Journal articles: 'Excretory/secretory (E/S) proteins'

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MAK, C. H., and R. C. KO. "DNA-binding activity in the excretory–secretory products ofTrichinella pseudospiralis(Nematoda: Trichinelloidea)." Parasitology 123, no. 3 (March 2001): 301–8. http://dx.doi.org/10.1017/s0031182001008459.

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A novel DNA-binding peptide ofMr∼30 kDa was documented for the first time in the excretory–secretory (E–S) products of the infective-stage larvae ofTrichinella pseudospiralis.Larvae recovered from muscles of infected mice were maintained for 48 h in DMEM medium. E–S products of worms extracted from the medium were analysed for DNA-binding activity by the electrophoretic mobility shift assay (EMSA). Multiple DNA-protein complexes were detected. A comparison of theMrof proteins in the complexes indicated that they could bind to the target DNA as a dimer, tetramer or multiples of tetramers. Site selection and competition analysis showed that the binding has a low specificity. A (G/C-rich)-gap-(G/T-rich)-DNA sequence pattern was extracted from a pool of degenerate PCR fragments binding to the E–S products. Results of immunoprecipitation and electrophoretic mobility supershift assay confirmed the authenticity of the DNA-binding protein as an E–S product.

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CERVI, L., G. ROSSI, and D. T. MASIH. "Potential role for excretory–secretory forms of glutathione-S-transferase (GST) in Fasciola hepatica." Parasitology 119, no. 6 (December 1999): 627–33. http://dx.doi.org/10.1017/s003118209900517x.

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The excretory–secretory antigen of Fasciola hepatica (ESA) is involved in the suppressive phenomena of cellular immune responses in rats. The ESA can depress the proliferative response of spleen mononuclear cells and inhibit nitric oxide (NO) production by peritoneal cells. In the present study we identified ESA proteins of ca 24 kDa, which shared significant sequence homology to glutathione-S-transferase (GST) obtained from homogenates of F. hepatica adults, other helminths and different mammals. When the dimeric form of these proteins ca 48 kDa was cultured with rat spleen cells, a significant decrease of proliferative response to Con A was detected, starting from 20 μg/ml of ESA protein (P<0·03). We also observed a significant inhibition of nitrite production by incubation with the dimeric form in normal peritoneal macrophages (P<0·04). These results indicated that the GST secreted by the parasite could be involved in evasion of the parasite from the host immune response.

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Cantacessi, Cinzia, Jason Mulvenna, Neil D. Young, Martin Kasny, Petr Horak, Ammar Aziz, Andreas Hofmann, Alex Loukas, and Robin B. Gasser. "A Deep Exploration of the Transcriptome and “Excretory/Secretory” Proteome of Adult Fascioloides magna." Molecular & Cellular Proteomics 11, no. 11 (August 16, 2012): 1340–53. http://dx.doi.org/10.1074/mcp.m112.019844.

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Parasitic liver flukes of the family Fasciolidae are responsible for major socioeconomic losses worldwide. However, at present, knowledge of the fundamental molecular biology of these organisms is scant. Here, we characterize, for the first time, the transcriptome and secreted proteome of the adult stage of the “giant liver fluke,” Fascioloides magna, using Illumina sequencing technology and one-dimensional SDS-PAGE and OFFGEL protein electrophoresis, respectively. A total of ∼54,000,000 reads were generated and assembled into ∼39,000 contiguous sequences (contigs); ∼20,000 peptides were predicted and classified based on homology searches, protein motifs, gene ontology, and biological pathway mapping. From the predicted proteome, 48.1% of proteins could be assigned to 384 biological pathway terms, including “spliceosome,” “RNA transport,” and “endocytosis.” Putative proteins involved in amino acid degradation were most abundant. Of the 835 secreted proteins predicted from the transcriptome of F. magna, 80 were identified in the excretory/secretory products from this parasite. Highly represented were antioxidant proteins, followed by peptidases (particularly cathepsins) and proteins involved in carbohydrate metabolism. The integration of transcriptomic and proteomic datasets generated herein sets the scene for future studies aimed at exploring the potential role(s) that molecules might play at the host–parasite interface and for establishing novel strategies for the treatment or control of parasitic fluke infections.

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Becerro-Recio, David, Javier González-Miguel, Alberto Ucero, Javier Sotillo, Álvaro Martínez-Moreno, José Pérez-Arévalo, Krystyna Cwiklinski, John P. Dalton, and Mar Siles-Lucas. "Recognition Pattern of the Fasciola hepatica Excretome/Secretome during the Course of an Experimental Infection in Sheep by 2D Immunoproteomics." Pathogens 10, no. 6 (June 9, 2021): 725. http://dx.doi.org/10.3390/pathogens10060725.

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Excretory/secretory products released by helminth parasites have been widely studied for their diagnostic utility, immunomodulatory properties, as well as for their use as vaccines. Due to their location at the host/parasite interface, the characterization of parasite secretions is important to unravel the molecular interactions governing the relationships between helminth parasites and their hosts. In this study, the excretory/secretory products from adult worms of the trematode Fasciola hepatica (FhES) were employed in a combination of two-dimensional electrophoresis, immunoblot and mass spectrometry, to analyze the immune response elicited in sheep during the course of an experimental infection. Ten different immunogenic proteins from FhES recognized by serum samples from infected sheep at 4, 8, and/or 12 weeks post-infection were identified. Among these, different isoforms of cathepsin L and B, peroxiredoxin, calmodulin, or glutathione S-transferase were recognized from the beginning to the end of the experimental infection, suggesting their potential role as immunomodulatory antigens. Furthermore, four FhES proteins (C2H2-type domain-containing protein, ferritin, superoxide dismutase, and globin-3) were identified for the first time as non-immunogenic proteins. These results may help to further understand host/parasite relationships in fasciolosis, and to identify potential diagnostic molecules and drug target candidates of F. hepatica.

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Kochanowski, Maciej, Joanna Dąbrowska, Mirosław Różycki, Jacek Sroka, Jacek Karamon, Aneta Bełcik, Weronika Korpysa-Dzirba, and Tomasz Cencek. "Proteomic Profiling and In Silico Characterization of the Secretome of Anisakis simplex Sensu Stricto L3 Larvae." Pathogens 11, no. 2 (February 14, 2022): 246. http://dx.doi.org/10.3390/pathogens11020246.

