A ConA-like lectin isolated from <i>Canavalia maritima</i> seeds alters the expression of genes related to virulence and biofilm formation in <i>Streptococcus mutans</i> — Oak Academic Publishing
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A ConA-like lectin isolated from <i>Canavalia maritima</i> seeds alters the expression of genes related to virulence and biofilm formation in <i>Streptococcus mutans</i>
Faculty of Dentistry, Institute of Applied Theology (INTA), Sobral, Brazil
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Integrate Biomolecules Laboratory (LIBS), Faculty of Medicine of Sobral, Federal University of Ceará, Sobral, Brazil
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Integrate Biomolecules Laboratory (LIBS), Faculty of Medicine of Sobral, Federal University of Ceará, Sobral, Brazil
,
Integrate Biomolecules Laboratory (LIBS), Faculty of Medicine of Sobral, Federal University of Ceará, Sobral, Brazil
,
Biologically Active Molecules Laboratory (Biomol-Lab), Department of Biochemistry and Molecular Biology, Federal University of Ceará, Forta-leza, Brazil
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Integrate Biomolecules Laboratory (LIBS), Department of Pathology and Legal Medicine, Federal University of Ceará, Fortaleza, Brazil
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Biologically Active Molecules Laboratory (Biomol-Lab), Department of Biochemistry and Molecular Biology, Federal University of Ceará, Forta-leza, Brazil
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Center of the Exact Sciences and Technology, Acaraú Valley State Uni-versity, Sobral, Brazil
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Center of Agricultural Science and Biological, Acaraú Valley State Uni-versity, Sobral, Brazil
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Integrate Biomolecules Laboratory (LIBS), Faculty of Medicine of Sobral, Federal University of Ceará, Sobral, Brazil
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Biologically Active Molecules Laboratory (Biomol-Lab), Department of Biochemistry and Molecular Biology, Federal University of Ceará, Forta-leza, Brazil
1 Faculty of Dentistry, Institute of Applied Theology (INTA), Sobral, Brazil
2 Integrate Biomolecules Laboratory (LIBS), Faculty of Medicine of Sobral, Federal University of Ceará, Sobral, Brazil
3 Integrate Biomolecules Laboratory (LIBS), Faculty of Medicine of Sobral, Federal University of Ceará, Sobral, Brazil
4 Integrate Biomolecules Laboratory (LIBS), Faculty of Medicine of Sobral, Federal University of Ceará, Sobral, Brazil
5 Biologically Active Molecules Laboratory (Biomol-Lab), Department of Biochemistry and Molecular Biology, Federal University of Ceará, Forta-leza, Brazil
6 Integrate Biomolecules Laboratory (LIBS), Department of Pathology and Legal Medicine, Federal University of Ceará, Fortaleza, Brazil
7 Biologically Active Molecules Laboratory (Biomol-Lab), Department of Biochemistry and Molecular Biology, Federal University of Ceará, Forta-leza, Brazil
8 Center of the Exact Sciences and Technology, Acaraú Valley State Uni-versity, Sobral, Brazil
9 Center of Agricultural Science and Biological, Acaraú Valley State Uni-versity, Sobral, Brazil
10 Integrate Biomolecules Laboratory (LIBS), Faculty of Medicine of Sobral, Federal University of Ceará, Sobral, Brazil
11 Biologically Active Molecules Laboratory (Biomol-Lab), Department of Biochemistry and Molecular Biology, Federal University of Ceará, Forta-leza, Brazil
Bacteria form biofilms as an adaptive mechanism in response to environmental changes. Streptococcus mutans is the biofilm-forming bacterium that is primarily associated with dental caries. The expression of important genes by bacteria in biofilms is different from that of planktonic cells. Lectins are proteins that bind specifically to carbohydrates and may have important biological activities on bacterial cells, acting as antibacterial and anti-biofilm agents. ConM ( Ca navalia maritima lectin) is a protein that is able to inhibit the planktonic growth and biofilm formation of S. mutans . In this context, this study aimed to evaluate the effects of ConM and concanavalin A (ConA) on the expression of genes related to virulence and biofilm formation in S. mutans . The results showed that ConM significantly reduced the expression of genes encoding enzymes related to adhesion, formation and regulation of biofilms. On the contrary, ConA did not alter the expression of the genes studied. Because the two lectins have a high degree of similarity, the differences in the actions of ConM and ConA may be explained by the small structural differences in the carbohydrate recognition domain of the lectins.
