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PubMed2005

Streptococcus iniae phosphoglucomutase is a virulence factor and a target for vaccine development.

Streptococcus iniae represents a major health and economic problem in fish species worldwide. Random Tn917 mutagenesis and high-throughput screening in a hybrid striped bass (HSB) model of meningoencephalitis identified attenuated S. iniae mutants. The Tn917 insertion in one mutant disrupted an S. iniae homologue of a phosphoglucomutase (pgm) gene. Electron microscopy revealed a decrease in capsule thickness and cell wall rigidity, with DeltaPGM mutant cells reaching sizes approximately 3-fold larger than those of the wild type (WT). The DeltaPGM mutant was cleared more rapidly in HSB blood and was more sensitive to killing by cationic antimicrobial peptides including moronecidin from HSB. In vivo, the DeltaPGM mutant was severely attenuated in HSB, as intraperitoneal challenge with 1,000 times the WT lethal dose produced only 2.5% mortality. Reintroduction of an intact copy of the S. iniae pgm gene on a plasmid vector restored antimicrobial peptide resistance and virulence to the DeltaPGM mutant. In analysis of the aborted infectious process, we found that DeltaPGM mutant organisms initially disseminated to the blood, brain, and spleen but were eliminated by 24 h without end organ damage. Ninety to 100% of fish injected with the DeltaPGM mutant and later challenged with a lethal dose of WT S. iniae survived. We conclude that the pgm gene is required for virulence in S. iniae, playing a role in normal cell wall morphology, surface capsule expression, and resistance to innate immune clearance mechanisms. An S. iniae DeltaPGM mutant is able to stimulate a protective immune response and may have value as a live attenuated vaccine for aquaculture.

Amino Acid Sequence↗
PubMed1971

Phosphoglucomutase mutants of Escherichia coli K-12.

Bacteria with strongly depressed phosphoglucomutase (EC 2.7.5.1) activity are found among the mutants of Escherichia coli which, when grown on maltose, accumulate sufficient amylose to be detectable by iodine staining. These pgm mutants grow poorly on galactose but also accumulate amylose on this carbon source. Growth on lactose does not produce high amylose but, instead, results in the induction of the enzymes of maltose metabolism, presumably by accumulation of maltose. These facts suggest that the catabolism of glucose-1-phosphate is strongly depressed in pgm mutants, although not completely abolished. Anabolism of glucose-1-phosphate is also strongly depressed, since amino acid- or glucose-grown pgm mutants are sensitive to phage C21, indicating a deficiency in the biosynthesis of uridine diphosphoglucose or uridine diphosphogalactose, or both. All pgm mutations isolated map at about 16 min on the genetic map, between purE and the gal operon.

Bacteriological Techniques↗
PubMed1994

Role of phosphoglucomutase in lipooligosaccharide biosynthesis in Neisseria gonorrhoeae.

A region of pSG30 that complements the pyocin-derived gonococcal lipooligosaccharide (LOS) mutants 1291d and 1291e was characterized by DNA sequence analysis and an open reading frame of 1,380 bases was identified that is 89% similar and 56% identical over 452 amino acids to the algC gene product from Pseudomonas aeruginosa that encodes phosphomannomutase. Enzymatic analysis of gonococcal crude protein extracts demonstrated that pSG30 encodes phosphoglucomutase (PGM) and phosphomannomutase activity. This activity is absent in 1291d and 1291e but is restored upon introduction of pSG30. PGM encoded by pSG34, a subclone of pSG30, was able to complement Escherichia coli PGM1, a strain deficient in PGM, as determined by bacteriophage C21 plaque formation. A revertant of 1291d that binds monoclonal antibody 2-1-L8 (specific for a 3.6-kDa LOS component) was isolated. The construction of a site-specific deletion of this region in the chromosome of 1291 confirms the role of this open reading frame in LOS biosynthesis.

Amino Acid Sequence↗
PubMed1994

The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core.

