2 protein, and ELISA test measured sensitivity and specificity as 95% and 97.5%, respectively.

E. granulosus metacestode contains a high amount of antigen B protein. These results confirm the reproducibility of high-quality rtEgB8/2 recombinant antigen as a reliable candidate in serological test.

• Diagnosis
• Echinococcus
• Hydatidosis
• Recombinant EgB8/2 – protein
• ranulosus ELISA

• ELISA
• Echinococcus granulosus
• Protein expression
• Purification
• Truncated EgB8/1
• Western blotting

• Animals
• Antibodies, Helminth/blood
• Antibodies, Helminth/immunology
• Antigens, Helminth/blood
• Antigens, Helminth/immunology
• Blotting, Western
• Cross Reactions
• Echinococcosis/diagnosis
• Echinococcus granulosus/immunology
• Enzyme-Linked Immunosorbent Assay/methods
• Humans
• Recombinant Proteins/blood
• Recombinant Proteins/immunology
• Sensitivity and Specificity
• Serologic Tests

• ELISA
• backyard pig
• influenza
• serology
• surveillance
• swine

• Antigen B2 (2B2t)
• P1 and P5 peptide of EPC1
• cystic echinococcosis
• diagnosis
• recombinant fusion protein

• ELISA/enzyme-linked immunosorbent assay
• Echinococcus spp
• cytokine
• hydatidosis
• immunodiagnosis

• China
• canine
• diagnosis
• taeniid cestodes
• zoonosis

• Animals
• Antibodies
• Antigens
• Cytokines
• DNA
• Echinococcus
• Followup
• Laboratory diagnosis
• Lymphoproliferation
• Patients

Taenia saginata, Taenia solium and Taenia asiatica (beef, pork and Asian tapeworms, respectively) are parasitic flatworms of major public health and food safety importance. Among them, T. asiatica is a newly recognized species that split from T. saginata via an intermediate host switch ∼1.14 Myr ago. Here we report the 169- and 168-Mb draft genomes of T. saginata and T. asiatica. Comparative analysis reveals that high rates of gene duplications and functional diversifications might have partially driven the divergence between T. asiatica and T. saginata. We observe accelerated evolutionary rates, adaptive evolutions in homeostasis regulation, tegument maintenance and lipid uptakes, and differential/specialized gene family expansions in T. asiatica that may favour its hepatotropism in the new intermediate host. We also identify potential targets for developing diagnostic or intervention tools against human tapeworms. These data provide new insights into the evolution of Taenia parasites, particularly the recent speciation of T. asiatica.

Only one of the three Taenia species causing taeniasis in humans was previously sequenced. Here the authors provide draft genomes of Taenia saginata and Taenia asiatica, analyse genome evolution of all three species, and identify potential targets for developing diagnostic markers or intervention tools.

• Cystic echinococcosis
• Hydatid cyst
• Immunodiagnosis

The hydatid disease parasite Echinococcus granulosus has a restricted lipid metabolism, and needs to harvest essential lipids from the host. Antigen B (EgAgB), an abundant lipoprotein of the larval stage (hydatid cyst), is thought to be important in lipid storage and transport. It contains a wide variety of lipid classes, from highly hydrophobic compounds to phospholipids. Its protein component belongs to the cestode-specific Hydrophobic Ligand Binding Protein family, which includes five 8-kDa isoforms encoded by a multigene family (EgAgB1-EgAgB5). How lipid and protein components are assembled into EgAgB particles remains unknown. EgAgB apolipoproteins self-associate into large oligomers, but the functional contribution of lipids to oligomerization is uncertain. Furthermore, binding of fatty acids to some EgAgB subunits has been reported, but their ability to bind other lipids and transfer them to acceptor membranes has not been studied.

Lipid-free EgAgB subunits obtained by reverse-phase HPLC were used to analyse their oligomerization, ligand binding and membrane interaction properties. Size exclusion chromatography and cross-linking experiments showed that EgAgB8/2 and EgAgB8/3 can self-associate, suggesting that lipids are not required for oligomerization. Furthermore, using fluorescent probes, both subunits were found to bind fatty acids, but not cholesterol analogues. Analysis of fatty acid transfer to phospholipid vesicles demonstrated that EgAgB8/2 and EgAgB8/3 are potentially capable of transferring fatty acids to membranes, and that the efficiency of transfer is dependent on the surface charge of the vesicles.

