Disease relevance of aroA

• An Escherichia coli hemolysin transport system-based vector for the export of polypeptides: export of Shiga-like toxin IIeB subunit by Salmonella typhimurium aroA [1].
• The aroA gene from Pasteurella multocida was cloned by complementation of the Escherichia coli aroA mutant AB2829 with a DNA library constructed in pUC18 [2].
• Molecular analysis of the aroA gene of Pasteurella multocida and vaccine potential of a constructed aroA mutant [2].
• The filamentous hemagglutinin (FHA) of Bordetella pertussis was expressed in the attenuated aroA mutant of Salmonella typhimurium, SL3261, and in a strain of Escherichia coli harboring Shigella flexneri plasmid pWR110, which encodes bacterial invasiveness for epithelial cells [3].
• Cloning and nucleotide sequence of the aroA gene of Bordetella pertussis [4].

High impact information on aroA

• A glyphosate-resistant aroA allele has been cloned in Escherichia coli from a mutagenized strain of Salmonella typhimurium [5].
• A hybrid gene fusion between mutant and wild type aroA gene sequences was constructed [5].
• Comparison of the mutant and wild type aroA gene sequences reveals a single base pair change resulting in a Pro to Ser amino acid substitution at the 101st codon of the protein [5].
• The nucleotide sequence of the P. multocida aroA gene indicated an open reading frame encoding a protein of 441 amino acids, which showed a high degree of homology with the amino acid sequences of various other bacterial AroA proteins [2].
• The cloned P. multocida aroA gene was inactivated by insertion of a kanamycin-resistance gene and reintroduced by allelic exchange into the chromosome of P. multocida using the suicide vector pJM703 [2].

Chemical compound and disease context of aroA

• The gene for 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase (aroA) cloned from Campylobacter jejuni (Cj) strain 81116 was identified by complementation of an Escherichia coli (Ec) auxotrophic aroA mutant [6].
• A DNA fragment encoding a kanamycin resistance determinant was used to insertionally inactivate the cloned aroA gene of Bordetella pertussis in Escherichia coli K-12, and a conjugative shuttle vector system based on the suicide vector pRTP1 was used to deliver the mutations from E. coli back into B. pertussis CN2992FS and BP1 [7].

Biological context of aroA

• As demonstrated by the study of listeriolysin-defective L. monocytogenes or of S. typhimurium SL7207 aroA engineered to secrete listeriolysin, escape of bacteria or of plasmid DNA from the intracytoplasmic vacuole is required for transfer of genetic information to occur [8].
• The aroA gene of A. salmonicida was cloned in Escherichia coli, and the nucleotide sequence was determined [9].
• Immunization of mice with S. typhimurium aroA strains carrying the hybrid genes expressed from these two promoters resulted in significant B subunit-specific mucosal and serum antibody responses [10].
• The mutation resulted in attenuation when bacteria were injected intramuscularly into Atlantic salmon (Salmo salar L.). Introduction of the wild-type aroA gene into the A. salmonicida mutants on a broad-host-range plasmid restored virulence [9].
• The aroA locus of Bordetella pertussis, encoding 5-enolpyruvylshikimate 3-phosphate synthase, has been cloned into Escherichia coli by using a cosmid vector [4].

Anatomical context of aroA

• S. typhimurium aroA mutants apparently have a membrane export defect which prevents the transport of LamB and its derivatives across the cytoplasmic membrane [10].
• DNA transfer with S. typhimurium was observed only from atten-uated aroA strain SL7207 into COS-1 cell line [8].
• These results show that Y. enterocolitica aroA mutants can be used effectively as carriers of heterologous antigens to the murine immune system [11].
• 5-Enolpyruvylshikimate-3-phosphate (EPSP) synthase, the product of the Escherichia coli aroA gene, has been overproduced in E. coli BL21(lambda DE3) under the control of the T7 gene 10 promoter and ribosome binding site, to a level of approximately 50% of total cell protein [12].

Associations of aroA with chemical compounds

• The enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EC 2.5.1.19), encoded by the aroA locus, is a target site of glyphosate inhibition in bacteria [5].
• Gene replacement was finally achieved by constructing a replacement plasmid with aroA inactivated by insertion of a P. haemolytica ampicillin resistance fragment into a unique NdeI site in aroA [13].
• The only other enzyme known to catalyse the transfer of the intact 1-carboxyvinyl moiety of phosphoenolpyruvate to a substrate is the 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19), the sixth enzyme of the shikimate pathway [14].

Analytical, diagnostic and therapeutic context of aroA

• The codon usage pattern of aroA was found to be quite distinct from that of the vapA gene coding for the surface array protein layer (A layer) [9].
• The aroA gene, encoding 5-enolpyruvylshikimate 3-phosphate synthase, from Pasteurella haemolytica biotype A, serotype 1 was cloned by complementation of the aroA mutation in Escherichia coli strain AB2829 after electroporation with a DNA library constructed in pUC18 [15].
• Molecular cloning and sequencing of the aroA gene from Actinobacillus pleuropneumoniae and its use in a PCR assay for rapid identification [16].
• Southern blot analysis confirmed that aroA of the mutant was inactivated and that the mutant was without a plasmid [13].

References