title: Capsule expression in Streptococcus mitis modulates interaction with oral keratinocytes and alters susceptibility to human antimicrobial peptides.
abstract: Streptococcus mitis is a colonizer of the oral cavity and the nasopharynx, and is closely related to Streptococcus pneumoniae. Both species occur in encapsulated and unencapsulated forms, but in S. mitis the role of the capsule in host interactions is mostly unknown. Therefore, the aim of this study was to examine how capsule expression in S. mitis can modulate interactions with the host with relevance for colonization. The S. mitis type strain, as well as two mutants of the type strain, an isogenic capsule deletion mutant, and a capsule switch mutant expressing the serotype 4 capsule of S. pneumoniae TIGR4, were used. Wild-type and capsule deletion strains of S. pneumoniae TIGR4 were included for comparison. We found that capsule production in S. mitis reduced adhesion to oral and lung epithelial cells. Further, exposure of oral epithelial cells to encapsulated S. mitis resulted in higher interleukin-6 and CXCL-8 transcription levels relative to the unencapsulated mutant. Capsule expression in S. mitis increased the sensitivity to human neutrophil peptide 1-3 but reduced the sensitivity to human β-defensin-3 and cathelicidin. This was in contrast with S. pneumoniae in which capsule expression has been generally associated with increased sensitivity to human antimicrobial peptides (AMPs). Collectively, these findings indicate that capsule expression in S. mitis is important in modulating interactions with epithelial cells, and is associated with increased or reduced susceptibility to AMPs depending on the nature of the AMP.
authors.affiliation: Department of Oral Biology, Faculty of Dentistry, University of Oslo, Norway.
authors.forename: H V
authors.initials: HV
authors.lastname: Rukke
authors.affiliation: Department of Oral Biology, Faculty of Dentistry, University of Oslo, Norway.
authors.forename: S A
authors.initials: SA
authors.lastname: Engen
authors.affiliation: Department of Oral Biology, Faculty of Dentistry, University of Oslo, Norway.
authors.forename: K
authors.initials: K
authors.lastname: Schenck
authors.affiliation: Department of Oral Biology, Faculty of Dentistry, University of Oslo, Norway.
authors.forename: F C
authors.initials: FC
authors.lastname: Petersen
mesh_terms: D000890:Anti-Infective Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D001422:Bacterial Adhesion; D016667:Bacterial Capsules / Q000187:drug effects* / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D054804:Cathelicidins / Q000494:pharmacology; D045744:Cell Line, Tumor; D004847:Epithelial Cells / Q000276:immunology / Q000382:microbiology; D006801:Humans; D015850:Interleukin-6 / Q000235:genetics; D016209:Interleukin-8 / Q000235:genetics; D015603:Keratinocytes / Q000276:immunology / Q000382:microbiology*; D009055:Mouth / Q000166:cytology* / Q000276:immunology / Q000382:microbiology; D009154:Mutation; D034361:Streptococcus mitis / Q000166:cytology* / Q000187:drug effects* / Q000235:genetics / Q000276:immunology; D013296:Streptococcus pneumoniae / Q000166:cytology / Q000235:genetics / Q000276:immunology / Q000502:physiology; D023084:alpha-Defensins / Q000494:pharmacology*; D023083:beta-Defensins / Q000494:pharmacology
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; C508606:CXCL8 protein, human; D054804:Cathelicidins; C508600:IL6 protein, human; D015850:Interleukin-6; D016209:Interleukin-8; D023084:alpha-Defensins; D023083:beta-Defensins; C406413:human neutrophil peptide 1; C406416:human neutrophil peptide 2; C406427:human neutrophil peptide 3
keywords: Streptococcus; Streptococcus mitis; Streptococcus pneumoniae; capsule; human antimicrobial peptides