Molecular characterization and expression analysis of annexin B3 and B38 as secretory proteins in Echinococcus granulosus.

Tytuł:: Molecular characterization and expression analysis of annexin B3 and B38 as secretory proteins in Echinococcus granulosus.
Autorzy:: Song H; Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
He X; Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Du X; Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Hua R; Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Xu J; Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
He R; Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Xie Y; Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Gu X; Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Peng X; Department of Chemistry, College of Life and Basic Science, Sichuan Agricultural University, Wenjiang, 611130, China.
Yang G; Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China. .
Źródło:: Parasites & vectors [Parasit Vectors] 2021 Feb 08; Vol. 14 (1), pp. 103. Date of Electronic Publication: 2021 Feb 08.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Original Publication: London : BioMed Central
MeSH Terms:: Annexins/*classification
Annexins/*genetics
Echinococcus granulosus/*genetics
Amino Acid Sequence ; Animals ; Annexins/chemistry ; Cloning, Molecular ; Computational Biology ; Dogs ; Echinococcosis/parasitology ; Female ; Male ; Protein Binding ; Rabbits ; Sequence Alignment ; Sheep
References:: Deplazes P, Rinaldi L, Rojas CAA, Torgerson PR, Jenkins EJ. Global distribution of alveolar and cystic echinococcosis. Adv Parasit. 2017;95:315–493. (PMID: 10.1016/bs.apar.2016.11.001)
Othieno E, Ocaido M, Mupere E, Omadang L, Oba P, Okwi AL. Knowledge, attitude, and beliefs of communities and health staff about Echinococcus granulosus infection in selected pastoral and agropastoral regions of Uganda. J Parasitol Res. 2018;2018:1–10. (PMID: 10.1155/2018/5819545)
Rialch A, Raina OK, Tigga MN, Anandanarayanan A, Verma MR. Evaluation of Echinococcus granulosus recombinant EgAgB8/1, EgAgB8/2 and EPC1 antigens in the diagnosis of cystic echinococcosis in buffaloes. Vet Parasitol. 2018;252:29–34. (PMID: 2955914710.1016/j.vetpar.2018.01.020)
World Health Organization. Investing to overcome the global impact of neglected tropical diseases: third WHO report on neglected tropical diseases 2015, vol. 3. Geneva: World Health Organization; 2015.
Wen H, Vuitton L, Tuxun T, Li J, Vuitton DA, Zhang W, et al. Echinococcosis: advances in the 21st century. Clin Microbiol Rev. 2019;32:1–39. (PMID: 10.1128/CMR.00075-18)
Virginio VG, Monteiro KM, Drumond F, de Carvalho MO, Vargas DM, Zaha A, et al. Excretory/secretory products from in vitro-cultured Echinococcus granulosus protoscoleces. Mol Biochem Parasitol. 2012;183:15–22. (PMID: 2226109010.1016/j.molbiopara.2012.01.001)
Zeghir-Bouteldja R, Polomé A, Bousbata S, Touil-Boukoffa C. Comparative proteome profiling of hydatid fluid from Algerian patients reveals cyst location-related variation in Echinococcus granulosus. Acta Trop. 2017;171:199–206. (PMID: 2841204810.1016/j.actatropica.2017.03.034)
Siles-Lucas M, Sánchez-Ovejero C, González-Sánchez M, González E, Falcón-Pérez JM, Boufana B, et al. Isolation and characterization of exosomes derived from fertile sheep hydatid cysts. Vet Parasitol. 2017;236:22–33. (PMID: 2828876010.1016/j.vetpar.2017.01.022)
Schloer S, Pajonczyk D, Rescher U. Annexins in translational research: hidden treasures to be found. Int J Mol Sci. 2018;19:1781. (PMID: 603222410.3390/ijms190617816032224)
Gerke V, Creutz CE, Moss SE. Annexins: linking Ca method. Methods. 2001;25:402–8. (PMID: 10.1006/meth.2001.1262)
Zhang Y, Wang K, Guo Y, Lu Y, Yan H, Song Y, et al. Annexin B1 from Taenia solium metacestodes is a newly characterized member of the annexin family. Biol Chem. 2007;388:601–10. (PMID: 1755290710.1515/BC.2007.071)
Choi S, Kwon S, Lee E, Kim K. Molecular cloning, functional characterization and localization of an annexin from a fish gill fluke Microcotyle sebastis (Platyhelminthes: Monogenea). Mol Biochem Parasitol. 2009;163:48–53. (PMID: 1895508910.1016/j.molbiopara.2008.09.009)
Zheng H, Zhang W, Zhang L, Zhang Z, Li J, Lu G, et al. The genome of the hydatid tapeworm Echinococcus granulosus. Nat Genet. 2013;45:1168–75. (PMID: 2401364010.1038/ng.2757)
Cantacessi C, Seddon JM, Miller TL, Leow CY, Thomas L, Mason L, et al. A genome-wide analysis of annexins from parasitic organisms and their vectors. Sci Rep. 2013;3:1–8. (PMID: 10.1038/srep02893)
Guo C, Xie Y, Liu Y, Wang N, Zhan J, Zhou X, et al. Molecular characterization of annexin B2, B3 and B12 in Taenia multiceps. Genes. 2018;9:559. (PMID: 626762310.3390/genes91105596267623)
Morgan R, Martin-Almedina S, Iglesias J, Gonzalez-Florez M, Fernandez M. Evolutionary perspective on annexin calcium-binding domains. BBA-Mol Cell Res. 2004;1742:133–40.
He L, Ren M, Chen X, Wang X, Li S, Lin J, et al. Biochemical and immunological characterization of annexin B30 from Clonorchis sinensis excretory/secretory products. Parasitol Res. 2014;113:2743–55. (PMID: 2486101110.1007/s00436-014-3935-4)
Simpson AJG, Smithers SR. Schistosomes: surface, egg and circulating antigens. Curr Top Microbiol Immunol. 1985;120:205–39. (PMID: 3933917)
Dalton JP, Skelly PJ, Halton DW. Role of the tegument and gut in nutrient uptake by parasitic platyhelminths. Can J Zool. 2004;82:211–32. (PMID: 10.1139/z03-213)
Galindo M, Schadebrodt G, Galanti N. Echinococcus granulosus: cellular territories and morphological regions in mature protoscoleces. Exp Parasitol. 2008;119:524–33. (PMID: 1850805010.1016/j.exppara.2008.04.013)
Gerke V, Moss SE. Annexins: from structure to function. Physiol Rev. 2002;82:331–71. (PMID: 1191709210.1152/physrev.00030.2001)
Vergnolle N, Pages P, Guimbaud R, Chaussade S, Bueno L, Escourrou J, et al. Annexin 1 is secreted in situ during ulcerative colitis in humans. Inflamm Bowel Dis. 2004;10:584–92. (PMID: 1547251910.1097/00054725-200409000-00013)
Donnelly SR, Moss SE. Annexins in the secretory pathway. Cell Mol Life Sci. 1997;53:533–8. (PMID: 923093210.1007/s000180050068)
Samia Y, Ajantha S, Egle S, Virginia C, Flower RJ, Bernhard R. Anti-allergic cromones inhibit histamine and eicosanoid release from activated human and murine mast cells by releasing annexin A1. PLoS ONE. 2013;8:e58963. (PMID: 10.1371/journal.pone.0058963)
Aziz A, Zhang W, Li J, Loukas A, McManus DP, Mulvenna J. Proteomic characterisation of Echinococcus granulosus hydatid cyst fluid from sheep, cattle and humans. J Proteomics. 2011;74:1560–72. (PMID: 2136250510.1016/j.jprot.2011.02.021)
Zhou X, Wang W, Cui F, Shi C, Ma Y, Yu Y, et al. Extracellular vesicles derived from Echinococcus granulosus hydatid cyst fluid from patients: isolation, characterization and evaluation of immunomodulatory functions on T cells. Int J Parasitol. 2019;49:1029–37. (PMID: 3173433910.1016/j.ijpara.2019.08.003)
Siracusano A, Delunardo F, Teggi A, Ortona E. Cystic echinococcosis: aspects of immune response, immunopathogenesis and immune evasion from the human host. Endocr Metab Immune Disorders Drug Targets. 2012;12:16–23. (PMID: 10.2174/187153012799279117)
Zheng Y. Strategies of Echinococcus species responses to immune attacks: implications for therapeutic tool development. Int Immunopharmacol. 2013;17:495–501. (PMID: 2397365110.1016/j.intimp.2013.07.022)
Grant Information:: No. 31672547 the National Natural Science Foundation of China; No. 2020YFN0030 the Key TechnologyR&D Program of Sichuan Province, China
Contributed Indexing:: Keywords: Annexin; Calcium ion; Echinococcus granulosus; Immunofluorescence localization; Secretory protein; Western blotting
Substance Nomenclature:: 0 (Annexins)
Entry Date(s):: Date Created: 20210209 Date Completed: 20210819 Latest Revision: 20211029
Update Code:: 20240104
PubMed Central ID:: PMC7869467
DOI:: 10.1186/s13071-021-04596-7
PMID:: 33557917
: Czasopismo naukowe

