Evidence for the presence of two distinct phosphoenolpyruvate: Mannose phosphotransferase systems in Streptococcus mutans GS5-2

Néron, Sonia

doi:10.1016/0378-1097(87)90489-7

Cited by 4 publications

(7 citation statements)

References 7 publications

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“…Growth in 0.2% mannose was faster for JAM1 (doubling time Х180 min) than for the wild-type strain (doubling time Х255 min). This finding is in contrast with that reported for S. mutans GS-5, in which a spontaneously arising EII Man -deficient strain grew more slowly than the parent in glucose but growth in mannose was unaffected (23,24). Of note, no significant differences in growth rates were observed between the wild-type strain and JAM1 when 0.2% fructose was used as the sole carbohydrate source (Table 2).…”

Section: Characteristics Of Eiiabcontrasting

confidence: 86%

Characterization of Streptococcus mutans Strains Deficient in EIIAB ^Man of the Sugar Phosphotransferase System

Abranches

Chen

Burne

2003

Appl Environ Microbiol

107

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The phosphoenolpyruvate:sugar phosphotransferase system (PTS) is the major sugar uptake system in oral streptococci. The role of EIIAB Man (encoded by manL) in gene regulation and sugar transport was investigated in Streptococcus mutans UA159. The manL knockout strain, JAM1, grew more slowly than the wild-type strain in glucose but grew faster in mannose and did not display diauxic growth, indicating that EIIAB Man is involved in sugar uptake and in carbohydrate catabolite repression. PTS assays of JAM1, and of strains lacking the inducible (fruI) and constitutive (fruCD) EII fructose, revealed that S. mutans EIIAB Man transported mannose and glucose and provided evidence that there was also a mannose-inducible or glucose-repressible mannose PTS. Additionally, there appears to be a fructose PTS that is different than FruI and FruCD. To determine whether EIIAB Man controlled expression of the known virulence genes, glucosyltransferases (gtfBC) and fructosyltransferase (ftf) promoter fusions of these genes were established in the wild-type and EIIAB Man -deficient strains. In the manL mutant, the level of chloramphenicol acetyltransferase activity expressed from the gtfBC promoter was up to threefold lower than that seen with the wild-type strain at pH 6 and 7, indicating that EIIAB Man is required for optimal expression of gtfBC. No significant differences were observed between the mutant and the wild-type background in ftf regulation, with the exception that under glucose-limiting conditions at pH 7, the mutant exhibited a 2.1-fold increase in ftf expression. Two-dimensional gel analysis of batch-grown cells of the EIIAB Man -deficient strain indicated that the expression of at least 38 proteins was altered compared to that seen with the wild-type strain, revealing that EIIAB Man has a pleiotropic effect on gene expression.Oral streptococci depend on dietary carbohydrates and carbohydrates presented in oral secretions for growth and persistence in the mouth. The ability of oral streptococci to metabolize a wide variety of carbohydrates to produce organic acids is directly related to their ability to elicit dental caries. The phosphoenolpyruvate (PEP):sugar phosphotransferase system (PTS) is the primary sugar transport system in oral streptococci, especially under carbohydrate-limiting conditions, and plays important roles in global control of gene expression (20,29,30,37,38). The PTS consists of two proteins that are common to all PTS substrates, enzyme I (EI) and the heatstable phosphocarrier protein HPr, as well as a variety of sugar-specific permeases, known as EII complexes, which catalyze the transport and concomitant phosphorylation of the substrate. The EII complexes usually consist of three domains, A, B, and C, but sometimes a fourth domain, D, is required (20, 29). The A and B domains participate in phosphorylation of the cognate substrates, whereas the C and D domains comprise the membrane permeases. The EII domains can either be covalently linked as a single protein or can be present in various combi...

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Section: Characteristics Of Eiiabcontrasting

confidence: 86%

Characterization of Streptococcus mutans Strains Deficient in EIIAB ^Man of the Sugar Phosphotransferase System

Abranches

Chen

Burne

2003

Appl Environ Microbiol

107

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“…These results suggested that strain GM500 was defective at the level of the mannose PTS and possessed a distinct glucose PTS that could transport glucose into the cell. The presence of a second inducible mannose PTS recently discovered in S. mutans GS5-2 might explain the fact that strain GM500 grew well on mannose (see Table 1) (23). The results of PTS activities obtained with strains 27352 and MM202 also indicated that the mutant strain MM202 was affected at the level of the mannose PTS, but possessed a distinct glucose PTS ( Table 2).…”

Section: Glucose Is Transported By Two Phosphoenoipyruvate: Phosphotrmentioning

confidence: 85%

Two functionally different glucose phosphotransferase transport systems in Streptococcus mutans and Streptococcus sobrinus

