A streptolysin S homologue is essential for β-haemolytic Streptococcus constellatus subsp. constellatus cytotoxicity

Tabata, Atsushi; Sato, Yuji; Maya, Kentaro; Nakano, Kota; Kikuchi, Ken; Whiley, Robert A.; Ohkura, Kazuto; Tomoyasu, Toshifumi; Nagamune, Hideaki

doi:10.1099/mic.0.075580-0

Cited by 13 publications

(21 citation statements)

References 37 publications

(45 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…pharyngis SK1060 and S. constellatus subsp. viborgensis SK1359 (Tabata et al, ). In line with this published data, several independent observations support the hypothesis of SLS acquisition via horizontal gene transfer for S. anginosus .…”

Section: Discussionmentioning

confidence: 99%

Heterogeneity of Streptococcus anginosus ß‐hemolysis in relation to CRISPR/Cas

Bauer

Neffgen

Grempels

et al. 2020

Molecular Oral Microbiology

View full text Add to dashboard Cite

Streptococcus anginosus is a commensal of the oral mucosa that can cause severe invasive infections. A considerable proportion of Streptococcus anginosus strains are ß‐hemolytic due to the presence of an SLS‐like gene cluster. However, the majority of strains do not display ß‐hemolysis. To investigate ß‐hemolysin heterogeneity in S. anginosus, we determined the presence of sag genes and correlated it with the presence of CRISPR/Cas genes in a collection of ß‐hemolytic and non‐ß‐hemolytic strains. All of the ß‐hemolytic strains carried the sag gene cluster. In contrast to other streptococci, clinical S. anginosus strains that do not display ß‐hemolysis do not harbor sag genes. Phylogenetic analysis of the ß‐hemolytic strains revealed that they belong to two previously defined clusters within S. anginosus. Correlation with CRISPR/Cas genes showed a significant difference for the presence of CRISPR/Cas in ß‐hemolytic versus non‐ß‐hemolytic isolates. The presence of the CRISPR/Cas type IIA or type IIC locus is associated with the absence of sag genes; in 65% of the non‐ß‐hemolytic strains a CRISPR/Cas locus was found, while only 24% of ß‐hemolytic strains carry CRISPR/Cas genes. Further analysis of the spacer content of the CRISPR systems revealed the presence of multiple self‐targeting sequences directed against S. anginosus genes. These results support the hypothesis that horizontal gene transfer is involved in the acquisition of ß‐hemolysin genes and that CRISPR/Cas may limit DNA uptake in S. anginosus.

show abstract

Section: Discussionmentioning

confidence: 99%

Heterogeneity of Streptococcus anginosus ß‐hemolysis in relation to CRISPR/Cas

Bauer

Neffgen

Grempels

et al. 2020

Molecular Oral Microbiology

View full text Add to dashboard Cite

show abstract

“…We have been investigating the pathogenic potential of β-hemolytic AGS, and had revealed that SLS is the sole hemolytic factor of the β-hemolytic AGS, except in S. intermedius that secretes the protein hemolysin intermedilysin [10,12]. In addition, we had revealed that the β-hemolytic S. constellatus subsp.…”

Section: Discussionmentioning

confidence: 99%

“…However, we had reported previously that the culture supernatant of the β-hemolytic S. constellatus subsp. constellatus strain W277 showed cytotoxicity to the human hepatocellular carcinoma cell culture line HepG2 [12]. Moreover, in our investigation on the SLS from β-hemolytic AGS strains, we had not ruled out the cytotoxic potential of the SLS secreted from these strains.…”

mentioning

confidence: 85%

“…Based on the results from our laboratory and those of other research groups, two kinds of βhemolytic factors were reported for AGS. One is the intermedilysin, a protein hemolysin belonging to the family of cholesterol-dependent cytolysins (CDCs) secreted by S. intermedius [9], and the other is the streptolysin S (SLS), a peptide hemolysin produced by β-hemolytic AGS except S. intermedius [10][11][12]. SLS has been a long-established peptide hemolysin secreted from a human pathogen strain of S. pyogenes [13,14], and is reported to be produced as a post-translationally modified product from the precursor encoded by the sag operon on the AGS genome.…”