We show that EgAgB apolipoproteins can oligomerize in the absence of lipids, and can bind and transfer fatty acids to phospholipid membranes. Since imported fatty acids are essential for Echinococcus granulosus, these findings provide a mechanism whereby EgAgB could engage in lipid acquisition and/or transport between parasite tissues. These results may therefore indicate vulnerabilities open to targeting by new types of drugs for hydatidosis therapy.

Echinococcus granulosus is a causative agent of hydatidosis, a parasitic disease that affects humans and livestock with significant economic and public health impact worldwide. Antigen B (EgAgB), an abundant product of E. granulosus larvae, is a lipoprotein that carries a wide variety of lipids, including fatty acids and cholesterol. As E. granulosus is unable to synthesize these lipids, EgAgB likely plays an important role in parasite metabolism, participating in both the acquisition of host lipids and their distribution between parasite tissues. The protein component of EgAgB consists of 8 kDa subunits encoded by separate genes. However, the biochemical properties of EgAgB subunits, particularly their ability to bind and transfer lipids, are poorly known. Herein, using in vitro assays, we found that EgAgB subunits were capable of oligomerizing in the absence of lipids and to bind fatty acids, but not cholesterol. Moreover, EgAgB subunits showed the ability to transfer fatty acids to artificial phospholipid membranes. These results indicate new points of attack at which the parasite might be vulnerable to drugs.

• Amino Acid Sequence
• Animals
• Echinococcosis/parasitology
• Fatty Acids/metabolism
• Humans
• Lipids
• Lipoproteins/chemistry
• Lipoproteins/metabolism
• Membranes/metabolism
• Molecular Sequence Data
• Phospholipids/metabolism
• Polymerization
• Protein Subunits

• Wellcome Trust

• Antigen B
• Cestode
• Echinococcus
• HLBP
• Lipoprotein
• Tapeworm

• Amino Acid Sequence
• Animals
• Carrier Proteins/metabolism
• Echinococcosis/parasitology
• Echinococcus granulosus/growth & development
• Echinococcus granulosus/physiology
• Host-Parasite Interactions
• Humans
• Lipoproteins/chemistry
• Lipoproteins/metabolism
• Models, Molecular
• Molecular Sequence Data
• Sequence Alignment

• Haematophagous
• Naturally acquired tick resistance
• Paramyosin
• Rhipicephalus (Boophilus) microplus
• Tick-bovine relationship

Two main families of lipid binding proteins have been identified in parasitic Platyhelminthes: hydrophobic ligand binding proteins (HLBPs) and fatty acid binding proteins (FABPs). Members of the former family of proteins are specific to the Cestoda class, while FABPs are conserved across a wide range of animal species. Because Platyhelminthes are unable to synthesize their own lipids, these lipid-binding proteins are important molecules in these organisms. HLBPs are a high molecular mass complex of proteins and lipids. They are composed of subunits of low molecular mass proteins and a wide array of lipid molecules ranging from CoA esters to cholesterol. These proteins are excretory-secretory molecules and are key serological tools for diagnosis of diseases caused by cestodes. FABPs are mainly intracellular proteins of low molecular weight. They are also vaccine candidates. Despite that the knowledge of their function is scarce, the differences in their molecular organization, ligand preferences, intra/extracellular localization, evolution, and phylogenetic distribution, suggest that platyhelminths HLBPs and FABPs should play different functions. FABPs might be involved in the removal of fatty acids from the inner surface of the cell membrane and in their subsequent targeting to specific cellular destinations. In contrast, HLBPs might be involved in fatty acid uptake from the host environment.

