The Amino Acid Nutrition of Group a Hemolytic Streptococci, With Reference to the Effect of Glutathione on the Cystine Requirement

Slade, Hutton D.; Knox, Grace A.; Slamp, William C.

doi:10.1128/jb.62.5.669-675.1951

Cited by 18 publications

(12 citation statements)

References 11 publications

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“…At the same time, the possible physiological role of glutathione in Gram-positive bacteria has been described in a variety of settings. For instance, as a mediumsupplement supporting growth in Lactococcus lactis, Lactobacillus casei, S. agalactiae, S. bovis, S. pyogenes, and S. mutans (Slade et al, 1951;Prescott, 1961;Brown, 1974;Sherrill and Fahey, 1998;Pophaly et al, 2012), as a protective agent for oxidative-, acid-, and osmotic stress in L. lactis and S. mutans (Korithoski et al, 2007;Zhang et al, 2010), and as a molecular factor contributing to virulence in Listeria monocytogenes, S. pyogenes, and S. pneumoniae (Brenot et al, 2004;Gopal et al, 2005;Stroeher et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Molecular and structural basis of glutathione import in Gram‐positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans

Vergauwen

Verstraete

Senadheera

et al. 2013

Molecular Microbiology

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SummaryGlutathione (GSH) protects cells against oxidative injury and maintains a range of vital functions across all branches of life. Despite recent advances in our understanding of the transport mechanisms responsible for maintaining the spatiotemporal homeostasis of GSH and its conjugates in eukaryotes and Gram-negative bacteria, the molecular and structural basis of GSH import into Gram-positive bacteria has remained largely uncharacterized. Here, we employ genetic, biochemical and structural studies to investigate a possible glutathione import axis in Streptococcus mutans, an organism that has hitherto served as a model system. We show that GshT, a type 3 solute binding protein, displays physiologically relevant affinity for GSH and glutathione disulfide (GSSG). The crystal structure of GshT in complex with GSSG reveals a collapsed structure whereby the GS-Ileg of GSSG is accommodated tightly via extensive interactions contributed by the N-and C-terminal lobes of GshT, while the GS-II leg extends to the solvent. This can explain the ligand promiscuity of GshT in terms of binding glutathione analogues with substitutions at the cysteine-sulfur or the glycine-carboxylate. Finally, we show that GshT primes glutathione import via the L-cystine ABC transporter TcyBC, a membrane permease, which had previously exclusively been associated with the transport of L-cystine.

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Section: Introductionmentioning

confidence: 99%

Molecular and structural basis of glutathione import in Gram‐positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans

Vergauwen

Verstraete

Senadheera

et al. 2013

Molecular Microbiology

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“…Later, Sprince and Woolley reported the requirement of a factor, subsequently termed strepogenin (22), for growth in a casein hydrolysate basal medium (28). Two partially defined media that were described by Slade and co-workers contained a nondialyzable polypeptide from pancreatic digest of casein (19) or heated ovalbumin (20) in an otherwise chemically defined medium (CDM). Ogburn et al (18), while studying the production of protease, were able to obtain a low yield of organisms from a chemically defined medium after sequential reduction of casein hydrolysate.…”

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confidence: 99%

Growth characteristics of group A streptococci in a new chemically defined medium

Rijn¹,

Kessler²

1980

Infect Immun

441

145

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A new chemically defined medium for the growth of group A streptococci has been formulated. The advantages of this new medium over previously described defined media are: (i) rates of growth (i.e., doubling times) of 20 strains were comparable to the rates of growth in complex media; (ii) each strain grew to a higher culture density in the new defined medium than in complex media; (iii) transfer from complex media with small inocula was possible without any prior adaptation regimen; and (iv) the production of virulence factors (i.e., M protein and hyaluronic acid) and extracellular enzymes during growth in this new medium was comparable to that in complex media.

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“…g . Slade & K n o x (1950), Slade et al (1951), Fox (1961), Mickelson (1964). These substances should be present in the growth medium employed in the present study in sufficient concentration ( H o l m & Falsen 1967), and should not be limiting for the S 1 0 formation, but more detailed studies will be performed on this aspect.…”

Section: Discussionmentioning

confidence: 99%

“…In laboratories performing this test the production of streptolysin 0 (90) of acceptable activity and storability is therefore a current problem. Although the factors essential for the cultivation of beta-hemolytic streptococci and the production of streptolysin 0 have been studied by many authors ( M c l l w a i n 1946, Bernheimer & Pappenheimer 1942, Slade & K n o x 1950, Zampieri et al 1960, Slade et al 1951, Fox 1961and Mickelson 1964 most of the growth media commonly employed for S 1 0 production e.g. the Todd-Hewitt broth ( T o d d & Hewitt 1932) are lacking one or the other of these growth factors.…”

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confidence: 99%

THE FORMATION OF STREPTOLYSIN O UNDER STABILIZED pH CONDITIONS

Holm

Möller

1971

Acta Pathologica Microbiologica Scandinavica Section B Microbio

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Employing a system for continued pH adjustment and a growth medium cohtaining factors essential for streptococcal g o w t h and SI 0 production, the formation of Sl 0 at different growth phases was studied. The S1 0 formed during the early phase of exponential growth could not be completely neutralized by its corresponding' antibody thus indicating a lack of or a lower antigenicity of this streptolysin. The mechanism for S1 0 formation is probably an active process where a feed back system might be involved.

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The Amino Acid Nutrition of Group a Hemolytic Streptococci, With Reference to the Effect of Glutathione on the Cystine Requirement

Cited by 18 publications

References 11 publications

Molecular and structural basis of glutathione import in Gram‐positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans

Molecular and structural basis of glutathione import in Gram‐positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans

Growth characteristics of group A streptococci in a new chemically defined medium

THE FORMATION OF STREPTOLYSIN O UNDER STABILIZED pH CONDITIONS

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