In silico characterization of acid phosphatase in the functional genome of the amazon prawn

Autores

  • Janieli do Socorro Amorim da Luz Sousa
  • Gabriel Monteiro de Lima
  • Bruna Ramalho Maciel
  • Ítalo Lutz
  • Carlos Murilo Tenório Maciel
  • Cristiana Ramalho Maciel

DOI:

https://doi.org/10.34188/bjaerv7n2-093

Palavras-chave:

defense mechanism, oxidative stress response, Macrobrachium amazonicum, environmental quality

Resumo

The acid phosphatase (ACP) enzyme is responsible for the hydrolysis of phosphate monoesters under acidic conditions, being widely found in microorganisms, animals and plants. In crustaceans, the ACP plays a key role in the defense mechanism of distinct species. Furthermore, the expression of ACP is sensitive to pollution, being particularly related to the stress response by the exposure to heavy metals and organophosphate pesticides. However, most studies in crustaceans refer to the biochemical properties of ACP but little is known about its structural characterization.  In the present work, we carried out in silico searches of ACP in the functional genome of Macrobrachium amazonicum, recognized as the most abundant freshwater prawn in Amazon. The ACP gene of M. amazonicum comprised a total of 3326 nucleotides (nt), including a complete open reading frame (ORF) of 1389 nt corresponding to the translation of 462 aminoacids. Signal peptide and intermembrane regions as well as conserved Pfam Pur_ac_phosph_N, Metallophos and Pfam Metallophos_C domains were present in the protein. In addition, we located 8 active sites, 25 homotrimeric and 15 homotetrameric interfaces, and 7 metal-binding sites. In general, we detected highly conserved sites shared among crustaceans.  These data might be useful to provide effective biomarkers to assess the environmental quality and further biotechnological applications of ACP.

Referências

Anand, A., & Srivastava, P. K. (2012). A molecular description of acid phosphatase. In Applied Biochemistry and Biotechnology (Vol. 167, Issue 8, pp. 2174–2197). https://doi.org/10.1007/s12010-012-9694-8

Anger, K. (2013). Neotropical Macrobrachium (Caridea: Palaemonidae): on the biology, origin, and radiation of freshwater-invading shrimp. Journal of Crustacean Biology, 33(2), 151–183. https://doi.org/10.1163/1937240X-00002124

Barbieri, E., Olinto Branco, J., do Carmo Ferrão Santos, M., & Ruiz Hidalgo, K. (2013). Effects of cadmium and zinc on oxygen consumption and ammonia excretion of the sea-bob shrimp, according to the temperature. Bol. Inst. Pesca, 39(3), 299–309.

Bhadouria, J., & Giri, J. (2022). Purple acid phosphatases: roles in phosphate utilization and new emerging functions. In Plant Cell Reports (Vol. 41, Issue 1, pp. 33–51). Springer Science and Business Media Deutschland GmbH. https://doi.org/10.1007/s00299-021-02773-7

Chong-Carrillo, O., Vega-Villasante, F., Arencibia-Jorge, R., Akintola, S. L., Michán-Aguirre, L., & Cupul-Magaña, F. G. (2015). Research on the river shrimps of the genus Macrobrachium (Bate, 1868) (Decapoda: Caridea: Palaemonidae) with known or potential economic importance: Strengths and weaknesses shown through scientometrics. Latin American Journal of Aquatic Research, 43(4), 684–690. https://doi.org/10.3856/vol43-issue4-fulltext-7

Dantzger, D. D., Dantzger, M., Jonsson, C. M., & Aoyama, H. (2017). In Vitro Effects of Agriculture Pollutants on Microcrustacean and Fish Acid Phosphatases. Water, Air, and Soil Pollution, 228(10). https://doi.org/10.1007/s11270-017-3570-7

Duckert, P., Brunak, S., & Blom, N. (2004). Prediction of proprotein convertase cleavage sites. Protein Engineering, Design and Selection, 17(1), 107–112. https://doi.org/10.1093/protein/gzh013

Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D., & Bairoch, A. (2005). Protein Analysis Tools on the ExPASy Server From: The Proteomics Protocols Handbook. http://www.expasy.org/tools/.

Huang, Y., & Ren, Q. (2020). Research progress in innate immunity of freshwater crustaceans. In Developmental and Comparative Immunology (Vol. 104). Elsevier Ltd. https://doi.org/10.1016/j.dci.2019.103569

Iwanaga, S., & Lee, B. L. (2005). Recent Advances in the Innate Immunity of Invertebrate Animals. In Journal of Biochemistry and Molecular Biology (Vol. 38, Issue 2).