• Echinococcus
• FABPs
• HLBPs
• platyhelminthes

A standardized test for the serodiagnosis of human cystic echinococcosis (CE) is still needed, because of the low specificity and sensitivity of the currently available commercial tools and the lack of proper evaluation of the existing recombinant antigens. In a previous work, we defined the new ELISA-B2t diagnostic tool for the detection of specific IgGs in CE patients, which showed high sensitivity and specificity, and was useful in monitoring the clinical evolution of surgically treated CE patients. Nevertheless, this recombinant antigen gave rise to false-negative results in a percentage of CE patients. Therefore, in an attempt to improve its sensitivity, we constructed B2t-derived recombinant antigens with two, four and eight tandem repeat of B2t units, and tested them by ELISA on serum samples of CE patients and patients with related parasites. The best diagnostic values were obtained with the two tandem repeat 2B2t antigen. The influence of several clinical variables on the performance of the tests was also evaluated. Finally, the diagnostic performance of the 2B2t-ELISA was compared with that of an indirect haemagglutination commercial test. The 2B2t recombinant antigen performed better than the HF and B2t antigens, and the IHA commercial kit. Therefore, this new 2B2t-ELISA is a promising candidate test for the serodiagnosis of CE in clinical settings.

Cystic echinococcosis (CE) is a widespread zoonotic disease. Its complex clinical presentation precludes a “one-size-fits-all” approach to clinical management, particularly with regard to serodiagnosis. While CE is often detected incidentally by imaging, imaging findings may be inconclusive. Therefore, there is a need for standardised and approachable diagnostic tools that may complement imaging data. In this regard, serological tests based in the use of native antigens like hydatid fluid present a low specificity and sensitivity. Although recombinant antigens with potential to replace native antigens have been proposed in the literature, none has been systematically tested for diagnostic performance. Here, we describe the new recombinant antigen 2B2t, derived from the previously described recombinant B2t, and determine its usefulness for the serodiagnosis of CE by ELISA in patients with a complete set of clinical data. The influence of clinical variables on the performance of 2B2t was evaluated and compared with the hydatid fluid (the most commonly used antigen for CE serology) and a commercial diagnostic kit based on the haemagglutination reaction. Our results show that the 2B2t antigen has potential to be routinely used for the standardised diagnosis of CE in clinical settings.

• Animals
• Chemical Fractionation
• Chromatography, Gas
• Echinococcus granulosus/chemistry
• Lipids/analysis
• Lipids/isolation & purification
• Lipoproteins/chemistry
• Lipoproteins/isolation & purification
• Molecular Weight

• Amino Acid Sequence
• Animals
• Cattle
• Echinococcosis/parasitology
• Electrophoresis
• Humans
• Lipoproteins/chemistry
• Lipoproteins/isolation & purification
• Mass Spectrometry
• Microscopy
• Molecular Sequence Data
• Protein Multimerization
• Protein Subunits/chemistry
• Sequence Homology, Amino Acid

• Animals
• Australia
• China
• Conserved Sequence
• DNA, Helminth/genetics
• Dogs
• Echinococcosis/parasitology
• Echinococcosis/veterinary
• Echinococcus granulosus/genetics
• Echinococcus granulosus/isolation & purification
• Gene Expression Profiling
• Gene Expression Regulation
• Genes, Helminth
• Lipoproteins/genetics
• Macropodidae/parasitology
• Multigene Family
• Polymerase Chain Reaction
• Polymorphism, Genetic
• Sequence Alignment

Production of native antigens for serodiagnosis of helminthic infections is laborious and hampered by batch-to-batch variation. For serodiagnosis of echinococcosis, especially cystic disease, most screening tests rely on crude or purified Echinococcus granulosus hydatid cyst fluid. To resolve limitations associated with native antigens in serological tests, the use of standardized and highly pure antigens produced by chemical synthesis offers considerable advantages, provided appropriate diagnostic sensitivity and specificity is achieved.

Making use of the growing collection of genomic and proteomic data, we applied a set of bioinformatic selection criteria to a collection of protein sequences including conceptually translated nucleotide sequence data of two related tapeworms, Echinococcus multilocularis and Echinococcus granulosus. Our approach targeted alpha-helical coiled-coils and intrinsically unstructured regions of parasite proteins potentially exposed to the host immune system. From 6 proteins of E. multilocularis and 5 proteins of E. granulosus, 45 peptides between 24 and 30 amino acids in length were designed. These peptides were chemically synthesized, spotted on microarrays and screened for reactivity with sera from infected humans. Peptides reacting above the cut-off were validated in enzyme-linked immunosorbent assays (ELISA). Peptides identified failed to differentiate between E. multilocularis and E. granulosus infection. The peptide performing best reached 57% sensitivity and 94% specificity. This candidate derived from Echinococcus multilocularis antigen B8/1 and showed strong reactivity to sera from patients infected either with E. multilocularis or E. granulosus.