Pełny tekst

Background: Cystic echinococcosis is a parasitic zoonotic disease, which poses a threat to public health and animal husbandry, and causes significant economic losses. Annexins are a family of phospholipid-binding proteins with calcium ion-binding activity, which have many functions.
Methods: Two annexin protein family genes [Echinococcus granulosus annexin B3 (EgAnxB3) and EgAnxB38] were cloned and molecularly characterized using bioinformatic analysis. The immunoreactivity of recombinant EgAnxB3 (rEgAnxB3) and rEgAnxB38 was investigated using western blotting. The distribution of EgAnxB3 and EgAnxB38 in protoscoleces (PSCs), the germinal layer, 18-day strobilated worms and 45-day adult worms was analyzed by immunofluorescence localization, and their secretory characteristics were analyzed preliminarily; in addition, quantitative real-time reverse transcription polymerase chain reaction was used to analyze their transcript levels in PSCs and 28-day strobilated worms stages. The phospholipid-binding activities of rEgAnxB3 and rEgAnxB38 were also analyzed.
Results: EgAnxB3 and EgAnxB38 are conserved and contain calcium-binding sites. Both rEgAnxB3 and rEgAnxB38 could be specifically recognized by the serum samples from E. granulosus-infected sheep, indicating that they had strong immunoreactivity. EgAnxB3 and EgAnxB38 were distributed in all stages of E. granulosus, and their transcript levels were high in the 28-day strobilated worms. They were found in liver tissues near the cysts. In addition, rEgAnxB3 has Ca 2+ -dependent phospholipid-binding properties.
Conclusions: EgAnxB3 and EgAnxB38 contain calcium-binding sites, and rEgAnxB3 has Ca 2+ -dependent phospholipid-binding properties. EgAnxB3 and EgAnxB38 were transcribed in PSCs and 28-day strobilated worms. They were expressed in all stages of E. granulosus, and distributed in the liver tissues near the hydatid cyst, indicating that they are secreted proteins that play a crucial role in the development of E. granulosus.

Zaloguj się, aby uzyskać dostęp do pełnego tekstu.

Informacja