Unravelling the Multiple Functions of the Architecturally Intricate β-galactosidase, BgaA

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The adherence of bacteria to host cells is a critical step in most bacterial infections; yet, mechanisms are poorly understood for many bacteria, including Streptococcus pneumoniae (pneumococcus), a human pathogen of global relevance. The surface of this bacterium is decorated with a landscape of large and structurally sophisticated proteins that mediate contact with the host. Here we show that the sugar-degrading β-galactosidase BgaA, can bind and cleave sugars through separate portions of this protein, which is one of the largest pneumococcal surface proteins and a model for architecturally intricate carbohydrate-active surface proteins. Non-enzymatic carbohydrate-binding modules in BgaA mediate adherence to specific host-cell surface carbohydrates. The identification of the first adhesin-carbohydrate receptor pair in S. pneumoniae provides critical molecular-level support for the long-held hypothesis that pneumococci bind carbohydrates on host cells and extends the paradigm of carbohydrate-binding module function. The enzymatically active portion of BgaA enables the bacterium to grow on host-derived glycans and evade the immune system, aspects of the host-pathogen interaction we show can be modulated by a specific inhibitor of enzymatic activity. Our work advances the concept that large bacterial surface proteins mediate complex host-bacterial interactions through specific functions of the varied regions comprising these proteins.

Vyšlo v časopise: Unravelling the Multiple Functions of the Architecturally Intricate β-galactosidase, BgaA. PLoS Pathog 10(9): e32767. doi:10.1371/journal.ppat.1004364
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004364

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