This study provides proof of principle for the discovery of diagnostically relevant peptides by bioinformatic selection complemented with screening on a high-throughput microarray platform. Our data showed that a single peptide cannot provide sufficient diagnostic sensitivity whereas pooling several peptide antigens improved sensitivity; thus combinations of several peptides may lead the way to new diagnostic tests that replace, or at least complement conventional immunodiagnosis of echinococcosis. Our strategy could prove useful for diagnostic developments in other pathogens.

Crude or purified, somatic or metabolic extracts of native antigens are routinely used for the serodiagnosis of human helminthic infections. These antigens are often cross-reactive, i.e., recognized by sera from patients infected with heterologous helminth species. To overcome limitations in antigen production, test sensitivity and specificity, chemically synthesized peptides offer a pure and standardized alternative, provided they yield acceptable operative characteristics. Ongoing genome and proteome work create new resources for the identification of antigens. Making use of the growing amount of genomic and proteomic data available in public databases, we tested a bioinformatic procedure for the selection of potentially antigenic peptides from a collection of protein sequences including conceptually translated nucleotide sequence data of Echinococcus multilocularis and E. granulosus (Plathyhelminthes, Cestoda). The in silico selection was combined with high-throughput screening of peptides on microarray and systematic validation of reactive candidates in enzyme-linked immunosorbent assay. Our study proved the applicability of this approach for selection of peptide antigens with good diagnostic characteristics. Our results suggested the pooling of several peptides to reach a high level of sensitivity required for reliable immunodiagnosis.

• Animals
• Antibodies, Helminth/blood
• Antigens, Helminth
• Echinococcosis/diagnosis
• Echinococcus granulosus/genetics
• Echinococcus granulosus/immunology
• Echinococcus multilocularis/genetics
• Echinococcus multilocularis/immunology
• Enzyme-Linked Immunosorbent Assay
• Humans
• Parasitology/methods
• Peptides/chemical synthesis
• Protein Array Analysis
• Sensitivity and Specificity
• Serologic Tests/methods

• Animals
• Antibodies, Protozoan/blood
• Clinical Laboratory Techniques/methods
• Echinococcosis/diagnosis
• Echinococcus granulosus/genetics
• Echinococcus granulosus/immunology
• Enzyme-Linked Immunosorbent Assay/methods
• Humans
• Lipoproteins
• Recombinant Proteins
• Sensitivity and Specificity

• Animals
• DNA, Protozoan/chemistry
• DNA, Protozoan/genetics
• Echinococcosis/diagnosis
• Echinococcosis/epidemiology
• Echinococcosis/parasitology
• Echinococcus granulosus/genetics
• Echinococcus granulosus/isolation & purification
• Echinococcus multilocularis/genetics
• Echinococcus multilocularis/isolation & purification
• Feces/parasitology
• Humans
• Polymerase Chain Reaction
• Zoonoses/epidemiology
• Zoonoses/parasitology

• Amino Acid Sequence
• Animals
• Base Sequence
• Camelus
• Cattle
• Cluster Analysis
• DNA, Complementary/chemistry
• DNA, Helminth/chemistry
• Echinococcosis/parasitology
• Echinococcus granulosus/classification
• Echinococcus granulosus/genetics
• Echinococcus granulosus/immunology
• Lipoproteins/chemistry
• Lipoproteins/genetics
• Molecular Sequence Data
• Multigene Family
• Phylogeny
• Polymorphism, Genetic
• Polymorphism, Single-Stranded Conformational
• Reverse Transcriptase Polymerase Chain Reaction
• Sequence Alignment
• Sheep
• Swine