Néron

Vadeboncoeur

1987

Oral Microbiology and Immunology

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Spontaneous phosphotransferase negative mutants of Streptococcus mutans GS5‐2 (mutant GM500) and of Streptococcus sobrinus 27352 (mutant MM202) were isolated by screening for 2‐deoxyglucose resistance using lactose as the growth substrate. Measurements of phosphoenolpyruvate: phosphotransferase activities with isolated membranes and purified Enzyme I and HPr indicated that the mutant strains were defective at the level of membrane components of the phosphoenolpyruvate: mannose phosphotranferase system but still possessed phosphoenolpyruvate: glucose phosphotransferase activity. These results were corroborated by uptake studies performed with resting cells. Our results suggest that glucose is transported by 2 distinct phosphoenolpyruvate: phosphotransferase systems in S. mutans and S. sobrinus, one of which is also capable of transporting mannose. This glucose‐mannose transport system is involved in catabolite repression and inducer exclusion, and controls, by way of these mechanisms, the metabolism of lactose.

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“…For example, in L. lactis glucose can be imported via the mannose or cellobiose PTSs or the glucose permease GlcU (Castro et al, 2009). In S. mutans alone, PTS systems have been identified for glucose (Schachtele & Mayo, 1973), mannitol, glucitol (Brown & Wittenberger, 1973;Maryanski & Wittenberger, 1975), lactose (Calmes, 1978), sucrose (Slee & Tanzer, 1979;St Martin & Wittenberger, 1979), mannose (Vadeboncoeur, 1984;Néron & Glucose is either internalized and concomitantly phosphorylated the PTS systems (PtcABC or PtnABCD) or imported by the GlcU permease and phosphorylated by glucose kinase. PTS systems are represented by circles, while non-PTS sugar import systems are represented by squares.…”

Section: Sugar Importmentioning

confidence: 99%

“…Nomenclature used is for Lactococcus lactis. Vadeboncoeur, 1987), fructose (Gauthier et al, 1984a, b), maltose (Würsch & Koellreutter, 1985), and trehalose (Poy & Jacobson, 1990).…”

Section: Sugar Importmentioning

confidence: 99%

From meadows to milk to mucosa – adaptation ofStreptococcusandLactococcusspecies to their nutritional environments

Zeyniyev

Kuipers

et al. 2012

FEMS Microbiol Rev

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Lactic acid bacteria (LAB) are indigenous to food-related habitats as well as associated with the mucosal surfaces of animals. The LAB family Streptococcaceae consists of the genera Lactococcus and Streptococcus. Members of the family include the industrially important species Lactococcus lactis, which has a long history safe use in the fermentative food industry, and the disease-causing streptococci Streptococcus pneumoniae and Streptococcus pyogenes. The central metabolic pathways of the Streptococcaceae family have been extensively studied because of their relevance in the industrial use of some species, as well as their influence on virulence of others. Recent developments in high-throughput proteomic and DNA-microarray techniques, in in vivo NMR studies, and importantly in whole-genome sequencing have resulted in new insights into the metabolism of the Streptococcaceae family. The development of cost-effective high-throughput sequencing has resulted in the publication of numerous whole-genome sequences of lactococcal and streptococcal species. Comparative genomic analysis of these closely related but environmentally diverse species provides insight into the evolution of this family of LAB and shows that the relatively small genomes of members of the Streptococcaceae family have been largely shaped by the nutritionally rich environments they inhabit.

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Evidence for the presence of two distinct phosphoenolpyruvate: Mannose phosphotransferase systems in Streptococcus mutans GS5-2

Cited by 4 publications

References 7 publications

Characterization of Streptococcus mutans Strains Deficient in EIIAB ^Man of the Sugar Phosphotransferase System

Characterization of Streptococcus mutans Strains Deficient in EIIAB ^Man of the Sugar Phosphotransferase System

Two functionally different glucose phosphotransferase transport systems in Streptococcus mutans and Streptococcus sobrinus

From meadows to milk to mucosa – adaptation ofStreptococcusandLactococcusspecies to their nutritional environments

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Evidence for the presence of two distinct phosphoenolpyruvate: Mannose phosphotransferase systems in Streptococcus mutans GS5-2

Cited by 4 publications

References 7 publications

Characterization of Streptococcus mutans Strains Deficient in EIIAB Man of the Sugar Phosphotransferase System

Characterization of Streptococcus mutans Strains Deficient in EIIAB Man of the Sugar Phosphotransferase System

Two functionally different glucose phosphotransferase transport systems in Streptococcus mutans and Streptococcus sobrinus

From meadows to milk to mucosa – adaptation ofStreptococcusandLactococcusspecies to their nutritional environments

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Characterization of Streptococcus mutans Strains Deficient in EIIAB ^Man of the Sugar Phosphotransferase System

Characterization of Streptococcus mutans Strains Deficient in EIIAB ^Man of the Sugar Phosphotransferase System