Oxygen-Stable Hemolysins of Group a Streptococci

Ginsburg, Isaac; Harris, T. N.

doi:10.1084/jem.118.6.919

Cited by 26 publications

(13 citation statements)

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“…125, 126 Despite these challenges, analysis of crude preparations indicated that the active component of SLS was a peptide. 127–130 However, it was not until the year 2000 that transposon mutagenesis and DNA sequencing studies 131, 132 revealed that SLS was a RiPP. 133, 134 These genomic studies demonstrated that nine genes, sagABCDEFGHI , comprised the SLS operon (Figure 6).…”

Section: Linear Azole-containing Peptides (Laps)mentioning

confidence: 99%

YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function

et al. 2017

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With advances in sequencing technology, uncharacterized proteins and domains of unknown function (DUFs) are rapidly accumulating in sequence databases and offer an opportunity to discover new protein chemistry and reaction mechanisms. The focus of this review, the formerly enigmatic YcaO superfamily (DUF181), has been found to catalyze a unique phosphorylation of a ribosomal peptide backbone amide upon attack by different nucleophiles. Established nucleophiles are the side chains of Cys, Ser, and Thr which gives rise to azoline/azole biosynthesis in ribosomally synthesized and posttranslationally modified peptide (RiPP) natural products. However, much remains unknown about the potential for YcaO proteins to collaborate with other nucleophiles. Recent work suggests potential in forming thioamides, macroamidines, and possibly additional post-translational modifications. This review covers all knowledge through mid-2016 regarding the biosynthetic gene clusters (BGCs), natural products, functions, mechanisms, and applications of YcaO proteins and outlines likely future research directions for this protein superfamily.

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Section: Linear Azole-containing Peptides (Laps)mentioning

confidence: 99%

YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function

et al. 2017

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“…First, in experiments reported elsewhere in these studies it was found, after incubation of RNA hemolysin with tween and the subsequent resolution of the mixtures by DEAE cellulose chromatography, that the fraction containing the tween, which had 70 per cent of the hemolytic activity after the incubation, was not contaminated with RNA, within the limits of detection of the orcinol method (11). Second, in experiments reported recently by Egami and Koyama (12), RNA hemolysin labeled with C 14 amino acids was incubated with tween 40 and the mixture was resolved on DEAE cellulose.…”

Section: Discussionmentioning

confidence: 94%

Oxygen-Stable Hemolysins of Group a Streptococci

Ginsburg

Harris

1965

The Journal of Experimental Medicine

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In the previous paper (1) data were presented on the relationship of the cellbound hemolysin (CBtI) of a Group A streptococci to the oxygen-stable hemolysin produced by these organisms in the presence of RNA. It was shown that a number of agents and conditions affected similarly the formation and activity of the cell-bound and RNA-induced hemolysins. The fact that (in the absence of an effective inducer of the oxygen-stable hemolysins, such as RNA) no traces of soluble hemolysin can be detected in the suspending medium of washed streptococci even with high CBH activity suggested that in the absence of such an inducer a hemolytic moiety can be transferred directly from the streptococci to the red cells, as has, in fact, been indicated in a preliminary report (1). The hemolysin thus transferred would act on some cell membrane component to cause the permeability changes which result in the lysis of the cells. However, the actual mechanism of lysis of red blood cells (RBC) and other mammalian cells by CBH (2) and the oxygen-stable streptococcal hemolysins is not understood.In the present paper experiments on the mechanism of lysis of red blood cells by washed streptococci possessing CBH activity are reported, and a proposed relationship between the CBH and the group of streptococcal oxygen-stable hemolysins is presented. Materials and MethodsThe streptococcal strain, culture media, and the preparation and titration of RNA and the cell-bound hemolysin were described in a preceding paper (1). Group O human red blood cells were used throughout.

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“…These apparently para doxical effects are explicable by mutal transfer of SLS polypeptide among carrier substances [17,18]. Thus, after synthesis, the toxin polypeptide is tran sported into cell envelope and probably bound to an endogenous carrier site, transiently [19,20], U pon incubation with AF or azo dye having higher affin ity, SLS is transferred to exogenous carrier and se creted into m edium as the active exotoxin complex.…”

Section: Discussionmentioning

confidence: 99%

Effects of Trypan Blue and Related Compounds on Production and Activity of Streptolysin S

Taketo

1982

Zeitschrift Für Naturforschung C

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Streptolysin S, Trypan Blue, Hemolysis, Streptococcus pyogenesMost dyes related to trypan blue inhibited hemolytic activity of oligonucleotide-streptolysin S (SLS) complex, an exotoxin produced by Streptococcus pyogenes. Order of the inhibition was: trypan blue > benzo blue 2B > Congo red > Evans blue > benzo purpurine 4B > thiazine red > trypan red. When resting streptococcal cells were incubated with these dyes, significant amount of the hemolysin was produced. The carrier (or inducing) activity for SLS was further manifested in growing cell system and the potency of the compounds was as follows: Congo red > benzo blue 2B > trypan blue > Evans blue > Benzo purpurine 4B > thiazine red > trypan red. In this system, Congo red was more effective than oligonucleotide fraction rich in guanyl residue. Chromotrope 2B, H acid and o-tolidine were ineffective, as the carrier as well as the inhibitor. Based on these results, structure-function relationship among SLS, the carrier and the inhibitor was discussed.

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Oxygen-Stable Hemolysins of Group a Streptococci

Cited by 26 publications

References 10 publications

YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function

YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function

Oxygen-Stable Hemolysins of Group a Streptococci

Effects of Trypan Blue and Related Compounds on Production and Activity of Streptolysin S

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