Antifungal Effect of Bauhinia variegata Lectin (BvL) on Bipolaris oryzae.


Journal

Current microbiology
ISSN: 1432-0991
Titre abrégé: Curr Microbiol
Pays: United States
ID NLM: 7808448

Informations de publication

Date de publication:
27 Aug 2024
Historique:
received: 08 05 2024
accepted: 15 08 2024
medline: 27 8 2024
pubmed: 27 8 2024
entrez: 27 8 2024
Statut: epublish

Résumé

The search for less harmful, ecologically efficient, more specific, and natural alternatives for the control of pathogens is essential. Bauhinia variegata lectin (BvL) is a protein that has numerous biological activities, including antifungal. The present study examines the potential in vitro of B. variegata lectin against the fungus Bipolaris oryzae, responsible for agricultural losses in southern Brazil, due to damage to rice fields during seed germination. Bioassays to assess the inhibition potential of BvL were performed, including fungal growth, spore formation, and germination, in concentrations of 0, 25, 50, and 100 µg mL

Identifiants

pubmed: 39190055
doi: 10.1007/s00284-024-03848-w
pii: 10.1007/s00284-024-03848-w
doi:

Substances chimiques

Antifungal Agents 0
Plant Lectins 0
Lectins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

329

Informations de copyright

© 2024. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Références

Ghini R, Kimati H (2002) Resistência de fungos a fungicidas, Embrapa Meio Ambient 78. http://arxiv.org/abs/1011.1669%0A . https://doi.org/10.1088/1751-8113/44/8/085201 . Accessed 20 Mar 2020
Wang HX, Ng TB (2003) Dendrocin, a distinctive antifungal protein from bamboo shoots. Biochem Biophys Res Commun 307:750–755. https://doi.org/10.1016/S0006-291X(03)01229-4
doi: 10.1016/S0006-291X(03)01229-4 pubmed: 12893287
Yevtushenko DP, Romero R, Forward BS, Hancock RE, Kay WW, Misra S (2005) Pathogen-induced expression of a cecropin A-melittin antimicrobial peptide gene confers antifungal resistance in transgenic tobacco. J Exp Bot 56:1685–1695. https://doi.org/10.1093/jxb/eri165
doi: 10.1093/jxb/eri165 pubmed: 15863447
Corrado G, Arciello S, Fanti P, Fiandra L, Garonna A, Digilio MC, Lorito M, Giordana B, Pennacchio F, Rao R (2008) The Chitinase A from the baculovirus AcMNPV enhances resistance to both fungi and herbivorous pests in tobacco. Transgenic Res 17:557–571. https://doi.org/10.1007/s11248-007-9129-4
doi: 10.1007/s11248-007-9129-4 pubmed: 17851776
de Farias CRJ, Afonso APS, Pierobom CR, Del Ponte EM (2011) Regional survey and identification of Bipolaris spp. associated with rice seeds in Rio Grande do Sul State, Brazil. Ciência Rural 42:369–372. https://doi.org/10.1146/annurev.py.26.090188.000345
doi: 10.1146/annurev.py.26.090188.000345
Amaral MFZJ, Bara MTF (2005) Avaliaçâo da atividade antifúngica de extratos de plantas sobre o crescimento de fitopatógenos. Rev Eletrônica Farmácia 2:5–8
Souza JD, Silva MBR, Argolo ACC, Napoleão TH, Sá RA, Correia MTS, Paiva PMG, Silva MDC, Coelho LCBB (2011) A new Bauhinia monandra galactose-specific lectin purified in milligram quantities from secondary roots with antifungal and termiticidal activities. Int Biodeterior Biodegrad 65:696–702. https://doi.org/10.1016/j.ibiod.2011.02.009
doi: 10.1016/j.ibiod.2011.02.009
Kheeree N, Sangvanich P, Puthong S, Karnchanatat A (2010) Antifungal and antiproliferative activities of lectin from the rhizomes of Curcuma amarissima Roscoe. Appl Biochem Biotechnol 162:912–925. https://doi.org/10.1007/s12010-009-8804-8
doi: 10.1007/s12010-009-8804-8 pubmed: 19838861
Pelegrini P, Noronha E, Muniz M, Vasconcelos I, Oliveira J, Franco O (2006) An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins. Biochim Biophys Acta 1764:1141–1146. https://doi.org/10.1016/j.bbapap.2006.04.010
doi: 10.1016/j.bbapap.2006.04.010 pubmed: 16766236