• Aftercare
• Animals
• Antibodies, Helminth/biosynthesis
• Antibodies, Helminth/blood
• Antigens, Helminth/analysis
• Antigens, Helminth/genetics
• Cross Reactions
• Disease Reservoirs
• Dog Diseases/diagnosis
• Dog Diseases/parasitology
• Dogs/parasitology
• Echinococcosis/diagnosis
• Echinococcosis/immunology
• Echinococcosis/parasitology
• Echinococcus granulosus/genetics
• Echinococcus granulosus/growth & development
• Echinococcus granulosus/immunology
• Echinococcus granulosus/isolation & purification
• Enzyme-Linked Immunosorbent Assay/methods
• Enzyme-Linked Immunosorbent Assay/standards
• Enzyme-Linked Immunosorbent Assay/trends
• Humans
• Immunoblotting/methods
• Immunoblotting/standards
• Immunoblotting/trends
• Immunoglobulin G/biosynthesis
• Immunoglobulin G/blood
• Immunologic Tests/trends
• Lymphokines/metabolism
• Sensitivity and Specificity
• Th1 Cells/immunology
• Th2 Cells/immunology
• Zoonoses

• Amino Acid Sequence
• Animals
• Antigens, Helminth/chemistry
• Antigens, Helminth/immunology
• Biopolymers
• Chromatography, Gel
• Circular Dichroism
• Echinococcus granulosus/immunology
• Models, Molecular
• Molecular Sequence Data
• Protein Conformation
• Protein Structure, Secondary
• Recombinant Proteins/chemistry
• Recombinant Proteins/immunology
• Sequence Homology, Amino Acid
• Spectrometry, Fluorescence
• Static Electricity

• Adaptation, Physiological/genetics
• Amino Acid Sequence
• Animals
• Antigens, Helminth/genetics
• Echinococcus/classification
• Echinococcus/genetics
• Echinococcus/immunology
• Evolution, Molecular
• Genes, Helminth
• Helminth Proteins/genetics
• Lipoproteins/genetics
• Molecular Sequence Data
• Multigene Family
• Selection, Genetic
• Species Specificity

• Animals
• Antigens, Helminth/immunology
• Antigens, Helminth/isolation & purification
• Echinococcosis/diagnosis
• Echinococcosis/immunology
• Echinococcosis/parasitology
• Echinococcus granulosus/immunology
• Echinococcus granulosus/isolation & purification
• Enzyme-Linked Immunosorbent Assay/methods
• Humans

• Animals
• Echinococcosis/diagnosis
• Echinococcosis/immunology
• Echinococcosis/parasitology
• Echinococcus granulosus/genetics
• Echinococcus granulosus/immunology
• Echinococcus granulosus/metabolism
• Echinococcus multilocularis/genetics
• Echinococcus multilocularis/immunology
• Echinococcus multilocularis/metabolism
• Helminth Proteins/chemistry
• Helminth Proteins/genetics
• Helminth Proteins/immunology
• Helminth Proteins/metabolism
• Humans
• Lipoproteins/chemistry
• Lipoproteins/genetics
• Lipoproteins/immunology
• Lipoproteins/metabolism
• Th2 Cells/immunology

• 1R01TW01565-01 FIC NIH HHS

• Animals
• Antibodies, Helminth/blood
• Antigens, Helminth/immunology
• Double-Blind Method
• Echinococcosis/diagnosis
• Echinococcosis/parasitology
• Echinococcus granulosus/immunology
• Enzyme-Linked Immunosorbent Assay/methods
• Enzyme-Linked Immunosorbent Assay/standards
• Humans
• Reproducibility of Results
• South America

• D43 TW005718 FIC NIH HHS
• AI051976 NIAID NIH HHS
• U01 AI035894 NIAID NIH HHS
• AI35894 NIAID NIH HHS
• P01 AI051976 NIAID NIH HHS
• TW05718 FIC NIH HHS

• Amino Acid Sequence
• Animals
• Base Sequence
• Camelus
• Cattle
• Echinococcus granulosus/genetics
• Echinococcus granulosus/immunology
• Gene Expression Profiling/methods
• Genome, Protozoan/genetics
• Helminth Proteins/chemistry
• Helminth Proteins/genetics
• Humans
• Lipoproteins/chemistry
• Lipoproteins/genetics
• Molecular Sequence Data
• Phylogeny
• Polymerase Chain Reaction/methods
• Polymorphism, Genetic/genetics
• Polymorphism, Single-Stranded Conformational
• Sequence Alignment
• Sequence Analysis, DNA
• Sequence Homology, Amino Acid
• Sequence Homology, Nucleic Acid
• Sheep
• Swine