We have constructed strains of Pseudomonas aeruginosa with mutations in the algC gene, previously shown to encode the enzyme phosphomannomutase. The algC mutants of a serotype O5 strain (PAO1) and a serotype O3 strain (PAC1R) did not express lipopolysaccharide (LPS) O side chains or the A-band (common antigen) polysaccharide. The migration of LPS from the algC mutant strains in Tricine-sodium dodecyl sulfate-polyacrylamide gels was similar to that of LPS from a PAO1 LPS-rough mutant, strain AK1012, and from a PAC1R LPS-rough mutant, PAC605, each previously shown to be deficient in the incorporation of glucose onto the LPS core (K. F. Jarrell and A. M. Kropinski, J. Virol. 40:411-420, 1981, and P. S. N. Rowe and P. M. Meadow, Eur. J. Biochem. 132:329-337, 1983). We show that, as expected, the algC mutant strains had no detectable phosphomannomutase activity and that neither algC strain had detectable phosphoglucomutase (PGM) activity. To confirm that the PGM activity was encoded by the algC gene, we transferred the cloned, intact P. aeruginosa algC gene to a pgm mutant of Escherichia coli and observed complementation of the pgm phenotype. Our finding that the algC gene product has PGM activity and that strains with mutations in this gene produce a truncated LPS core suggests that the synthesis of glucose 1-phosphate is necessary in the biosynthesis of the P. aeruginosa LPS core. The data presented here thus demonstrate that the algC gene is required for the synthesis of a complete LPS core in two strains with different LPS core and O side chain structures.

Amino Acid Sequence↗
PubMed1998

Gene organization and transcription analysis of the Agrobacterium tumefaciens glycogen (glg) operon: two transcripts for the single phosphoglucomutase gene.

The gene organization and transcription of the Agrobacterium glg operon differ from those in other bacteria. Agrobacterium tumefaciens A348 contains a 9.1-kb gene cluster harboring genes for glycogen metabolism. The nucleotide sequence and gene organization of a region containing ADP-glucose pyrophosphorylase (glgC), glycogen synthetase (glgA), and phosphoglucomutase (pgm) genes have been previously described (A. Uttaro and R. A. Ugalde, Gene 150:117-122, 1994). In this work we report that the glycogen phosphorylase (glgP) and branching enzyme (glgB) genes are located immediately upstream of this region. The complete nucleotide sequences of the glgP and glgB genes were obtained, and mutants were constructed by targeted insertional mutagenesis with a kanamycin cassette. Enzymatic assays and reverse transcription PCR carried out with the wild type and with glgP and glgB mutants, as well as primer extension experiments and beta-galactosidase fusions, revealed that this region containing five open reading frames (glgPBCA and pgm) is transcribed unidirectionally as a single operon under the control of a promoter located upstream of the glycogen phosphorylase gene (glgP). An alternative transcript was identified starting 168 bp upstream of an internal ATG start codon of the pgm gene, which is translated as a 71-amino-acid-shorter Pgm protein which complements in vivo a pgm mutant. This alternative transcript has a promoter with the motif TATCAAN5G, identified in octopine Ti plasmid as an autoinducible TraR promoter. This promoter is >200 times more efficient in A. tumefaciens than in Escherichia coli, as judged by the level of enzymatic activity of a lacZ-pgm fusion.

1,4-alpha-Glucan Branching Enzyme↗
PubMed2000

Capsule biosynthesis and basic metabolism in Streptococcus pneumoniae are linked through the cellular phosphoglucomutase.

Synthesis of the type 3 capsular polysaccharide of Streptococcus pneumoniae requires UDP-glucose (UDP-Glc) and UDP-glucuronic acid (UDP-GlcUA) for production of the [3)-beta-D-GlcUA-(1-->4)-beta-D-Glc-(1-->](n) polymer. The generation of UDP-Glc proceeds by conversion of Glc-6-P to Glc-1-P to UDP-Glc and is mediated by a phosphoglucomutase (PGM) and a Glc-1-P uridylyltransferase, respectively. Genes encoding both a Glc-1-P uridylyltransferase (cps3U) and a PGM homologue (cps3M) are present in the type 3 capsule locus, but these genes are not essential for capsule production. In this study, we characterized a mutant that produces fourfold less capsule than the type 3 parent. The spontaneous mutation resulting in this phenotype was not contained in the type 3 capsule locus but was instead located in a distant gene (pgm) encoding a second PGM homologue. The function of this gene product as a PGM was demonstrated through enzymatic and complementation studies. Insertional inactivation of pgm reduced capsule production to less than 10% of the parental level. The loss of PGM activity in the insertion mutants also caused growth defects and a strong selection for isolates containing second-site suppressor mutations. These results demonstrate that most of the PGM activity required for type 3 capsule biosynthesis is derived from the cellular PGM.

Amino Acid Sequence↗
PubMed2004

Among multiple phosphomannomutase gene orthologues, only one gene encodes a protein with phosphoglucomutase and phosphomannomutase activities in Thermococcus kodakaraensis.

