Literature DB >> 29644253

Lectin Binding Analysis of Streptococcus mutans Glycoproteins.

Alejandro Avilés-Reyes1, José A Lemos1, Jacqueline Abranches1.   

Abstract

Bacterial glycoproteins are of increasing interest due to their abundance in nature and importance in health and infectious diseases. However, only a very small fraction of bacterial glycoproteins have been characterized and its post-translational modification machinery identified. While analysis of glycoproteins can be achieved through various techniques, this is often limited by the specific characteristics of individual proteins such as type and level of glycosylation. Lectins are sugar-binding proteins that recognize specific glycoconjugates in a manner similar to antigen-antibody interactions. Here, we describe a simple method for the detection of glycoproteins using lectin-based Western blot analysis, which can be applied to different organisms and coupled with various other strategies for complementary analysis.

Entities:  

Year:  2015        PMID: 29644253      PMCID: PMC5891095          DOI: 10.21769/BioProtoc.1431

Source DB:  PubMed          Journal:  Bio Protoc        ISSN: 2331-8325


  2 in total

Review 1.  Protein glycosylation in bacteria: sweeter than ever.

Authors:  Harald Nothaft; Christine M Szymanski
Journal:  Nat Rev Microbiol       Date:  2010-11       Impact factor: 60.633

2.  Modification of Streptococcus mutans Cnm by PgfS contributes to adhesion, endothelial cell invasion, and virulence.

Authors:  Alejandro Avilés-Reyes; James H Miller; Patricia J Simpson-Haidaris; Fred K Hagen; Jacqueline Abranches; José A Lemos
Journal:  J Bacteriol       Date:  2014-05-16       Impact factor: 3.490

  2 in total

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