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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

has been cited by the following article:

• TITLE: A ConA-like lectin isolated from Canavalia maritima seeds alters the expression of genes related to virulence and biofilm formation in Streptococcus mutans

  AUTHORS: Theodora Thays Arruda Cavalcante, Victor Alves Carneiro, Cinara Carneiro Neves, Humberlânia de Sousa Duarte, Maria Gleiciane de Queiroz Martins, Francisco Vassiliepe Sousa Arruda, Mayron Alves de Vasconcelos, Hélcio Silva dos Santos, Rodrigo Maranguape da Silva Cunha, Benildo Sousa Cavada, Edson Holanda Teixeira

  KEYWORDS: Streptococcus mutants; Lectin; Canavalia maritima; Biofilm; Expression

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.12, December 26, 2013

  ABSTRACT: 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 (Canavalia 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.