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Anisakis simplex sensu stricto (s.s.) L3 larvae are one of the major etiological factors of human anisakiasis, which is one of the most important foodborne parasitic diseases. Nevertheless, to date, Anisakis secretome proteins, with important functions in nematode pathogenicity and host-parasite interactions, have not been extensively explored. Therefore, the aim of this study was to identify and characterize the excretory-secretory (ES) proteins of A. simplex L3 larvae. ES proteins of A. simplex were subjected to liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis, and the identified proteins were then analyzed using bioinformatics tools. A total of 158 proteins were detected. Detailed bioinformatic characterization of ES proteins was performed, including Gene Ontology (GO) analysis, identification of enzymes, Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways analysis, protein family classification, secretory pathway prediction, and detection of essential proteins. Furthermore, of all detected ES proteins, 1 was identified as an allergen, which was Ani s 4, and 18 were potential allergens, most of which were homologs of nematode and arthropod allergens. Nine potential pathogenicity-related proteins were predicted, which were predominantly homologs of chaperones. In addition, predicted host-parasite interactions between the Anisakis ES proteins and both human and fish proteins were identified. In conclusion, this study represents the first global analysis of Anisakis ES proteins. The findings provide a better understanding of survival and invasion strategies of A. simplex L3 larvae.

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MAK, C. H., Y. Y. Y. CHUNG, and R. C. KO. "Single-stranded endonuclease activity in the excretory–secretory products of Trichinella spiralis and Trichinella pseudospiralis." Parasitology 120, no. 5 (May 2000): 527–33. http://dx.doi.org/10.1017/s0031182099005879.

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A novel acidic extracellular single-stranded endonuclease was demonstrated for the first time in the excretory–secretory (E–S) products of 2 species of Trichinella. Unlike the double-stranded endonuclease reported earlier, the single-stranded molecule is divalent cation independent and is detected in both T. spiralis and T. pseudospiralis E–S products. It hydrolysed single-stranded DNA and RNA at comparable rates. The single-stranded endonuclease was sensitive to inhibition by Zn2+ and to high concentrations of NaCl. Zymographic analysis indicated that it was encoded by at least 3 peptides of Mr ∼ 50–60 kDa. The rate of hydrolysis of single-stranded targets by the E–S products was substantially higher than that of the double-stranded molecule. Due to the differences in peptide profile, divalent cation dependence, and species-specific expression, the single and double-stranded endonucleases are likely to be encoded by different proteins and may have different functions.

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Siles-Lucas, M., and C. Cuesta-Bandera. "Echinococcus granulosus in Spain: strain differentiation by SDS-PAGE of somatic and excretory/secretory proteins." Journal of Helminthology 70, no. 3 (September 1996): 253–57. http://dx.doi.org/10.1017/s0022149x00015492.

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AbstractA comparison was made, by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), of excretory/secretory (ES) – crude and immunopurified (with the corresponding anti-host serum) hydatid fluids – and somatic (S) – protoscoleces – proteins, from several ovine, equine, swine, bovine and human Echinococcus granulosus Spanish isolates. Likewise, the host influence on parasitic ES protein expression was studied, comparing purified hydatid fluids from ovine and equine cysts obtained from natural hosts and in RNMI mice. Purified hydatid fluids patterns, under reducing conditions, yielded the most precise differentiation of Spanish strains of E. granulosus into three groups (ovine—bovine-human, equine and swine), the finding of a characteristic 82 kDa band in equine isolates, and an unusual arrangement of bands between 50 and 6 kDa in swine samples. In addition, differences were found amongst crude and purified hydatid fluids, especially in bovine and swine isolates. The total protein patterns of protoscoleces were most complex, and therefore could not be used for strain differentiation. Finally, the purified hydatid fluids from cysts developed in natural and experimental hosts showed similar protein patterns, suggesting the lack of host influence, under our experimental conditions, on the expression of parasitic ES proteins.

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Nagano, Isao, Zhiliang Wu, and Yuzo Takahashi. "Species-Specific Antibody Responses to the Recombinant 53-Kilodalton Excretory and Secretory Proteins in Mice Infected with Trichinella spp." Clinical and Vaccine Immunology 15, no. 3 (January 9, 2008): 468–73. http://dx.doi.org/10.1128/cvi.00467-07.

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ABSTRACT The 53-kDa proteins in larval excretory and secretory (E-S) products were expressed from five Trichinella species (T. spiralis, T. britovi, T. nativa, T. pseudospiralis, and T. papuae), using the Escherichia coli expression system, and the antibody responses to the 53-kDa recombinant proteins in mice infected with Trichinella spp. were analyzed by Western blotting. The 53-kDa protein is conserved among the five Trichinella species, with >60% similarity in amino acid sequences. The 53-kDa recombinant proteins of T. spiralis and T. pseudospiralis reacted to sera from mice infected with T. spiralis and T. pseudospiralis at 8 days postinfection (p.i.), respectively. An antibody against the 53-kDa recombinant protein of T. spiralis recognized the 53-kDa protein in the crude extracts from adult worms and 30-day p.i. muscle larvae and E-S products from muscle larvae of T. spiralis but did not recognize any proteins from T. pseudospiralis. The sera from the mice infected with T. spiralis strongly reacted with the 53-kDa recombinant protein of T. spiralis but did not react with the 53-kDa recombinant proteins of T. britovi, T. nativa, T. pseudospiralis, and T. papuae. Similarly, the sera from mice infected with T. britovi, T. nativa, T. pseudospiralis, or T. papuae strongly reacted with the 53-kDa recombinant proteins of T. britovi, T. nativa, T. pseudospiralis, or T. papuae, respectively. These results showed that the 53-kDa recombinant proteins provide early and species-specific antibody responses in mice infected with Trichinella spp.

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SPINNER, W. G., F. J. THOMPSON, D. C. EMERY, and M. E. VINEY. "Characterization of genes with a putative key role in the parasitic lifestyle of the nematode Strongyloides ratti." Parasitology 139, no. 10 (May 2, 2012): 1317–28. http://dx.doi.org/10.1017/s0031182012000637.

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SUMMARYParasitic nematodes are significant pathogens of humans and other animals. The molecular and genetic basis of animal parasitism is not yet fully understood. Strongyloides spp. are a genus of gastrointestinal nematodes of which species infect approximately 100–200 million people worldwide. S. ratti is a natural parasite of the rat, and a useful and amenable laboratory model. Previous EST and microarray analyses of the S. ratti life cycle have identified genes whose expression was specific, or biased, to the parasitic adult stage, suggesting that they may play a key role in parasitism in this species. Here we have further investigated the expression of these genes (by RT-PCR) throughout the S. ratti life-cycle. We produced recombinant proteins in vitro for a subset of these genes, which were used in Western blot analyses to investigate the distribution of the gene products among different stages of the S. ratti life cycle. We tested the efficacy of these recombinant proteins as anti-S. ratti vaccines. One of the proteins was detected in the excretory/secretory products of the parasitic stages.

