ArticleThe Journal of biological chemistry2009
Differential recognition and hydrolysis of host carbohydrate antigens by Streptococcus pneumoniae family 98 glycoside hydrolases.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 45 citations in OpenAlex.
- Article
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- FUT2-ABO epistasis increases the risk of early childhood asthma and Streptococcus pneumoniae respiratory illnesses.Nature communications · 2020Article
- Crystal structure and receptor-interacting residues of MYDGF - a protein mediating ischemic tissue repair.Nature communications · 2019Article
- Two complementary α-fucosidases fromThe Journal of biological chemistry · 2019Article
- Differential Utilization of Basic Proline-Rich Glycoproteins during Growth of Oral Bacteria in Saliva.Applied and environmental microbiology · 2016Article
- Vaccination Drives Changes in Metabolic and Virulence Profiles of Streptococcus pneumoniae.PLoS pathogens · 2015Article
- Glycan complexity dictates microbial resource allocation in the large intestine.Nature communications · 2015Article
- Genomic signatures of human and animal disease in the zoonotic pathogen Streptococcus suis.Nature communications · 2015Article
- Mucin glycan foraging in the human gut microbiome.Frontiers in genetics · 2015Review
- Enhancement of biological reactions on cell surfaces via macromolecular crowding.Nature communications · 2014Article
- The hypothesis on function of glycosphingolipids and ABO blood groups revisited.Neurochemical research · 2012Review
- Article
- Structure of the fucose mutarotase from Streptococcus pneumoniae in complex with L-fucose.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Analysis of a new family of widely distributed metal-independent alpha-mannosidases provides unique insight into the processing of N-linked glycans.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The presence of a fucose utilization operon in the Streptococcus pneumoniae genome and its established importance in virulence indicates a reliance of this bacterium on the harvesting of host fucose-containing glycans. The identities of these glycans, however, and how they are harvested is presently unknown. The biochemical and high resolution x-ray crystallographic analysis of two family 98 glycoside hydrolases (GH98s) from distinctive forms of the fucose utilization operon that originate from different S. pneumoniae strains reveal that one enzyme, the predominant type among pneumococcal isolates, has a unique endo-beta-galactosidase activity on the LewisY antigen. Altered active site topography in the other species of GH98 enzyme tune its endo-beta-galactosidase activity to the blood group A and B antigens. Despite their different specificities, these enzymes, and by extension all family 98 glycoside hydrolases, use an inverting catalytic mechanism. Many bacterial and viral pathogens exploit host carbohydrate antigens for adherence as a precursor to colonization or infection. However, this is the first evidence of bacterial endoglycosidase enzymes that are known to play a role in virulence and are specific for distinct host carbohydrate antigens. The strain-specific distribution of two distinct types of GH98 enzymes further suggests that S. pneumoniae strains may specialize to exploit host-specific antigens that vary from host to host, a factor that may feature in whether a strain is capable of colonizing a host or establishing an invasive infection.
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