Fonseca VJ, Braga AL, Ribeiro Filho J, Teixeira CS, da Hora GC, Morais-Braga MF (2022) A review on the antimicrobial properties of lectins. Int J Biol Macromol 195:163–178. https://doi.org/10.1016/j.ijbiomac.2021.11.209
doi: 10.1016/j.ijbiomac.2021.11.209 pubmed: 34896466
Pan S, Tang J, Gu X (2010) Isolation and characterization of a novel fucose-binding lectin from the gill of bighead carp (Aristichthys nobilis). Vet Immunol Immunopathol 133:154–164. https://doi.org/10.1016/j.vetimm.2009.07.015
doi: 10.1016/j.vetimm.2009.07.015 pubmed: 19709756
Sharon N, Lis H (1990) Legume lectins—a large family of homologous proteins. FASEB J 4:3198–3208. https://doi.org/10.1096/fasebj.4.14.2227211
doi: 10.1096/fasebj.4.14.2227211 pubmed: 2227211
Filho VC (2009) Chemical composition and biological potential of plants from the genus Bauhinia. Phyther Res 23:1347–1354. https://doi.org/10.1002/ptr.2756
doi: 10.1002/ptr.2756
Pinto LS, Nagano CS, Oliveira TM, Moura TR, Sampaio AH, Debray H, Pinto VP, Dellagostin OA, Cavada BS (2008) Purification and molecular cloning of a new galactose-specific lectin from Bauhinia variegata seeds. J Biosci 33:355–363. https://doi.org/10.1007/s12038-008-0055-2
doi: 10.1007/s12038-008-0055-2 pubmed: 19005235
Klafke GB, Moreira GMSG, Monte LG, Pereira JL, Brandolt TM, Xavier MO, Santi-Gadelha T, Dellagostin OA, da Silva Pinto L (2013) Assessment of plant lectin antifungal potential against yeasts of major importance in medical mycology. Mycopathologia 175:147–151. https://doi.org/10.1007/s11046-012-9596-x
doi: 10.1007/s11046-012-9596-x pubmed: 23161017
Do Nascimento Neto LG, Da Silva Pinto L, Bastos RM, Evaristo FFV, De Vasconcelos MA, Carneiro VA, Arruda FVS, Porto ALF, Leal RB, Da Silva VA, Cavada BS, Teixeira EH (2011) Effect of the lectin of Bauhinia variegata and its recombinant isoform on surgically induced skin wounds in a murine model. Molecules 16:9298–9315. https://doi.org/10.3390/molecules16119298
doi: 10.3390/molecules16119298
Lin P, Tzi BN (2008) Preparation and biological properties of a melibiose binding lectin from Bauhinia variegata seeds. J Agric Food Chem 56:10481–10486. https://doi.org/10.1021/jf8016332
doi: 10.1021/jf8016332 pubmed: 18942841
Chan YS, Ng TB (2014) Bauhinia variegata var. variegata lectin: isolation, characterization, and comparison. Appl Biochem Biotechnol 175(1):75–84. https://doi.org/10.1007/s12010-014-1261-z
doi: 10.1007/s12010-014-1261-z pubmed: 25240852
Mishra RP, Ganaie AA, Allaie AH (2016) Isolation and purification of a galactose specific lectin from seeds of Bauhinia Variegata and evaluation of its antimicrobial potential. Int J Pharm Sci Res. https://doi.org/10.13040/IJPSR.0975-8232.7(2).804-09
doi: 10.13040/IJPSR.0975-8232.7(2).804-09
Teixeira EH, Napimoga MH, Carneiro VA, De Oliveira TM, Nascimento KS, Nagano CS, Souza JB, Havt A, Pinto VPT, Gonçalves RB, Farias WRL, Saker-Sampaio S, Sampaio AH, Cavada BS (2007) In vitro inhibition of oral streptococci binding to the acquired pellicle by algal lectins. J Appl Microbiol 103:1001–1006. https://doi.org/10.1111/j.1365-2672.2007.03326.x
doi: 10.1111/j.1365-2672.2007.03326.x pubmed: 17897204
Wu J, Wang J, Wang S, Rao P (2016) Lunatin, a novel lectin with antifungal and antiproliferative bioactivities from Phaseolus lunatus billb. Int J Biol Macromol 89:717–724. https://doi.org/10.1016/j.ijbiomac.2016.04.092
doi: 10.1016/j.ijbiomac.2016.04.092 pubmed: 27164500
Freire MDGM, Gomes VM, Corsini RE, Machado OLT, De Simone SG, Novello JC, Marangoni SÉ, Macedo MLR (2002) Isolation and partial characterization of a novel lectin from Talisia esculenta seeds that interferes with fungal growth. Plant Physiol Biochem 40:61–68. https://doi.org/10.1016/S0981-9428(01)01342-0
doi: 10.1016/S0981-9428(01)01342-0
Silva HC, Pinto LDS, Teixeira EH, Nascimento KS, Cavada BS, Silva ALC (2014) BUL: a novel lectin from Bauhinia ungulata L. seeds with fungistatic and antiproliferative activities. Process Biochem 49:203–209. https://doi.org/10.1016/j.procbio.2013.10.020