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Grzelak, Sylwia, Anna Stachyra, Jerzy Stefaniak, Karolina Mrówka, Bożena Moskwa, and Justyna Bień-Kalinowska. "Immunoproteomic analysis of Trichinella spiralis and Trichinella britovi excretory-secretory muscle larvae proteins recognized by sera from humans infected with Trichinella." PLOS ONE 15, no. 11 (November 5, 2020): e0241918. http://dx.doi.org/10.1371/journal.pone.0241918.

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The present study compares the immunogenic patterns of muscle larvae excretory-secretory proteins (ML E-S) from T. spiralis and T. britovi recognized by Trichinella-infected human sera. Samples were analyzed using two-dimensional electrophoresis (2-DE) coupled with 2D-immunoblot and liquid chromatography-tandem mass spectrometry LC-MS/MS analysis, two ELISA procedures and a confirmatory 1D-immunoblot test. Sera were obtained from nine patients with a history of ingestion of raw or undercooked meat who presented typical clinical manifestations of trichinellosis and from eleven healthy people. Specific anti-Trichinella IgG antibodies were detected in all samples tested with the Home-ELISA kits, but in only four samples for the commercially-available kit. The 1D-immunoblot results indicated that all nine serum samples were positive for T. spiralis ML E-S antigens, expressed as the presence of specific bands. In contrast, eight of the serum samples with T. britovi E-S ML antigens were positive, with one serum sample taken from a patient at 33dpi (days post infection) being negative. To identify immunoreactive proteins that are specifically recognized by host antibodies, both species of ML E-S proteins were subjected to 2D-immunoblotting with human serum taken at 49 dpi. The sera recognized 22 protein spots for T. spiralis and 18 for T. britovi in 2D-immunoblot analysis. Their molecular weights (MW) ranged from 50 to 60 kDa. LC-MS/MS analysis identified both common and specifically-recognized immunoreactive proteins: transmembrane serine protease 9, serine protease, antigen targeted by protective antibodies and Actin-1 partial were shared for both Trichinella species; hypothetical protein T01_7775 and P49 antigen, partial those specific to T. spiralis; deoxyribonuclease-2-alpha and hypothetical protein T03_17187/T12_7360 were specific to T. britovi. Our results demonstrate the value of 2-DE and 2D-immunblot as versatile tools for pinpointing factors contributing to the parasite-host relationship by comparing the secretomes of different Trichinella species.

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Ditgen, Dana, Emmanuela M. Anandarajah, Jan Hansmann, Dominic Winter, Guido Schramm, Klaus D. Erttmann, Eva Liebau, and Norbert W. Brattig. "Multifunctional Thioredoxin-Like Protein from the Gastrointestinal Parasitic NematodesStrongyloides rattiandTrichuris suisAffects Mucosal Homeostasis." Journal of Parasitology Research 2016 (2016): 1–17. http://dx.doi.org/10.1155/2016/8421597.

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The cellular redox state is important for the regulation of multiple functions and is essential for the maintenance of cellular homeostasis and antioxidant defense. In the excretory/secretory (E/S) products ofStrongyloides rattiandTrichuris suissequences for thioredoxin (Trx) and Trx-like protein (Trx-lp) were identified. To characterize the antioxidant Trx-lp and its interaction with the parasite’s mucosal habitat,S. rattiandT. suisTrx-lps were cloned and recombinantly expressed. The primary antioxidative activity was assured by reduction of insulin and IgM. Further analysis applying anin vitromucosal 3D-cell culture model revealed that the secreted Trx-lps were able to bind to monocytic and intestinal epithelial cells and induce the time-dependent release of cytokines such as TNF-α, IL-22, and TSLP. In addition, the redox proteins also possessed chemotactic activity for monocytic THP-1 cells and fostered epithelial wound healing activity. These results confirm that the parasite-secreted Trx-lps are multifunctional proteins that can affect the host intestinal mucosa.

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Wainwright, Eleanor, and Rebecca K. Shears. "Trichuris WAP and CAP proteins: Potential whipworm vaccine candidates?" PLOS Neglected Tropical Diseases 16, no. 12 (December 22, 2022): e0010933. http://dx.doi.org/10.1371/journal.pntd.0010933.

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Trichuris trichiura and T. suis are gastrointestinal dwelling roundworms that infect humans and pigs, respectively. Heavy infections cause gastrointestinal symptoms and impaired growth and development. Vaccination has the potential to reduce the disease burden of whipworm infection; however, there are currently no commercially available vaccines against these parasites and very few against other gastrointestinal-dwelling nematodes of medical and agricultural importance. The naturally occurring mouse whipworm, T. muris, has been used for decades to model human trichuriasis, and the immunogenic potential of the excretory/secretory material (E/S, which can be collected following ex vivo culture of worms) has been studied in the context of vaccine candidate identification. Despite this, researchers are yet to progress an effective vaccine candidate to clinical trials. The T. muris, T. trichiura, and T. suis genomes each encode between 10 and 27 whey acidic protein (WAP) domain-containing proteins and 15 to 34 cysteine-rich secretory protein/antigen 5/pathogenesis related-1 (CAP) family members. WAP and CAP proteins have been postulated to play key roles in host–parasite interactions and may possess immunomodulatory functions. In addition, both protein families have been explored in the context of helminth vaccines. Here, we use phylogenetic and functional analysis to investigate the evolutionary relationship between WAP and CAP proteins encoded by T. muris, T. trichiura, and T. suis. We highlight several WAP and CAP proteins that warrant further study to understand their biological function and as possible vaccine candidates against T. trichiura and/or T. suis, based on the close evolutionary relationship with WAP or CAP proteins identified within T. muris E/S products.

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Nielsen, M. E., and K. Buchmann. "Glutathione-s-transferase is an important antigen in the eel nematode Anguillicola crassus." Journal of Helminthology 71, no. 4 (December 1997): 319–24. http://dx.doi.org/10.1017/s0022149x00016138.