Four orthologous genes (TK1108, TK1404, TK1777, and TK2185) that can be annotated as phosphomannomutase (PMM) genes (COG1109) have been identified in the genome of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. We previously found that TK1777 actually encodes a phosphopentomutase. In order to determine which of the remaining three orthologues encodes a phosphoglucomutase (PGM), we examined the PGM activity in T. kodakaraensis cells and identified the gene responsible for this activity. Heterologous gene expression and purification and characterization of the recombinant protein indicated that TK1108 encoded a protein with high levels of PGM activity (690 U mg(-1)), along with high levels of PMM activity (401 U mg(-1)). Similar analyses of the remaining two orthologues revealed that their protein products exhibited neither PGM nor PMM activity. PGM activity and transcription of TK1108 in T. kodakaraensis were found to be higher in cells grown on starch than in cells grown on pyruvate. Our results clearly indicate that, among the four PMM gene orthologues in T. kodakaraensis, only one gene, TK1108, actually encodes a protein with PGM and PMM activities.

Amino Acid Sequence↗
PubMed1969

Electrophoretic variants of phosphoglucomutase in Saccharomyces species.

Strains of Saccharomyces cerevisiae and species with which S. cerevisiae is interfertile display a characteristic pattern of electrophoretic variants of phosphoglucomutase (PGM) consisting of a major component and one or two minor components, all of which migrate toward the cathode. The patterns are consistent with an earlier finding that two unlinked genes, one of which has two known alleles, determine the synthesis of PGM in S. cerevisiae. The PGM patterns of strains of S. fragilis, S. lactis, and S. marxianus, species thought to be closely related to each other and only distantly related to S. cerevisiae, also displayed a characteristic pattern of PGM variants, but it was quite different from that of S. cerevisiae. In these species five or six electrophoretic variants could be detected, all of which migrated toward the anode. We interpret the differences in the PGM variants of the two groups of species as a reflection of differences in genetic composition which have arisen in two phylogenetically distinct groups that have become sexually isolated from each other.

Alleles↗
PubMed1985

Glucose 1,6-bisphosphate decline in human erythrocytes: possible involvement of phosphoglucomutase PGM2 isoenzymes.

Human erythrocytes incubated with various sugars lower their glucose 1,6-bisphosphate (Glc-1,6-P2) content, as do haemolysates containing exogenous Glc-1,6-P2 incubated with sugar monophosphates (sugar-P). Experiments performed with isolated erythrocyte phosphoglucomutase (PGM) isoenzymes indicate that only definite isoenzymatic forms, namely PGM2, are able to consume Glc-1,6-P2 during the mutation of sugar-P other than glucose-P. In this process a phosphate group is released from Glc-1,6-P2 and can be partially recovered in the biphosphate of the mutated sugar-P. The relevance of this mechanism of Glc-1,6-P2 degradation is discussed in regard to the physiological turnover of the biphosphate.

Adenine Nucleotides↗
PubMed1993

Fetal growth, gestation length and phosphoglucomutase-1 phenotype.

This study investigates reports that phosphoglucomutase-1 (PGM1) phenotype is associated with fetal growth and gestation length. A total of 350 women were studied, 234 having uncomplicated pregnancies and 114 with a baby weighing greater than 90th centile, corrected for parity, gestation and fetal sex. All women had gestation confirmed by early ultrasound. Conventional cellulose acetate electrophoresis was used to distinguish the three common PGM1 phenotypes and polyacrylamide gel isoelectric focusing to distinguish the ten PGM1 subtypes. Neither PGM1 phenotype nor subtype were found to be associated with gestation length or standardised birth weight. Logistic regression, where maternal age, parity, fetal sex, maternal weight, gestation and smoking were introduced as explanatory variables in addition to PGM1 phenotype testing against the dependent variables birth weight, standardised birth weight and gestation length, did not show differences related to PGM1 phenotype. Two possible reasons for the discrepancy with previously published data are discussed. We conclude that the study provides no support for the belief that PGM1 phenotype is related to fetal growth or gestation length and that the original observations could have arisen as a result of statistical artefact due to multiple testing.

Biomarkers↗
PubMed1975

Distribution of adenylate kinase and phosphoglucomutase isoenzymes in the population of the city of New York.