McDougald, D., Rice, S.A., Barraud, N., Steinberg, P.D. and Kjelleberg, S. (2012) Should we stay or should we go: mechanisms and ecological consequences for biofilm dispersal. Nature Reviews Microbiology, 10, 39-50. http://dx.doi.org/10.1038/nrmicro2695
Paquette, D.W., Brodala, N. and Williams, R.C. (2006) Risk factors for endosseous dental implant failure. Dental Clinics of North America, 50, 361-374. http://dx.doi.org/10.1016/j.cden.2006.05.002
Dhir, S. (2013) Biofilm and dental implant: The microbial link. Journal of Indian Society of Periodontology, 17, 5-11. http://dx.doi.org/10.4103/0972-124X.107466
Buser, D. and Merickse-Stern, R. (1997) Long term evaluation of nonsubmerged ITI implants. Part 1: 8 year life table analysis of a prospective multicenter study with 2359 implants. Clinical Oral Implants Research, 8, 161-172. http://dx.doi.org/10.4103/0972-124X.107466
Marsh, P.D. (2005) Dental plaque: biological significance of a biofilm and community life-style. Journal of Clinical Periodontology, 32,7-15. http://dx.doi.org/10.1034/j.1600-0501.1997.080302.x
Brooun, A., Liu, S. and Lewis, K.A. (2000) A Dose-Response study of antibiotic resistance in Pseudomonas aeruginosa biofilms. Antimicrobial Agents and Chemotherapy, 44, 640-646. http://dx.doi.org/10.1111/j.1600-051X.2005.00790.x
Sauer, K. and Camper, A.K. (2001) Characterization of phenotypic changes in Pseudomonas putida in response to surface-associated growth. Journal of Bacteriology, 183, 6579-6589. http://dx.doi.org/10.1128/AAC.44.3.640-646.2000
Shemesh, M., Tam, A. and Steinberg, D. (2007) Expression of biofilm-associated genes of Streptococcus mutans in response to glucose and sucrose. Journal of Medical Microbiology, 56, 1528-1535. http://dx.doi.org/10.1128/JB.183.22.6579-6589.2001
Shemesh, M., Tam, A., Aharoni, R. and Steinberg, D. (2010) Genetic adaptation of Streptococcus mutans during biofilm formation on different types of surfaces. BMC Microbiology, 10, 51. http://dx.doi.org/10.1099/jmm.0.47146-0
Wen, Z.T. and Burne, R.A. (2002) Functional genomics approach to identifying genes required for biofilm development by Streptococcus mutans. Applied and Environmental Microbiology, 68, 1196-1203. http://dx.doi.org/10.1186/1471-2180-10-51
Bies, C., Lehr, C.M. and Woodley, J.F. (2004) Lectinmediated drug targeting: history and applications. Advanced Drug Delivery Reviews, 56, 425-435. http://dx.doi.org/10.1128/AEM.69.1.722.2003
Rakhshandehroo, M., Stienstra, R., De Wit, N.J., Bragt, M.C., Haluzik, M., Mensink, R.P., Müller, M. and Kersten, S. (2012) Plasma mannose-binding lectin is stimulated by PPARα in humans. American Journal of Physiology-Endocrinology and Metabolism, 302, 595-602. http://dx.doi.org/10.1016/j.addr.2003.10.030
Zappelli, C., Van Der Zwaan, C., Thijssen-Timmer, D.C., Mertens, K. and Meijer, A.B. (2012) Novel role for galectin-8 protein as mediator of coagulation factor V endocytosis by megakaryocytes. The Journal of Biological Chemistry, 287, 8327-8335. http://dx.doi.org/10.1152/ajpendo.00299.2011
Hirabayashi, J. (2008) Concept, strategy and realization of lectin-based glycan profiling. Journal of Biochemistry, 144, 139-147. http://dx.doi.org/10.1074/jbc.M111.305151