Janson, G., Zhang, C., Prado, M. G., & Paiardini, A. (2017). PyMod 2.0: Improvements in protein sequence-structure analysis and homology modeling within PyMOL. Bioinformatics, 33(3), 444–446. https://doi.org/10.1093/bioinformatics/btw638

Jiang, Q., Jiang, Z., Ao, S., Gao, X., Zhu, X., Zhang, Z., & Zhang, X. (2021). Multi-biomarker assessment in the giant freshwater prawn Macrobrachium rosenbergii after deltamethrin exposure. Ecotoxicology and Environmental Safety, 214. https://doi.org/10.1016/j.ecoenv.2021.112067

Lionetto, M. G., Caricato, R., Giordano, M. E., Pascariello, M. F., Marinosci, L., & Schettino, T. (2003). Integrated use of biomarkers (acetylcholinesterase and antioxidant enzymes activities) in Mytilus galloprovincialis and Mullus barbatus in an Italian coastal marine area. Marine Pollution Bulletin, 46(3), 324-330. https://doi.org/10.1016/S0025-326X(02)00403-4.

Jones, P., Binns, D., Chang, H. Y., Fraser, M., Li, W., McAnulla, C., McWilliam, H., Maslen, J., Mitchell, A., Nuka, G., Pesseat, S., Quinn, A. F., Sangrador-Vegas, A., Scheremetjew, M., Yong, S. Y., Lopez, R., & Hunter, S. (2014). InterProScan 5: Genome-scale protein function classification. Bioinformatics, 30(9), 1236–1240. https://doi.org/10.1093/bioinformatics/btu031

Kumar, S., Stecher, G., Li, M., Knyaz, C., & Tamura, K. (2018). MEGA X: Molecular evolutionary genetics analysis across computing platforms. Molecular Biology and Evolution, 35(6), 1547–1549. https://doi.org/10.1093/molbev/msy096

Letunic, I., & Bork, P. (2018). 20 years of the SMART protein domain annotation resource. Nucleic Acids Research, 46(D1), D493–D496. https://doi.org/10.1093/nar/gkx922

Li, F., & Xiang, J. (2013). Recent advances in researches on the innate immunity of shrimp in China. In Developmental and Comparative Immunology (Vol. 39, Issues 1–2, pp. 11–26). Elsevier Ltd. https://doi.org/10.1016/j.dci.2012.03.016

Lima, J. de F., Silva, L. M. A. da, Silva, T. C. da, Garcia, J. da S., Pereira, I. da S., & Amaral, K. D. S. (2014). Reproductive aspects of Macrobrachium amazonicum (Decapoda: Palaemonidae) in the state of Amapá, Amazon River mouth. Acta Amazonica, 44, 245–254.

Loker, E. S., Adema, C. M., Zhang, S., & Kepler, T. B. (2004). Invertebrate immune systems – not homogeneous, not simple, not well understood. Immunological Reviews, 198(1), 10–24. https://doi.org/10.1111/j.0105-2896.2004.0117.x

Maciel, C. (2015). Transcriptomas do Macrobrachium amazonicum desenvolvidos no Sequenciador Ion Torrent. UFPA.

Maciel, C. R., & Valenti, W. C. (2009). Biology, Fisheries, and Aquaculture of the Amazon River Prawn Macrobrachium amazonicum: A Review.

Marques, M. H. C., Silva, I. C. e, Zacardi, D. M., Santos, M. A. S. dos, Brabo, M. F., & Maciel, C. R. (2020). Perfil do consumidor de camarão-da-Amazônia no Estado do Pará: socioeconômica, frequência de consumo e preferências. Research, Society and Development, 9(9), e525997316. https://doi.org/10.33448/rsd-v9i9.7316

Patil, V. N., Kadam, G. H., & Raut, P. D. (2014). Enzymological alterations produced by chronic malathion exposure in freshwater crab, paratelphusa (barytelphusa) jacquemontii. International Journal of Science, Environment and Technology, 3(1), 303–313.

Prestes, R. M., & Vincenci, K. L. (2019). Bioindicadores como avaliação de impacto ambiental. Brazilian Journal of Animal and Environmental Research, 2(4), 1473-1493.

