Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 401349
Title ApuA, a multifunctional x-glucan-degrading enzyme of Streptococcus suis, mediates adhesion to porcine epithelium and mucus
Author(s) Ferrando, M.L.; Fuentes, S.; Greeff, A. de; Smith, H.E.; Wells, J.
Source Microbiology 156 (2010). - ISSN 1350-0872 - p. 2818 - 2828.
Department(s) Host Microbe Interactomics
Laboratory of Virology
CVI Infection Biology
Publication type Refereed Article in a scientific journal
Publication year 2010
Keyword(s) group-a streptococcus - gram-positive bacteria - toxic-shock-syndrome - germ-free pigs - actinobacillus-actinomycetemcomitans - nasopharyngeal colonization - molecular characterization - staphylococcus-aureus - vaccine development - gene inactivation
Abstract We have identified apuA in Streptococcus suis, which encodes a bifunctional amylopullulanase with conserved -amylase and pullulanase substrate-binding domains and catalytic motifs. ApuA exhibited properties typical of a Gram-positive surface protein, with a putative signal sequence and LPKTGE cell-wall-anchoring motif. A recombinant protein containing the predicted N-terminal -amylase domain of ApuA was shown to have -(1,4) glycosidic activity. Additionally, an apuA mutant of S. suis lacked the pullulanase -(1,6) glycosidic activity detected in a cell-surface protein extract of wild-type S. suis. ApuA was required for normal growth in complex medium containing pullulan as the major carbon source, suggesting that this enzyme plays a role in nutrient acquisition in vivo via the degradation of glycogen and food-derived starch in the nasopharyngeal and oral cavities. ApuA was shown to promote adhesion to porcine epithelium and mucus in vitro, highlighting a link between carbohydrate utilization and the ability of S. suis to colonize and infect the host.
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