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AbstractDifferent organs and secretions/excretions of the swimbladder parasite, Anguillicola crassus (Nematoda), were tested for the presence of antigens to the humoral immune response previously detected in the European eel, Anguilla anguilla. Proteins from different fractions of Anguillicola crassus were separated using SDS–PAGE (sodium-dodecyl-sulphate polyacrylamide-gel electrophoresis) under reducing conditions and electroblotted onto nitrocellulose membranes. Infected eels showed a specific antibody response to a 43 kDa antigen in the cuticle and towards two gonad antigens around 34 and 43 kDa. In protein released from the worms, two secretory/excretory antigens of approximately 28 kDa were found. The secretion/excretion rate of protein from the parasite to the surroundings was determined. Subsequently, an ELISA system was established applying these antigens as the first layer of coating. Furthermore, antigens from Anguillicola crassus were examined for the presence of glutathione-s-transferase (GST) using a specific antibody against GST. The antigens were found to be subunits of GST.

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Carson, Jack P., and Geoffrey N. Gobert. "Modulation of the Host Immune Response by Schistosome Egg-Secreted Proteins Is a Critical Avenue of Host–Parasite Communication." Pathogens 10, no. 7 (July 8, 2021): 863. http://dx.doi.org/10.3390/pathogens10070863.

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During a schistosome infection, the interactions that occur between the mammalian host and the parasite change rapidly once egg laying begins. Both juvenile and adult schistosomes adapt to indefinitely avoid the host immune system. In contrast, the survival of eggs relies on quickly traversing from the host. Following the commencement of egg laying, the host immune response undergoes a shift from a type 1 helper (Th1) inflammatory response to a type 2 helper (Th2) granulomatous response. This change is driven by immunomodulatory proteins within the egg excretory/secretory products (ESPs), which interact with host cells and alter their behaviour to promote egg translocation. However, in parallel, these ESPs also provoke the development of chronic schistosomiasis pathology. Recent studies using high-throughput proteomics have begun to characterise the components of schistosome egg ESPs, particularly those of Schistosoma mansoni, S. japonicum and S. haematobium. Future application of this knowledge may lead to the identification of proteins with novel immunomodulatory activity or pathological importance. However, efforts in this area are limited by a lack of in situ or in vivo functional characterisation of these proteins. This review will highlight the current knowledge of the content and demonstrated functions of schistosome egg ESPs.

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Hafidi, Nur Nasuha, Jaclyn Swan, Pierre Faou, Rohan Lowe, Harinda Rajapaksha, Callum Cairns, Michael Stear, and Travis Beddoe. "Teladorsagia Circumcincta Galectin-Mucosal Interactome in Sheep." Veterinary Sciences 8, no. 10 (October 4, 2021): 216. http://dx.doi.org/10.3390/vetsci8100216.

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Teladorsagia circumcincta is the most important gastrointestinal parasite in the livestock industry in temperate regions around the world, causing great economic losses. The infective third-stage larvae (L3) of Teladorsagia circumcincta secrete a large number of excretory-secretory (E/S) molecules, some of which are likely to play critical roles in modulating the host immune response. One of the most abundant E/S molecules is a protein termed Tci-gal-1, which has similarity to mammalian galectins. Galectins are a family of carbohydrate-binding molecules, with characteristic domain organisation and affinity for β-galactosids that mediate a variety of important cellular functions including inflammation and immune responses. To understand the role of Tci-gal-1 at the host–parasite interface, we used a proteomics pull-down approach to identify Tc-gal-1 interacting proteins from sheep abomasal scrapes and whole tissue. A total of 135 unique proteins were identified from whole abomasal tissue samples, while 89 proteins were isolated from abomasal scrape samples. Of these proteins, 63 were present in both samples. Many of the host proteins identified, such as trefoil factors and mucin-like proteins, play critical roles in the host response. The identification of Tci-gal-1 binding partners provides new insights on host–parasite interactions and could lead to the development of new control strategies.

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ISLAM, M. K., T. MIYOSHI, Y. YOKOMIZO, and N. TSUJI. "Molecular cloning and partial characterization of a nematode-specific 24 kDa protein fromAscaris suum." Parasitology 130, no. 1 (December 13, 2004): 131–39. http://dx.doi.org/10.1017/s0031182004006250.

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The cloning and molecular characterization of a cDNA encodingAscaris suum24 kDa antigen (As24) are described. The cDNA sequence consists of 853 bp with an open reading frame coding for a protein of 147 amino acids with an inferred signal peptide of 19 amino acids. The predicted molecular mass and pI were 16 kDa and 8·35 respectively. The endogenous protein in adultA. suumwas 24 kDa with the expected pI. A search of the public databases revealed over 50% homology with proteins from filarial parasites but not to other known proteins, suggesting that As24 is a nematode-specific protein. Immunohistochemical studies using polyclonal antibodies raised againstEscherichia coli-expressed recombinant As24 demonstrated that the endogenous As24 proteins were intensely localized in unembryonated eggs within the uterus, uterine and gut epithelium, muscle tissues and in the hypodermis of an adult femaleA. suum. Endogenous As24 was expressed throughoutA. suumdevelopment and was detected in the excretory/secretory products by immunoblot analysis. Importantly, a homologous protein(s) was detected inAscarisfrom human andToxocara canisfrom dog, suggesting that As24 is a nematode-specific protein.

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VERMEIRE, J. J., and T. P. YOSHINO. "Antioxidant gene expression and function in in vitro-developing Schistosoma mansoni mother sporocysts: possible role in self-protection." Parasitology 134, no. 10 (April 20, 2007): 1369–78. http://dx.doi.org/10.1017/s0031182007002697.

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SUMMARYThe ability of the larval forms of Schistosoma mansoni to invade and parasitize their molluscan host, Biomphalaria glabrata, is determined by a multitude of factors. In this study we sought to elucidate the possible mechanisms by which the invading larvae are able to counteract the potentially harmful oxidative environment presented by the host upon initial miracidial infection. This was attempted by examining the gene expression profile of parasite antioxidant enzymes of the linked glutathione-(GSH) thioredoxin (Trx) redox pathway during early intramolluscan larval development. Three such enzymes, the peroxiredoxins (Prx1, Prx2 and Prx3) were examined as to their activity and sites of expression within S. mansoni miracidia and in vitro-cultured mother sporocysts. Results of these studies demonstrated that the H2O2-reducing enzymes Prx1 and 2 are upregulated during early mother sporocyst development compared to miracidia. Immunolocalization studies further indicated that Prx1 and Prx2 proteins are expressed within the apical papillae of miracidia and tegumental syncytium of sporocysts, and are released with parasite excretory-secretory proteins (ESP) during in vitro larval transformation. Removal of Prx1 and Prx2 from larval ESP by immunoabsorption significantly reduced the ability of ESP to breakdown exogenous H2O2, thereby directly linking ESP Prx proteins with H2O2-scavenging activity. Moreover, exposure of live sporocysts to exogenous H2O2 stimulated an upregulation of Prx1 and 2 gene expression suggesting the involvement of H2O2–responsive elements in regulating larval Prx gene expression. These data provide evidence that Prx1 and Prx2 may function in the protection of S. mansoni sporocysts during the early stages of infection.

