Identification of genes affecting expression of phosphoglycerate kinase on the surface of group B streptococcus
Autor: | Tyler J. Boone, Gregory J. Tyrrell |
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Rok vydání: | 2012 |
Předmět: |
Immunology
Mutant Antimicrobial peptides Mutagenesis (molecular biology technique) Bacitracin Biology medicine.disease_cause Applied Microbiology and Biotechnology Microbiology Streptococcus agalactiae Hemolysin Proteins Genetics medicine Molecular Biology Gene Nisin Antigens Bacterial Phosphoglycerate kinase Streptococcus Membrane Proteins Gene Expression Regulation Bacterial General Medicine bacterial infections and mycoses Molecular biology Anti-Bacterial Agents Phosphoglycerate Kinase Genes Bacterial bacteria Peptides medicine.drug |
Zdroj: | Canadian Journal of Microbiology. 58:433-441 |
ISSN: | 1480-3275 0008-4166 |
DOI: | 10.1139/w2012-015 |
Popis: | Group B streptococcal phosphoglycerate kinase (GBS-PGK), a glycolytic enzyme, has previously been identified on the surface of group B streptococcus (GBS). To identify genes involved in surface expression of GBS-PGK, we performed Tn917 mutagenesis followed by quantification of PGK expressed on the GBS surface. Tn917 mutagenesis identified 4 genes (sag0966, sag0979, sag0980, and sag1003) that when disrupted, alter expression of GBS-PGK on the bacterial surface. Three of the identified genes were localized to a region of the GBS genome containing genes (sag0973–sag0977) predicted to be involved in resistance to antimicrobial peptides. One mutant isolate, designated NCS13sag1003::Tn917, was found to have increased sensitivity to the antimicrobial peptides bacitracin and nisin. In addition, all of the mutant strains assayed were found to have decreased β-hemolysis. In conclusion, we have identified genes involved in surface expression of GBS-PGK. These genes also appear to be involved in antimicrobial peptide resistance and regulate expression of the β-hemolysin. |
Databáze: | OpenAIRE |
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