Blood samples from unrelated persons living in New York, N.Y., were examined for phosphoglucomutase (PGM) and adenylate kinase (AK) phenotypes, the sample consisting of 164 Caucasians, 133 Negroes, 129 persons of Spanish origin or descent, and 156 Chinese for PGM and 136 Caucasians, 134 Negroes, 136 persons of Spanish origin or descent, and 156 Chinese for AK. The PGM1 gene frequency was found to be 0.7774 for Caucasians, 0.8083 for Negroes, 0.7461 for Hispanic persons, and 0.7917 for Chinese. One Hispanic person had a very rare type, PGM 8-1-FAST. The AK1 gene frequency was found to be 0.9669 for Caucasians, 0.9813 for Negroes, 0.9779 for Hispanic persons, and 1.000 for Chinese.

Adenylate Kinase↗
PubMed1983

Human phosphoglucomutase locus 1: red cell enzymatic activities associated with common isoelectric focusing phenotypes.

Human phosphoglucomutase activity has been determined in red blood cells obtained from 348 unrelated subjects. The mean activities attributed to the four common PGM1 alleles, expressed as micromoles of G6P produced per gram of Hb per hour were 53 for PGMa31, 60 for PGMa11, 61 for PGMa41 and 72 for PGMa21. The relative amount of variation associated with the electrophoretic polymorphism was estimated as 24%.

Alleles↗
PubMed1985

Phosphoglucomutase (PGM1) subtypes in a Finnish population determined by isoelectric focusing in agarose gel.

The red cell enzyme phosphoglucomutase first locus (PGM1) phenotypes of 639 adult Finns were determined by isoelectric focusing in agarose gel. All the ten commonly occurring phenotypes were detected and the frequencies of the four alleles at the PGM1 locus were as follows: PGMa11 = 0.5313, PGMa21 = 0.1800, PGMa31 = 0.2199 and PGMa41 = 0.0689. The PGM1 phenotypes of 221 mothers with 228 offspring were in accordance with autosomal codominant inheritance.

Alleles↗
PubMed1986

Phosphoglucomutase-1 subtypes: polymorphic occurrence of PGM1*7+ and geographical variation in Japan.

The distribution of gene frequencies in the phosphoglucomutase-1 (PGM1) system was investigated in two Japanese populations from Yamaguchi (Western Japan) and Okinawa (Southern Japan) using an improved isoelectric focusing method permitting the successful detection of the most anodal variant PGM1 3+. PGM1*7+ occurred with a polymorphic frequency of 0.012-0.021. A difference in the gene frequency was observed between the two populations. In comparison with neighboring populations, the Yamaguchi population was similar to Mongolians and Koreans in North China, and Okinawa to Zhuang in South China.

Alleles↗
PubMed1991

Phosphoglucomutase-1 polymorphism among Chinese in Taiwan.

Phosphoglucomutase-1 (PGM1) phenotyping of 1,128 Chinese blood donors was performed by thin-layer isoelectric focusing on agarose. The PGM1 gene frequencies were: 1A, 0.6005; 1B, 0.1500; 2A, 0.1510; 2B, 0.0973, and rare variants, 0.0058. The rare variants found in this series were PGM1 W21, W2, W3, W6 and W9 (or W10) with PGM1 W21 being the most common variant among Chinese with a phenotype frequency of 0.8%.

Alleles↗
PubMed1991

Phosphoglucomutase phenotyping among Chinese in Taiwan.

Phosphoglucomutase 1 (PGM1) phenotyping was performed in 1,128 Chinese blood donors by thin-layer isoelectric focusing on agarose. The PGM1 gene frequencies were as follows: 1A, 0.6005; 1B, 0.1500; 2A, 0.1510, 2B, 0.0973; variants, 0.0058, with W21, 0.0040. The variants found in this series were PGM1 W21, W2, W3, W6 and W9 (or W10) with PGM1 W21 being the most common variant among Chinese, having a phenotype frequency of 0.8%.

China↗
PubMed1991

Phosphoglucomutase-1 subtypes in two populations in Adriatic islands: presence of PGM1*W3 (PGM1*7+) allele.

Allele frequencies at the phosphoglucomutase-1 (PGM1) locus have been investigated in two Croatian (Yugoslavian) populations from neighboring islands, Silba and Olib. The genotype distributions are significantly different though the two islands are only 2 km apart. In the light of demographic and historical data, a few hypotheses explaining these results are discussed. A rare variant, PGM1*W3, usually found in Asia, is present in 4 inhabitants from the Olib island.

Alleles↗