• Animals
• Antibodies, Helminth/immunology
• Antibodies, Monoclonal/immunology
• Bacterial Proteins/chemistry
• Bacterial Proteins/isolation & purification
• Bacterial Proteins/metabolism
• Binding Sites
• Cestoda/chemistry
• Cestoda/metabolism
• Chromatography, Affinity
• Cyst Fluid/metabolism
• Escherichia coli/genetics
• Fatty Acids/chemistry
• Fatty Acids/metabolism
• Helminth Proteins/chemistry
• Helminth Proteins/immunology
• Helminth Proteins/metabolism
• Hydrophobic and Hydrophilic Interactions
• Kinetics
• Ligands
• Lipoproteins/chemistry
• Lipoproteins/immunology
• Lipoproteins/metabolism
• Recombinant Fusion Proteins/chemistry
• Recombinant Fusion Proteins/metabolism
• Spectrometry, Fluorescence

• Amino Acid Sequence
• Animals
• Antigens, Helminth/analysis
• Base Sequence
• Cloning, Molecular/methods
• DNA Primers
• DNA, Complementary/genetics
• DNA, Helminth/genetics
• Echinococcosis/diagnosis
• Echinococcus/growth & development
• Echinococcus/immunology
• Gene Library
• Gerbillinae
• Humans
• Larva/immunology
• Molecular Sequence Data
• Protein Subunits/analysis
• Reverse Transcriptase Polymerase Chain Reaction/methods
• Sequence Alignment
• Sequence Homology, Amino Acid
• Transcription, Genetic

• R01 TW001565 FIC NIH HHS
• 1 R01 TW01565-01 FIC NIH HHS

• echinococcus granulosus
• cystic hydatid disease
• elisa
• immunodiagnosis
• recombinant antigens

• Animals
• Antigens, Helminth/immunology
• Antigens, Helminth/isolation & purification
• Area Under Curve
• Case-Control Studies
• Echinococcosis/diagnosis
• Echinococcosis/immunology
• Echinococcus/immunology
• Epitopes/immunology
• Epitopes/isolation & purification
• Escherichia coli/immunology
• Humans
• Immunoglobulin G/analysis
• ROC Curve
• Recombinant Proteins/immunology
• Recombinant Proteins/isolation & purification
• Serologic Tests

• Allergy and Immunology
• Animals
• Echinococcosis/diagnosis
• Echinococcosis/genetics
• Echinococcosis/immunology
• Echinococcus/genetics
• Echinococcus/immunology
• Humans
• Immunity, Cellular
• Vaccination

• Wellcome Trust

• Amino Acid Sequence
• Animals
• Antibody Formation
• Base Sequence
• Blotting, Western
• Calcium-Binding Proteins/chemistry
• Calcium-Binding Proteins/genetics
• Calcium-Binding Proteins/immunology
• Calreticulin
• Cattle
• Cattle Diseases/immunology
• Cattle Diseases/parasitology
• Cloning, Molecular
• DNA, Complementary/chemistry
• Female
• Gene Expression Regulation
• Ixodidae/chemistry
• Ixodidae/classification
• Ixodidae/genetics
• Molecular Sequence Data
• Phylogeny
• Rabbits
• Reverse Transcriptase Polymerase Chain Reaction
• Ribonucleoproteins/chemistry
• Ribonucleoproteins/genetics
• Ribonucleoproteins/immunology
• Tick Infestations/immunology
• Tick Infestations/veterinary

• Amino Acid Sequence
• Animals
• Base Sequence
• Blotting, Southern
• DNA, Helminth/analysis
• Echinococcus/genetics
• Echinococcus/immunology
• Genes, Helminth
• Helminth Proteins
• Lipoproteins/genetics
• Molecular Sequence Data

• Animals
• Antibodies, Monoclonal
• Blotting, Southern
• Echinococcosis/diagnosis
• Echinococcus/genetics
• Echinococcus/immunology
• Echinococcus/isolation & purification
• Genetic Techniques
• Humans
• Immunologic Techniques
• Polymerase Chain Reaction
• Sensitivity and Specificity