Wong, J.H., Ng, T.B., Cheung, R.C., Ye, X.J., Wang, H.X., Lam, S.K., Lin, P., Chan, Y.S., Fang, E.F., Ngai, P.H., Xia, L.X., Ye, X.Y., Jiang, Y. and Liu, F. (2010) Proteins with antifungal properties and other medicinal applications from plants and mushrooms. Applied Microbiology and biotechnology, 87, 1221-1235. http://dx.doi.org/10.1093/jb/mvn043
Teixeira, E.H., Napimoga, M.H., Carneiro, V.A., De Oliveira, T.M., Cunha, R.M., Havt, A., Martins, J.L., Pinto, V.P., Gonçalves, R.B. and Cavada, B.S. (2006) In vitro inhibition of streptococci binding to enamel acquired pellicle by plant lectins. Journal of Applied Microbiology, 101, 111-116. http://dx.doi.org/10.1007/s00253-010-2690-4
Cavalcante, T.T., Da Rocha, B.A.M., Carneiro, V.A., Arruda, F.V.S., Do Nascimento, A.S.F., Sá, N.C., Nascimento, K.S., Cavada, B.S. and Teixeira, E.H. (2011) Effect of lectins from Diocleinae subtribe against oral Streptococci. Molecules, 16, 3530-3543. http://dx.doi.org/10.1111/j.1365-2672.2006.02910.x
Laemmili, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685. http://dx.doi.org/10.3390/molecules16053530
Ritz, M., Garenaux, A., Berge, M. and Federighi, M. (2009) Determination of rpoA as the most suitable internal control to study stress response in C. jejuni by RTqPCR and application to oxidative stress. Journal of Microbiological Methods, 76, 196-200. http://dx.doi.org/10.1016/j.mimet.2008.10.014
Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular cloning: A laboratory manual. 2nd Edition, Cold Spring Harbor, New York.
Wen, Z.T., Yates, D., Ahn, S.J. and Burne, R.A. (2010) Biofilm formation and virulence expression by Streptococcus mutans are altered when grown in dual-species model. BMC Microbiology, 10, 111. http://dx.doi.org/10.1186/1471-2180-10-111
Livak, K.J. and Schmittgen, T.D. (2001) Analysis of relative gene expression data using Real-Time Quantitative PCR and the 2–ΔΔCT Method. Methods, 25, 402-408. http://dx.doi.org/10.1006/meth.2001.1262
Tsumori, H. and Kuramitsu, H. (1997) The role of the Streptococcus mutans glucosyltransferases in the sucrose-dependent attachment to smooth surfaces: Essential role of the GtfC enzyme. Oral Microbiology and Immunology, 12, 274-280. http://dx.doi.org/10.1111/j.1399-302X.1997.tb00391.x
Banas, J.A. and Vickerman, M.M. (2003) Glucan-binding proteins of the oral streptococci. Critical Reviews in Oral Biology & Medicine, 14, 89-99. http://dx.doi.org/10.1177/154411130301400203
Jakubovics, N.S., Strömberg, N., Van Dolleweerd, C.J., Kelly, C.G. and Jenkinson, H.F. (2005) Differential binding specificities of oral streptococcal antigen I/II family adhesins for human or bacterial ligands. Molecular Microbiology, 55, 1591-1605. http://dx.doi.org/10.1111/j.1365-2958.2005.04495.x
Wen, Z.T., Baker, H.V. and Burne, R.A. (2006) Influence of BrpA on critical virulence attributes of Streptococcus mutans. Journal of Bacteriology, 188, 2983-2992. http://dx.doi.org/10.1128/JB.188.8.2983-2992.2006
Merritt J., Kreth, J., Qi, F., Sullivan, R. and Shi, W. (2005) Non-disruptive, real-time analyses of the metabolic status and viability of Streptococcus mutans cells in response to antimicrobial treatments. Journal of Microbiology Methods, 61, 161-170. http://dx.doi.org/10.1016/j.mimet.2004.11.012
Yang, D.Q., Liu, T.J., Zhou, X.D., He, K.F., Li, S. and Zhuang, H. (2005) Study on lactate dehydrogenase activity of Streptococcus mutans isolates derived from caries-active and caries-free individuals. Hua Xi Kou Qiang Yi Xue Za Zhi, 23, 116-118.