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Mekonnen, Gebeyaw G., Bemnet A. Tedla, Mark S. Pearson, Luke Becker, Matt Field, Abena S. Amoah, Govert van Dam, et al. "Characterisation of tetraspanins from Schistosoma haematobium and evaluation of their potential as novel diagnostic markers." PLOS Neglected Tropical Diseases 16, no. 1 (January 24, 2022): e0010151. http://dx.doi.org/10.1371/journal.pntd.0010151.

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Schistosoma haematobium is the leading cause of urogenital schistosomiasis and it is recognised as a class 1 carcinogen due to the robust association of infection with bladder cancer. In schistosomes, tetraspanins (TSPs) are abundantly present in different parasite proteomes and could be potential diagnostic candidates due to their accessibility to the host immune system. The large extracellular loops of six TSPs from the secretome (including the soluble excretory/secretory products, tegument and extracellular vesicles) of S. haematobium (Sh-TSP-2, Sh-TSP-4, Sh-TSP-5, Sh-TSP-6, Sh-TSP-18 and Sh-TSP-23) were expressed in a bacterial expression system and polyclonal antibodies were raised to the recombinant proteins to confirm the anatomical sites of expression within the parasite. Sh-TSP-2, and Sh-TSP-18 were identified on the tegument, whereas Sh-TSP-4, Sh-TSP-5, Sh-TSP-6 and Sh-TSP-23 were identified both on the tegument and internal tissues of adult parasites. The mRNAs encoding these TSPs were differentially expressed throughout all schistosome developmental stages tested. The potential diagnostic value of three of these Sh-TSPs was assessed using the urine of individuals (stratified by infection intensity) from an endemic area of Zimbabwe. The three Sh-TSPs were the targets of urine IgG responses in all cohorts, including individuals with very low levels of infection (those positive for circulating anodic antigen but negative for eggs by microscopy). This study provides new antigen candidates to immunologically diagnose S. haematobium infection, and the work presented here provides compelling evidence for the use of a biomarker signature to enhance the diagnostic capability of these tetraspanins.

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Ooba, C., Y. Nakamura, and N. Taira. "Larval somatic antigens effective in inducing an IgG response and protection against Strongyloides papillosus infection." Journal of Helminthology 70, no. 3 (September 1996): 231–35. http://dx.doi.org/10.1017/s0022149x00015467.

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AbstractA serum IgG response to Strongyloides papillosus infection was analysed in rabbits. IgG production was induced against 30–200 kDa larval somatic antigens and 21–160 kDa adult excretory/secretory (ES) antigens at 4 weeks postinfection. No immunoreactivity was detected between sera of infected animals and any proteins of larval ES and adult somatic antigens. Protection against larval challenge infection was investigated in rabbits immunized by primary infection and by intradermal inoculations of larval somatic and adult ES antigens. Primarily infected animals had 90% fewer or less worms from day 2 onwards after challenge, and lower faecal egg outputs after challenge, when compared with those in susceptible animals. Immunization with larval somatic antigens induced effective protection, showing 52.6–81.5% reductions in worm recovery from day 5 onwards after challenge, and lower faecal egg outputs after challenge. Systemic immunization with adult ES antigens failed to protect the animals against challenge. The possibility that resistance to S. papillosus reinfection is performed on the killing of migrating larvae in the early stages of infection is discussed. Systemic immune responses to larval somatic antigens might play an important role in the resistance.

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Aguayo, Vasti M., Edwin Colón, and Ana Espino. "Fasciola hepatica Glutathione S-tranferase suppresses the expression of inflammatory cytokines from murine macrophages in vitro and boosts the survival rate of C57Bl/6 mice against lethal doses of lipopolysaccharide." Journal of Immunology 198, no. 1_Supplement (May 1, 2017): 216.13. http://dx.doi.org/10.4049/jimmunol.198.supp.216.13.

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Abstract Fasciola hepatica, a world-wide parasitic helminth, is a well-known master of immunomodulation. The survival of this parasite in the mammalian host is highly dependent on its ability to avoid immune responses of the host for which the parasite employs excretory-secretory products (ESPs). Glutathione S-transferase (GST), one of the proteins in the repertoire of parasite ESPs, is an enzyme recognized for its anti-oxidant properties. GST has been studied as a vaccine candidate against animal fascioliasis, but its role in the immunomodulation has been poorly studied. In a previous study, we demonstrated that GST alone incites no activation of the nuclear factor NF-κB, yet it can suppress NF-κB when THP1-CD14 cells are exposed to GST 30 minutes before stimulation with TLR ligands. In this study, we investigate whether GST could exert a similar suppressive effect on NF-κB activation in THP1-CD14 cells when added several hours after TLR-ligand stimulation and if GST is able to suppress the expression of inflammatory cytokines in bone marrow derived macrophages (bmMØs) from naïve mice induced by LPS. Finally, we performed in vivo experiments to investigate whether one 200ug intraperitoneal (IP) injection with GST could increase the survival rate of C57BL/6 mice exposed to a lethal dose of LPS. Our results demonstrate that 10ug of GST on THP1-CD14 cells up to 3 hours after TLR-ligand stimulation significantly suppressed (p≤0.01) NF-kB activation. GST also suppressed the expression of TNF-α and IL-1β cytokines (p<0.05) in bmMØs in a dose dependent manner. Importantly, a single IP injection of GST boosted the survival rate of mice by 80% against lethal doses of LPS, suggesting GST is an anti-inflammatory molecule.

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Jiménez, Juan Carlos, Josette Fontaine, Jean-Marie Grzych, Eduardo Dei-Cas, and Monique Capron. "Systemic and Mucosal Responses to Oral Administration of Excretory and Secretory Antigens from Giardia intestinalis." Clinical Diagnostic Laboratory Immunology 11, no. 1 (January 2004): 152–60. http://dx.doi.org/10.1128/cdli.11.1.152-160.2004.