mentioning

confidence: 99%

“…For the SLS secreted from the β-hemolytic AGS strains, their function as the hemolytic factor was reported for β-SAA and other β-hemolytic AGS strains [10][11][12]. However, the cytotoxic potential of the SLS from β-SAA is still inconclusive.…”

mentioning

confidence: 99%

See 2 more Smart Citations

β-Hemolytic Streptococcus anginosus subsp. anginosus causes streptolysin S-dependent cytotoxicity to human cell culture lines in vitro

Tabata

Yamada

Ohtani

et al. 2019

Journal of Oral Microbiology

Self Cite

View full text Add to dashboard Cite

Background: Streptococcus anginosus subsp. anginosus (SAA) is one of the opportunistic pathogens in humans that inhabits the oral cavity. The type strain of SAA, NCTC10713 T , showed clear β-hemolysis on blood agar plates, and the sole β-hemolytic factor revealed two streptolysin S (SLS) molecules. SLS is well known as the peptide hemolysin produced from the human pathogen S. pyogenes and shows not only hemolytic activity on erythrocytes but also cytotoxic activity in cell culture lines in vitro and in vivo, such as in a mouse infection model. However, no cytotoxic activity of SLS produced from β-hemolytic SAA (β-SAA) has been reported so far. Objective and Design: In this study, the SLS-dependent cytotoxicity of the β-SAA strains including the genetically modified strains was investigated in vitro. Results: The SLS-producing β-SAA showed cytotoxicity in human cell culture lines under the co-cultivation condition and it was found that this cytotoxicity was caused by the SLS secreted into the extracellular milieu. Conclusion: The results from this study suggest that the SLS produced from β-SAA might indicate the cytotoxic potential similar to that of the SLS from S. pyogenes and the SLS-producing β-SAA would be recognized as "a wolf in sheep's clothing" More attention will be paid to the pathogenicity of β-hemolytic Anginosus group streptococci.

show abstract

Streptolysin S of Streptococcus anginosus exhibits broad-range hemolytic activity

Asam

Mauerer

Spellerberg

2014

Med Microbiol Immunol

View full text Add to dashboard Cite

Streptococcus anginosus is a commensal of mucous membranes and an emerging human pathogen. Some strains, including the type strain, display a prominent β-hemolytic phenotype. A gene cluster (sag), encoding a variant of streptolysin S (SLS) has recently been identified as the genetic background for β-hemolysin production in S. anginosus. In this study, we further characterized the hemolytic and cytolytic activity of the S. anginosus hemolysin in comparison with other streptococcal hemolysins. The results indicate that SLS of S. anginosus is a broad-range hemolysin able to lyse erythrocytes of different species, including horse, bovine, rabbit and even chicken. The hemolytic activity is temperature dependent, and a down-regulation of the hemolysin expression is induced in the presence of high glucose levels. Survival assays indicate that in contrast to other streptococcal species, S. anginosus does not require SLS for survival in the presence of human granulocytes. Cross-complementation studies using the sagB and sagD genes of Streptococcus pyogenes and Streptococcus dysgalactiae subsp. equisimilis demonstrated functional similarities to the S. anginosus SLS. Nevertheless, distinct differences to other streptolysin S variants were noted and provide further insights into the molecular mechanisms of SLS pathogen host interactions.

show abstract

A streptolysin S homologue is essential for β-haemolytic Streptococcus constellatus subsp. constellatus cytotoxicity

Cited by 13 publications

References 37 publications

Heterogeneity of Streptococcus anginosus ß‐hemolysis in relation to CRISPR/Cas

Heterogeneity of Streptococcus anginosus ß‐hemolysis in relation to CRISPR/Cas

β-Hemolytic Streptococcus anginosus subsp. anginosus causes streptolysin S-dependent cytotoxicity to human cell culture lines in vitro

Streptolysin S of Streptococcus anginosus exhibits broad-range hemolytic activity

Contact Info

Product

Resources

About