doi: 10.1016/j.procbio.2013.10.020
Regente M, Taveira GB, Pinedo M, Elizalde MM, Ticchi AJ, Diz MSS, Carvalho AO, De La Canal L, Gomes VM (2014) A sunflower lectin with antifungal properties and putative medical mycology applications. Curr Microbiol 69:88–95. https://doi.org/10.1007/s00284-014-0558-z
doi: 10.1007/s00284-014-0558-z pubmed: 24623187
Gomes FS, Procópio TF, Napoleão TH, Coelho LCBB, Paiva PMG (2013) Antimicrobial lectin from Schinus terebinthifolius leaf. J Appl Microbiol 114:672–679. https://doi.org/10.1111/jam.12086
doi: 10.1111/jam.12086 pubmed: 23190078
Sá RA, Gomes FS, Napoleão TH, Santos NDL, Melo CML, Gusmão NB, Coelho LCBB, Paiva PMG, Bieber LW (2009) Antibacterial and antifungal activities of Myracrodruon urundeuva heartwood. Wood Sci Technol 43:85–95. https://doi.org/10.1007/s00226-008-0220-7
doi: 10.1007/s00226-008-0220-7
Kanokwiroon K, Teanpaisan R, Wititsuwannakul D, Hooper AB, Wititsuwannakul R (2008) Antimicrobial activity of a protein purified from the latex of Hevea brasiliensis on oral microorganisms. Mycoses 51:301–307. https://doi.org/10.1111/j.1439-0507.2008.01490.x
doi: 10.1111/j.1439-0507.2008.01490.x pubmed: 18924261
Santana GMS, Albuquerque LP, Simões DA, Coelho LCBB, Paiva PMG, Gusmão NB (2009) Isolation of lectin from opuntia ficus-indica cladodes. In: VI Int. Congr. Cactus Pear Cochineal, International Society for Horticultural Science, pp 281–286. https://doi.org/10.17660/ActaHortic.2009.811.37
Selitrennikoff CP (2001) Antifungal proteins. Appl Environ Microbiol 67:2883–2894. https://doi.org/10.1128/AEM.67.7.2883-2894.2001
doi: 10.1128/AEM.67.7.2883-2894.2001 pubmed: 11425698 pmcid: 92957
Nanba H, Kuroda H (1971) Studies of fungicides. VII. Chemical composition of cell walls of Cochliobolus miyabeanus. Chem Pharm Bull 19:252–258. https://doi.org/10.1248/cpb.19.252
doi: 10.1248/cpb.19.252
Boleti APDA, Freire MDGM, Coelho MB, Da Silva W, Baldasso PA, Gomes VM, Marangoni S, Novello JC, Macedo MLR (2007) Insecticidal and antifungal activity of a protein from Pouteria torta seeds with lectin-like properties. J Agric Food Chem 55:2653–2658. https://doi.org/10.1021/jf0636317
doi: 10.1021/jf0636317 pubmed: 17348680
Sitohy M, Doheim M, Badr H (2007) Isolation and characterization of a lectin with antifungal activity from Egyptian Pisum sativum seeds. Food Chem 104:971–979. https://doi.org/10.1016/j.foodchem.2007.01.026
doi: 10.1016/j.foodchem.2007.01.026
Lis H, Sharon N (1981) Lectins in higher plants, Proteins and Nucleic Acids (USA)
van Deenen N, Prüfer D, Gronover CS (2011) A latex lectin from Euphorbia trigona is a potent inhibitor of fungal growth. Biol Plant 55:335–339. https://doi.org/10.1007/s10535-011-0049-z
doi: 10.1007/s10535-011-0049-z
Ramos MV, Brito D, Freitas CDT, Gonçalves JFC, Porfirio CTMN, Lobo MDP, Monteiro-Moreira ACO, Souza LAC, Fernandes AV (2018) Proteomic identification and purification of seed proteins from native Amazonian species displaying antifungal activity. Planta 248:197–209. https://doi.org/10.1007/s00425-018-2893-y
doi: 10.1007/s00425-018-2893-y pubmed: 29675765
Del Rio M, de la Canal L, Pinedo M, Regente M (2018) Internalization of a sunflower mannose-binding lectin into phytopathogenic fungal cells induces cytotoxicity. J Plant Physiol 221:22–31. https://doi.org/10.1016/j.jplph.2017.12.001
doi: 10.1016/j.jplph.2017.12.001 pubmed: 29223879
Dang L, Van Damme EJM (2015) Toxic proteins in plants. Phytochemistry 117:51–64. https://doi.org/10.1016/j.phytochem.2015.05.020
doi: 10.1016/j.phytochem.2015.05.020 pubmed: 26057229 pmcid: 7111729
Charungchitrak S, Petsom A, Sangvanich P, Karnchanatat A (2011) Antifungal and antibacterial activities of lectin from the seeds of Archidendron jiringa Nielsen. Food Chem 126:1025–1032. https://doi.org/10.1016/j.foodchem.2010.11.114
doi: 10.1016/j.foodchem.2010.11.114