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ABSTRACT Giardia, a flagellated protozoan that infects the upper small intestine of its vertebrate host, is the most common parasitic protist responsible for diarrhea worldwide. Molecules released by the parasite, particularly excretory and secretory antigens, seemed to be associated with pathogenesis as well as with the expression of Giardia virulence. In the present work, we examined the effect of oral administration of Giardia intestinalis excretory and secretory antigens on systemic and local antibody response as well as on mucosal injuries in BALB/c mice. Significant titers of serum-specific immunoglobulin G1 (IgG1) and specific IgG2a were observed. Systemic and mucosal specific IgA antibodies were also recorded. A transient production of serum-specific IgE antibody and high total IgE levels were also detected, suggesting the presence in excretory and secretory proteins of factors promoting a specific IgE response. The sera of excretory and secretory antigen-treated mice recognized proteins of 50 and 58 kDa as well as electrophoretic bands of 15, 63, and 72 kDa that could support a proteinase activity. The in vitro exposure of G. intestinalis trophozoites to heat-inactivated sera from mice orally inoculated with excretory and secretory antigens induced a decrease of growth, revealing a complement-independent inhibitory activity of specific serum antibodies. Furthermore, histological evaluation performed on the small and large intestines revealed moderate to acute histological changes comparable to those observed in natural or experimental Giardia infection characterized by eosinophilic infiltration, hypercellularity, and enterocytic desquamation. The present results suggested that Giardia excretory and secretory antigens stimulate a preferential Th2 response, which is probably involved in the intestinal alterations associated with giardiasis.

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SAADATNIA, GEITA, ZEEHAIDA MOHAMED, FATEMEH GHAFFARIFAR, EMELIA OSMAN, ZOHREH KAZEMI MOGHADAM, and RAHMAH NOORDIN. "Toxoplasma gondii excretory secretory antigenic proteins of diagnostic potential." APMIS 120, no. 1 (October 18, 2011): 47–55. http://dx.doi.org/10.1111/j.1600-0463.2011.02810.x.

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Lagatie, Ole, Ann Verheyen, Bieke Van Dorst, Linda Batsa Debrah, Alex Debrah, and Lieven J. Stuyver. "Linear epitopes in Onchocerca volvulus vaccine candidate proteins and excretory-secretory proteins." Parasite Immunology 40, no. 11 (October 8, 2018): e12587. http://dx.doi.org/10.1111/pim.12587.

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Ma, Zhenrong, Alaa Majeed Mutashar Alhameed, Atipatsa Chiwanda Kaminga, Bin Lu, Xuanwu Li, Jie Zhang, and Xiang Wu. "Bioinformatics of excretory/secretory proteins of Toxoplasma gondii strain ME49." Microbial Pathogenesis 140 (March 2020): 103951. http://dx.doi.org/10.1016/j.micpath.2019.103951.

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Sperotto, Rita Leal, Frederico Schmitt Kremer, Maria Elisabeth Aires Berne, Luciana F. Costa de Avila, Luciano da Silva Pinto, Karina Mariante Monteiro, Karin Silva Caumo, Henrique Bunselmeyer Ferreira, Natália Berne, and Sibele Borsuk. "Proteomic analysis of Toxocara canis excretory and secretory (TES) proteins." Molecular and Biochemical Parasitology 211 (January 2017): 39–47. http://dx.doi.org/10.1016/j.molbiopara.2016.09.002.

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Vervelde, L., M. A. W. van Leeuwen, M. Kruidenier, F. N. J. Kooyman, J. F. Huntley, I. van Die, and A. W. C. A. Cornelissen. "Protection studies with recombinant excretory/secretory proteins of Haemonchus contortus." Parasite Immunology 24, no. 4 (April 2002): 189–201. http://dx.doi.org/10.1046/j.1365-3024.2002.00454.x.

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Barthélémy, Roxane-Marie, Corinne Cuoc, Xavier Caubit, and Michel Brunet. "The shell glands in some calanoid copepods (Crustacea)." Canadian Journal of Zoology 79, no. 8 (August 1, 2001): 1490–502. http://dx.doi.org/10.1139/z01-104.

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This study represents the first structural, ultrastructural, and biochemical investigation of the shell glands in calanoid copepods. These glands, located inside the points of the last prosomal segment, constitute voluminous syncytial secretory units, each of which extends into an excretory canalicule with a cellular or syncytial wall. The canalicules merge into two collector canals, or shell ducts, that rejoin the oviducts and then open into the egg-laying ducts. Each secretory unit synthesizes heterogeneous granules containing both light and predominantly dense material. Exocytosis of these mature secretory granules occurs in an apical excretory chamber. In freshwater species, the modifications observed during the secretory cycle emphasize a gradual discharge from the secretory units in the hours following laying. Cytochemical and biochemical studies of the secretions reveal the presence of N-acetylglucosamine, galactose, and N-acetylgalactosamine glycoconjugated proteins.

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Cho, S. Y., Y. B. Chung, and Y. Kong. "Component proteins and protease activities in excretory-secretory product of sparganum." Korean Journal of Parasitology 30, no. 3 (1992): 227. http://dx.doi.org/10.3347/kjp.1992.30.3.227.

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Lee, Won-Kyu, Hye-Jin Ahn, Je-Hyun Baek, Chong-Heon Lee, Yeon Gyu Yu, and Ho-Woo Nam. "Comprehensive Proteome Analysis of the Excretory/Secretory Proteins of Toxoplasma gondii." Bulletin of the Korean Chemical Society 35, no. 10 (October 20, 2014): 3071–76. http://dx.doi.org/10.5012/bkcs.2014.35.10.3071.

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Reamtong, Onrapak, Nattapon Simanon, Tipparat Thiangtrongjit, Yanin Limpanont, Phiraphol Chusongsang, Yupa Chusongsang, Songtham Anuntakarun, Sunchai Payungporn, Orawan Phuphisut, and Poom Adisakwattana. "Proteomic analysis of adult Schistosoma mekongi somatic and excretory-secretory proteins." Acta Tropica 202 (February 2020): 105247. http://dx.doi.org/10.1016/j.actatropica.2019.105247.

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Morassutti, Alessandra L., Keith Levert, Paulo M. Pinto, Alexandre J. da Silva, Patricia Wilkins, and Carlos Graeff-Teixeira. "Characterization of Angiostrongylus cantonensis excretory–secretory proteins as potential diagnostic targets." Experimental Parasitology 130, no. 1 (January 2012): 26–31. http://dx.doi.org/10.1016/j.exppara.2011.10.003.

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Kocher, D. K., S. P. Ahuja, and M. L. Sood. "Haemonchus contortus: Characterization and Purification of Excretory/Secretory Protease(s)." Journal of Veterinary Medicine, Series B 45, no. 1-10 (January 12, 1998): 567–72. http://dx.doi.org/10.1111/j.1439-0450.1998.tb00828.x.

