Porphyromonas gingivalis fimbriae carbohydrate specificity assessment by glycomics

Abstract

Porphyromonas gingivalis is a major pathogen in adult periodontitis. Fimbriae play an important role in the initial interaction between the bacteria and the host. Our earlier studies suggested that the oligosaccharide moiety of lactoferrin is involved in the interaction with fimbriae. Porphyromonas gingivalis fimbriae bound strongly to albumin-fucosylamide (albumin-1-amido-1-deoxy-L-fucose) and to a lesser extent to albumin-N-acetyl-D-galactosamine (albumin-p-aminophenyl-N-acetyl-β-D-galactosaminide, but failed to bind bovine serum albumin. In this study we explored the glycan array to determine the carbohydrate-binding specificity of P. gingivalis fimbriae. Purified fimbriae bind to glycans which have a Lewis(x), Galβ1-4(Fucα1-3) GlcNAcβ structure in common. Interestingly, all glycans have a terminal fucose moiety and if fucose is removed, the fimbriae fail to bind. This is the first study that suggests that fucose is important for P. gingivalis fimbriae binding.

Polymicrobial Synergy Stimulates Porphyromonas Gingivalis Survival And Gingipain Expression In A Multispecies Subgingival Community

“…Strain 33F showed the lowest absolute level of binding and the lack of a strong relationship between the presence of fimbrillin and adherence suggests that FimA is not critical for binding to surface-associated serum proteins. This is in agreement with a previous study showing that P gingivalis fimbriae do not bind to serum albumin [29] although FimA fimbriae are known to be important for binding of P. gingivalis to other bacteria such as Streptococcus oralis [30].…”

Polymicrobial synergy stimulates Porphyromonas gingivalis survival and gingipain expression in a multi-species subgingival community

“…Strain 33F showed the lowest absolute level of binding and the lack of a strong relationship between the presence of fimbrillin and adherence suggests that FimA is not critical for binding to surface-associated serum proteins. This is in agreement with a previous study showing that P gingivalis fimbriae do not bind to serum albumin [ 32 ] although FimA fimbriae are known to be important for binding of P. gingivalis to other bacteria such as Streptococcus oralis [ 33 ].…”

“…Isoelectric focusing was carried out on 18-cm pH 4–7 linear immobilized pharmalyte gradient strips followed by gel electrophoresis on 10% polyacrylamide gels. Gels were stained with colloidal Coomassie brilliant blue G. The most abundant proteins were excised manually and subjected to LC–MS/MS as described previously [ 32 ]. Mass lists were created automatically and used as the input for Mascot MS/MS Ions searches of the NCBInr database using the Matrix Science web server.…”

Uncovering the molecular networks in periodontitis

“…For instance, more ‘omics studies are needed to identify bacterial adhesins, their targets, and virulence factors as well as human proteases, which can be potential predictors of disease progression and a discriminatory tool between different clinical presentations of periodontitis. For example, a glycomic study was already performed, which revealed the importance of fucose in host glycan moieties to P. gingivalis ’ fimbriae binding . Moreover, P. gingivalis ATCC 33277 fimbriae have been shown to adhere to acidic proline‐rich proteins, proline‐rich glycoproteins, and statherins, proteins present in parotid‐derived salivary secretion .…”