title: Dynamics of the Streptococcus gordonii Transcriptome in Response to Medium, Salivary α-Amylase, and Starch.
abstract: Streptococcus gordonii, a primary colonizer of the tooth surface, interacts with salivary α-amylase via amylase-binding protein A (AbpA). This enzyme hydrolyzes starch to glucose, maltose, and maltodextrins that can be utilized by various oral bacteria for nutrition. Microarray studies demonstrated that AbpA modulates gene expression in response to amylase, suggesting that the amylase-streptococcal interaction may function in ways other than nutrition. The goal of this study was to explore the role of AbpA in gene regulation through comparative transcriptional profiling of wild-type KS1 and AbpA(-) mutant KS1ΩabpA under various environmental conditions. A portion of the total RNA isolated from mid-log-phase cells grown in 5% CO2 in (i) complex medium with or without amylase, (ii) defined medium (DM) containing 0.8% glucose with/without amylase, and (iii) DM containing 0.2% glucose and amylase with or without starch was reverse transcribed to cDNA and the rest used for RNA sequencing. Changes in the expression of selected genes were validated by quantitative reverse transcription-PCR. Maltodextrin-associated genes, fatty acid synthesis genes and competence genes were differentially expressed in a medium-dependent manner. Genes in another cluster containing a putative histidine kinase/response regulator, peptide methionine sulfoxide reductase, thioredoxin protein, lipoprotein, and cytochrome c-type protein were downregulated in KS1ΩabpA under all of the environmental conditions tested. Thus, AbpA appears to modulate genes associated with maltodextrin utilization/transport and fatty acid synthesis. Importantly, in all growth conditions AbpA was associated with increased expression of a potential two-component signaling system associated with genes involved in reducing oxidative stress, suggesting a role in signal transduction and stress tolerance.
authors.affiliation: Department of Oral Biology, School of Dental Medicine, University at Buffalo, State University of New York, Buffalo, New York, USA.
authors.forename: Elaine M
authors.initials: EM
authors.lastname: Haase
authors.affiliation: Department of Oral Biology, School of Dental Medicine, University at Buffalo, State University of New York, Buffalo, New York, USA.
authors.forename: Xianghui
authors.initials: X
authors.lastname: Feng
authors.affiliation: Department of Oral Biology, School of Dental Medicine, University at Buffalo, State University of New York, Buffalo, New York, USA.
authors.forename: Jiachuan
authors.initials: J
authors.lastname: Pan
authors.affiliation: Department of Biostatistics, School of Public Health and Health Professions, University at Buffalo, State University of New York, Buffalo, New York, USA.
authors.forename: Jeffrey C
authors.initials: JC
authors.lastname: Miecznikowski
authors.affiliation: Department of Oral Biology, School of Dental Medicine, University at Buffalo, State University of New York, Buffalo, New York, USA fas1@buffalo.edu.
authors.forename: Frank A
authors.initials: FA
authors.lastname: Scannapieco
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism; D003470:Culture Media / Q000378:metabolism*; D017353:Gene Deletion; D020869:Gene Expression Profiling; D060888:Real-Time Polymerase Chain Reaction; D055291:Salivary alpha-Amylases / Q000378:metabolism*; D017423:Sequence Analysis, RNA; D013213:Starch / Q000378:metabolism*; D054773:Streptococcus gordonii / Q000187:drug effects* / Q000235:genetics*
chemical_list: C112818:AbpA protein, Streptococcus gordonii; D001425:Bacterial Outer Membrane Proteins; D003470:Culture Media; D013213:Starch; D055291:Salivary alpha-Amylases