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Yousef, Hesham A., Amira Afify, Afaf Abdel Meguid, and Hany M. Hassan. "Profiling of proteins and proteases in the products of the salivary gland, digestive tract and excretions from larvae of the camel nasal botfly, Cephalopina titillator (Clark)." Zeitschrift für Naturforschung C 70, no. 7-8 (July 1, 2015): 197–203. http://dx.doi.org/10.1515/znc-2014-4206.

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Abstract Proteins and proteolytic activities in the contents of the salivary gland (SGc), digestive tract (DTc) and excretory-secretory products (ESP) from larvae of the camel nasal botfly Cephalopina titillator were separated electrophoretically, and characterized. The protein profiles of the different samples were qualitatively quite similar in the larval stages L2 and L3. Zymogram analysis of proteases in the samples indicated that the digestive tract contained a greater variety of proteases than the salivary gland or the excretory-secretory products. They are mainly serine proteases. Proteases of ESP and DTc (especially of 3rd instar) contain trypsin- and chymotrypsin-like serine proteases, while the serine proteases of SGc are not of the trypsin- or chemotrypsin-type.

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Wang, Li, Zhong Quan Wang, Dan Dan Hu, and Jing Cui. "Proteomic Analysis ofTrichinella spiralisMuscle Larval Excretory-Secretory Proteins Recognized by Early Infection Sera." BioMed Research International 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/139745.

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Although the excretory-secretory (ES) proteins ofTrichinella spiralismuscle larvae are the most commonly used diagnostic antigens for trichinellosis, their main disadvantage is the false negative results during the early stage of infection and cross-reaction of their main components (43, 45, 49, and 53 kDa) with sera of patients with other helminthiasis. The aim of this study was to identify early specific diagnostic antigens inT. spiralisES proteins with 30–40 kDa. The ES proteins were analyzed by two-dimensional electrophoresis (2-DE), and a total of approximately 150 proteins spots were detected with isoelectric point (pI) varying from 4 to 7 and molecular weight from 14 to 66 kDa. When probed with sera from infected mice at 18 days postinfection, ten protein spots with molecular weight of 30–40 kDa were recognized and identified by MALDI-TOF/TOF-MS. All of ten spots were successfully identified and characterized to correlate with five different proteins, including two potential serine proteases, one antigen targeted by protective antibodies, one deoxyribonuclease (DNase) II, and one conserved hypothetical protein. These proteins might be the early specific diagnostic antigens for trichinellosis.

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Frank, Glenn R., and Robert B. Grieve. "Purification and characterization of three larval excretory-secretory proteins of Dirofilaria immitis." Molecular and Biochemical Parasitology 75, no. 2 (January 1996): 221–29. http://dx.doi.org/10.1016/0166-6851(95)02533-2.

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Vervelde, L., F. N. J. Kooyman, M. A. W. Van Leeuwen, H. D. F. H. Schallig, A. Mackellar, J. F. Huntley, and A. W. C. A. Cornelissen. "Age-related protective immunity after vaccination with Haemonchus contortus excretory/secretory proteins." Parasite Immunology 23, no. 8 (August 2001): 419–26. http://dx.doi.org/10.1046/j.1365-3024.2001.00391.x.

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37

Kim, Jong-Hyun, Ae-Hee Yang, Hae-Jin Sohn, Daesik Kim, Kyoung-Ju Song, and Ho-Joon Shin. "Immunodominant antigens in Naegleria fowleri excretory–secretory proteins were potential pathogenic factors." Parasitology Research 105, no. 6 (September 16, 2009): 1675–81. http://dx.doi.org/10.1007/s00436-009-1610-y.

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38

Nuamtanong, Supaporn, Onrapak Reamtong, Orawan Phuphisut, Palang Chotsiri, Preeyarat Malaithong, Paron Dekumyoy, and Poom Adisakwattana. "Transcriptome and excretory–secretory proteome of infective-stage larvae of the nematode Gnathostoma spinigerum reveal potential immunodiagnostic targets for development." Parasite 26 (2019): 34. http://dx.doi.org/10.1051/parasite/2019033.

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Background: Gnathostoma spinigerum is a harmful parasitic nematode that causes severe morbidity and mortality in humans and animals. Effective drugs and vaccines and reliable diagnostic methods are needed to prevent and control the associated diseases; however, the lack of genome, transcriptome, and proteome databases remains a major limitation. In this study, transcriptomic and secretomic analyses of advanced third-stage larvae of G. spinigerum (aL3Gs) were performed using next-generation sequencing, bioinformatics, and proteomics. Results: An analysis that incorporated transcriptome and bioinformatics data to predict excretory–secretory proteins (ESPs) classified 171 and 292 proteins into classical and non-classical secretory groups, respectively. Proteins with proteolytic (metalloprotease), cell signaling regulatory (i.e., kinases and phosphatase), and metabolic regulatory function (i.e., glucose and lipid metabolism) were significantly upregulated in the transcriptome and secretome. A two-dimensional (2D) immunomic analysis of aL3Gs-ESPs with G. spinigerum-infected human sera and related helminthiases suggested that the serine protease inhibitor (serpin) was a promising antigenic target for the further development of gnathostomiasis immunodiagnostic methods. Conclusions: The transcriptome and excretory–secretory proteome of aL3Gs can facilitate an understanding of the basic molecular biology of the parasite and identifying multiple associated factors, possibly promoting the discovery of novel drugs and vaccines. The 2D-immunomic analysis identified serpin, a protein secreted from aL3Gs, as an interesting candidate for immunodiagnosis that warrants immediate evaluation and validation.

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Caña-Bozada, Víctor, Martha Chapa-López, Rubén D. Díaz-Martín, Alejandra García-Gasca, José Ángel Huerta-Ocampo, Guillermo de Anda-Jáuregui, and F. Neptalí Morales-Serna. "In silico identification of excretory/secretory proteins and drug targets in monogenean parasites." Infection, Genetics and Evolution 93 (September 2021): 104931. http://dx.doi.org/10.1016/j.meegid.2021.104931.

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Son, Eui-Sun, and Ho-Woo Nam. "Detection and characterization of excretory/secretory proteins from Toxoplasma gondii by monoclonal antibodies." Korean Journal of Parasitology 39, no. 1 (2001): 49. http://dx.doi.org/10.3347/kjp.2001.39.1.49.

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Lodes, Michael J., and Timothy P. Yoshino. "Characterization of Excretory-Secretory Proteins Synthesized In vitro by Schistosoma mansoni Primary Sporocysts." Journal of Parasitology 75, no. 6 (December 1989): 853. http://dx.doi.org/10.2307/3282863.