Hillman, J.D., Chen, A., Duncan, M. and Lee, S.W. (1994) Evidence that L-(+)-lactate dehydrogenase deficiency is lethal in Streptococcus mutans. Infection and Immunity, 62, 60-64. http://iai.asm.org/content/62/1/60
Bezerra, G.A., Oliveira, T.M., Moreno, F.B., de Souza, E.P., Rocha, B.A., Benevides, R.G., Delatorre, P., De Azevedo Jr., W.F. and Cavada, B.S. (2007) Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: New insights into the understanding of the structure biological activity relationship in legume lectins. Journal of Structural Biology, 160, 168-176. http://dx.doi.org/10.1016/j.jsb.2007.07.012
Nóbrega, R.B., Rocha, B.M., Gadelha, C.A., SantiGadelha, T., Pires, A.F., Assreuy, A.M.S., Nascimento, K.S., Nagano, C.S., Sampaio, A.H., Cavada, B.S. and Delatorre, P. (2012) Structure of Dioclea virgata lectin: Relations between carbohydrate binding site and nitric oxide production. Biochimie, 94, 900-906. http://dx.doi.org/10.1016/j.biochi.2011.12.009
de Vasconcelos, M.A., Cunha, C.O., Arruda, F.V.S., Carneiro, V.A., Mercante, F.M., do Nascimento Neto, L.G., de Sousa, G.S., Rocha, B.A.M., Teixeira, E.H., Cavada, B.S. and dos Santos, R.P. (2012) Lectin from Canavalia brasiliensis seeds (ConBr) is a valuable biotechnological tool to stimulate the growth of Rhizobium tropici in vitro. Molecules, 17, 5244-5254. http://dx.doi.org/10.3390/molecules17055244
Bezerra, M.J.B., Rodrigues, N.V.F.C.,; Pires, A.F., Bezerra, G.A., Nobre, C.B., Alencar, K.L.L., Soares, P.M.G., Nascimento, K.S., Nagano, C.S., Martins, J.L., Gruber, K., Sampaio, A.H., Delatorre, P., Rocha, B.A.M., Assreuy, A.M.S. and Cavada, B.S. (2013) Crystal structure of Dioclea violacea lectin and a comparative study of vasorelaxant properties with Dioclea rostrata lectin. International Journal of Biochemistry & Cell Biology, 45, 807-815. http://dx.doi.org/10.1016/j.biocel.2013.01.012
Cavada, B.S., Barbosa, T., Arruda, S., Grangeiro, T.B. and Barral-Netto, M. (2001) Revisiting proteus: Do minor changes in lectin structure matter in biological activity? Lessons from and potential biotechnological uses of the Diocleinae subtribe lectins. Current Protein & Peptide Science, 2, 123-135. http://dx.doi.org/10.2174/1389203013381152
Bezerra, E.H., Rocha, B.A., Nagano, C.S., Bezerra, G.D., Moura, T.R., Bezerra, M.J., Benevides, R.G., Sampaio, A.H., Assreuy, A.M.S., Delatorre, P. and Cavada, B.S. (2011) Structural analysis of ConBr reveals molecular correlation between the carbohydrate recognition domain and nitric oxide release from endothelial cells. Biochemical and Biophysical Research Communications, 408, 566-570. http://dx.doi.org/10.1016/j.bbrc.2011.04.061