Robert, X., & Gouet, P. (2014). Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Research, 42(W1). https://doi.org/10.1093/nar/gku316

Sang, Z. wen, Bao, M. nan, Liang, Y., Chu, K. hou, & Wang, L. (2023). Identification of acid phosphatase (ShACP) from the freshwater crab Sinopotamon henanense and its expression pattern changes in response to cadmium. Ecotoxicology and Environmental Safety, 255. https://doi.org/10.1016/j.ecoenv.2023.114762

Schenk, G., Mitić, N. Š., Hanson, G. R., & Comba, P. (2013). Purple acid phosphatase: A journey into the function and mechanism of a colorful enzyme. In Coordination Chemistry Reviews (Vol. 257, Issue 2, pp. 473–482). https://doi.org/10.1016/j.ccr.2012.03.020

Tassanakajon, A., Somboonwiwat, K., Supungul, P., & Tang, S. (2013). Discovery of immune molecules and their crucial functions in shrimp immunity. Fish and Shellfish Immunology, 34(4), 954–967. https://doi.org/10.1016/j.fsi.2012.09.021

Wang, C., Wang, R., Yang, H., Wang, Y., & Zhang, Z. (2022). Gene cloning and transcriptional regulation of the alkaline and acid phosphatase genes in Scylla paramamosain. Gene, 810. https://doi.org/10.1016/j.gene.2021.146057

Wang, Y., Sun, J., Liu, J., Guo, Y., Xing, K., Lv, A., & Yiksung, Y. (2017). Histochemical localization of acid phosphatase, alkaline phosphatase and peroxidase in the hepatopancreas, mid-kidney, gill, head kidney, spleen and heart of cultured Cynoglossus semilaevis Günther. Chin. J. Histochem. Cytochem., 26, 229–234.

Waterhouse, A., Bertoni, M., Bienert, S., Studer, G., Tauriello, G., Gumienny, R., Heer, F. T., De Beer, T. A. P., Rempfer, C., Bordoli, L., Lepore, R., & Schwede, T. (2018). SWISS-MODEL: Homology modelling of protein structures and complexes. Nucleic Acids Research, 46(W1), W296–W303. https://doi.org/10.1093/nar/gky427

Wei, J., Liu, B., Fan, S., Zhang, B., Su, J., & Yu, D. (2017). Serum immune response of pearl oyster Pinctada fucata to xenografts and allografts. Fish and Shellfish Immunology, 62, 303–310. https://doi.org/10.1016/j.fsi.2017.01.039

Yamanaka, H. (2008). Biossensores Baseados no processo de iniBição enzimática paulo roberto Brasil de oliveira marques* e. In Quim. Nova (Vol. 31, Issue 7).

Zhao, T., Lozano, Y. M., & Rillig, M. C. (2021). Microplastics Increase Soil pH and Decrease Microbial Activities as a Function of Microplastic Shape, Polymer Type, and Exposure Time. Frontiers in Environmental Science, 9. https://doi.org/10.3389/fenvs.2021.675803

Downloads

Publicado

2024-06-11

Como Citar

Sousa, J. do S. A. da L., Lima, G. M. de, Maciel, B. R., Lutz, Ítalo, Maciel, C. M. T., & Maciel, C. R. (2024). In silico characterization of acid phosphatase in the functional genome of the amazon prawn. Brazilian Journal of Animal and Environmental Research, 7(2), e70373 . https://doi.org/10.34188/bjaerv7n2-093

Edição

v. 7 n. 2 (2024)

Seção

Artigos originais

Licença

  • O conteúdo dos artigos é de responsabilidade exclusiva dos autores.
  •  É permitida a reprodução total ou parcial do conteúdo dos artigos, desde que citada a fonte.
  •  Artigos com plágio serão recusados, e o autor do plágio perderá o direito de publicar nesta revista.
  •  Os nomes e endereços informados nesta revista serão utilizados exclusivamente para os serviços prestados por esta publicação e não estão disponíveis para outros fins ou a terceiros.
  •  Depois de enviar os artigos, os autores cedem os direitos autorais de seus artigos ao BJAER. Se você se arrepender da submissão, o autor tem o direito de solicitar ao BJAER que não publique seu artigo. Porém, essa solicitação deve ocorrer até dois meses antes da divulgação do número que o artigo será publicado.
  •  O BJAER usa a licença Creative Commons CC BY. Informações sobre esta licença podem ser encontradas em: https://creativecommons.org/licenses/by/3.0/br/

 

 

Brazilian Journal of Animal and Environmental Research (BJAER) se reserva o direito de efetuar nos originais alterações de ordem normativa, ortográfica e gramatical, com vistas a manter o padrão culto da língua, respeitando, porém, o estilo dos autores. Os trabalhos finais não serão enviadas aos autores.