Auteurs

Danillo de Oliveira Della Senta (D)

Programa de Pós-Graduação em Biotecnologia, Laboratório Bioinformática e Proteômica (BioPro Lab), Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Campus Universitário, s/n - Prédio 19, Pelotas, RS, 96010-900, Brazil.

Guilherme Cardoso (G)

Programa de Pós-Graduação em Biotecnologia, Laboratório Bioinformática e Proteômica (BioPro Lab), Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Campus Universitário, s/n - Prédio 19, Pelotas, RS, 96010-900, Brazil.

Alessandra Neis (A)

Programa de Pós-Graduação em Biotecnologia, Laboratório Bioinformática e Proteômica (BioPro Lab), Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Campus Universitário, s/n - Prédio 19, Pelotas, RS, 96010-900, Brazil.

Guilherme Feijó de Sousa (GF)

Programa de Pós-Graduação em Biotecnologia, Laboratório Bioinformática e Proteômica (BioPro Lab), Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Campus Universitário, s/n - Prédio 19, Pelotas, RS, 96010-900, Brazil.

Diego Serrasol do Amaral (DS)

Programa de Pós-Graduação em Biotecnologia, Laboratório Bioinformática e Proteômica (BioPro Lab), Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Campus Universitário, s/n - Prédio 19, Pelotas, RS, 96010-900, Brazil.

Cândida Jacobsen de Farias (CJ)

Faculdade de Agronomia Eliseu Maciel, Universidade Federal de Pelotas, Pelotas, Brazil.

Luciano da Silva Pinto (L)

Programa de Pós-Graduação em Biotecnologia, Laboratório Bioinformática e Proteômica (BioPro Lab), Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Campus Universitário, s/n - Prédio 19, Pelotas, RS, 96010-900, Brazil. dmpluc@gmail.com.

Articles similaires

Meiosis Schizosaccharomyces Schizosaccharomyces pombe Proteins Spores, Fungal

Perceptions of the neighbourhood food environment and food insecurity of families with children during the Covid-19 pandemic.

Irene Carolina Sousa Justiniano, Matheus Santos Cordeiro, Hillary Nascimento Coletro et al.
1.00
Humans COVID-19 Food Insecurity Cross-Sectional Studies Female
Humans COVID-19 Brazil Resilience, Psychological Cross-Sectional Studies
Genome, Viral Ralstonia Composting Solanum lycopersicum Bacteriophages

Classifications MeSH