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42

Lee, Jinyoung, Jung-Mi Kang, Tae Im Kim, Jong-Hyun Kim, Hae-Jin Sohn, Byoung-Kuk Na, and Ho-Joon Shin. "Excretory and Secretory Proteins ofNaegleria fowleriInduce Inflammatory Responses in BV-2 Microglial Cells." Journal of Eukaryotic Microbiology 64, no. 2 (August 23, 2016): 183–92. http://dx.doi.org/10.1111/jeu.12350.

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GIACOMIN, P. R., M. CAVA, D. J. TUMES, A. D. GAULD, D. R. IDDAWELA, S. R. MCCOLL, J. C. PARSONS, D. L. GORDON, and L. A. DENT. "Toxocara canislarval excretory/secretory proteins impair eosinophil-dependent resistance of mice toNippostrongylus brasiliensis." Parasite Immunology 30, no. 8 (August 2008): 435–45. http://dx.doi.org/10.1111/j.1365-3024.2008.01040.x.

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Liao, Qi, Xiongying Yuan, Hui Xiao, Changning Liu, Zhiyue Lv, Yi Zhao, and Zhongdao Wu. "Identifying Schistosoma japonicum Excretory/Secretory Proteins and Their Interactions with Host Immune System." PLoS ONE 6, no. 8 (August 24, 2011): e23786. http://dx.doi.org/10.1371/journal.pone.0023786.

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45

Denkers, E. Y., D. L. Wassom, C. J. Krco, and C. E. Hayes. "The mouse antibody response to Trichinella spiralis defines a single, immunodominant epitope shared by multiple antigens." Journal of Immunology 144, no. 8 (April 15, 1990): 3152–59. http://dx.doi.org/10.4049/jimmunol.144.8.3152.

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Abstract Immunoblot analysis was used to characterize the Trichinella spiralis L1 larval Ag recognized by antisera from T. spiralis-infected AKR/J mice. Antisera were analyzed for reactivity with crude worm extract, excretory/secretory proteins and cuticle proteins from L1 larvae. The response was biphasic; antibodies against one set of Ag were detected 13 days after infection (group I Ag), and antibodies against a different set of Ag were detected 35 days after infection (group II Ag). Excretory/secretory and cuticle proteins were recognized only by antibodies produced late in infection. The predominant isotype in day 42 antiserum was IgG1, and 80% of these IgG1 antibodies reacted with a stage-specific determinant shared by virtually all group II Ag. A mAb reactive with the shared determinant was used to purify the group II Ag from L1 larval extract. Such affinity-purified Ag were protective when used to immunize mice against subsequent infection, and T cells from infected mice proliferated when cultured with these Ag in vitro. Other mouse strains also made a strong serum antibody response to the group II Ag. We hypothesize that immune responses to the shared epitope play an important role in determining the outcome of the host-parasite interaction during infection.

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ELSE, K. J., D. WAKELIN, D. L. WASSOM, and K. M. HAUDA. "MHC-restricted antibody responses to Trichuris muris excretory/secretory (E/S) antigen." Parasite Immunology 12, no. 4-5 (September 1990): 509–27. http://dx.doi.org/10.1111/j.1365-3024.1990.tb00985.x.

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47

Matthews, R. A., and B. F. Matthews. "Cryptocotyle lingua in mullet, Chelon labrosus; significance of metacercarial excretory proteins in the stimulation of the immune response." Journal of Helminthology 67, no. 1 (March 1993): 1–9. http://dx.doi.org/10.1017/s0022149x00012785.

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Abstract‘O’ group mullet, Chelon labrosus. were experimentally infected with Cryptocotyle lingua (Heterophyidae) by tail dip in a suspension of cercariae. Metacercariae were excised after 1 and 24 hours and prepared for TEM and post-embedding immunogold labelling. Antisera to cercariae of C. lingua were raised in adult mullet by natural infection via the skin and by intra-peritoneal injection of sonicate. The membrane-bound vesicles within the syncytial lining of the metacercarial excretory vesicle were found to be intensely antigenic with both antisera: the epidermal secretory bodies type 5 within the cystogenousglands gave a positive response. Penetration gland contents were not found to be antigenic with either antiserum. Discharge of the membrane-bound vesicles coinciding with both the reorganization of the lining of the metacercarial excretory vesicle and with cyst wall formation appears to be of significance in the initiation of the host immune response. That the term ‘excretory vesicle’ in Digenea may be a misnomer is discussed in the light of current information regarding the wide range of functions attributed to this structure.

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Schallig, H. D. F. H., M. A. W. van Leeuwen, and W. M. L. Hendrikx. "Immune responses of Texel sheep to excretory/secretory products of adult Haemonchus contortus." Parasitology 108, no. 3 (April 1994): 351–57. http://dx.doi.org/10.1017/s0031182000076198.

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SUMMARYThe excretory/secretory (E/S) products of adult Haemonchus contortus comprise of at least 15 polypeptides with molecular weights ranging from 10 to > 100 kDa. These E/S products induce an immune response in infected Texel sheep, as demonstrated by specific IgGI levels and a significant lymphocyte proliferation index. Moreover, immunoblotting analysis revealed that sera of primary H. contortus-infected sheep specifically recognize a 24 kDa E/S product. In addition, sera of challenged sheep react strongly with a 15 kDa E/S product. The other E/S products of H. contortus showed immunoreactivity with serum samples of Haemonchus-infected sheep as well as with samples of sheep harbouring other trichostrongylid infections. These cross-reacting epitopes are the main cause of the lack of specificity of an E/S material- based ELISA. This ELISA can differentiate Haemonchus infections from Nematodirus battus infections, but not from Ostertagia circumcincta or Trichostrongylus colubriformis infections.

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AL-ATTAR, TAHANY, WAFAA EL-KERSH, GEHAN SADEK, NANCY HARBA, SALWA OSHEIBA, and REHAM BRAKAT. "A STUDY OF IMMUNOTHERAPEUTIC EFFICACY OF TRICHINELLA SPIRALIS EXCRETORY-SECRETORY PROTEINS IN MURINE TRICHINELLOSIS." Journal of the Egyptian Society of Parasitology 50, no. 2 (August 1, 2020): 281–92. http://dx.doi.org/10.21608/jesp.2020.113049.

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Singh, Nisha, Sangram Singh, and Arun Kumar Rawat. "In Silico Identification of L. Donovani Excretory-secretory Proteins Interacting with Human SLC11 A1." Journal of scientific research 64, no. 01 (2020): 134–39. http://dx.doi.org/10.37398/jsr.2020.640119.

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Journal articles on the topic 'Excretory/secretory (E/S) proteins'

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