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  • 1
    Keywords: Emerging infectious diseases ; Bacteriology ; Infectious Diseases ; Bacteriology ; Springer eBooks
    Description / Table of Contents: Specimen Collection, Processing, Culture, and Biochemical Identification of Acinetobacter spp. -- Genotyping of Acinetobacter baumannii in Nosocomial Outbreak and Surveillance -- Antimicrobial Susceptibility Testing Methods for Acinetobacter spp -- Methods to Evaluate Colistin Heteroresistance in Acinetobacter baumannii -- Testing Metal Sensitivity of A. baumannii Strains: Survival in Copper Supplemented Liquid Media and on Copper-Containing Surfaces -- A New Method for Determination of Minimum Biofilm Eradication Concentration for Accurate Antimicrobial Therapy -- Transformation of Acinetobacter baumannii: Electroporation -- Methods for Natural Transformation in Acinetobacter baumannii -- Vesicle Mediated Gene Transfer in A. baumannii -- Targeted Gene Replacement in Acinetobacter baumannii -- RecET-Mediated Recombineering in Acinetobacter baumannii -- Methods for Tn-seq Analysis in Acinetobacter baumannii -- Tn7-Based Single Copy Insertion Vectors for Acinetobacter baumannii -- Distinguishing Colony Opacity Variants and Measuring Opacity Variation in Acinetobacter baumannii -- A Simple Static Biofilm Assay for Acinetobacter baumannii -- BioFluxTM 200 Microfluidic System to Study A. baumannii Biofilm Formation in a Dynamic Mode of Growth -- In Vitro Motility Assays for Acinetobacter Species -- Desiccation Tolerance Assays for Acinetobacter baumannii -- Measuring Intracellular Metal Concentration via ICP-MS Following Copper Exposure -- PBP Isolation and DD-Carboxypeptidase Assay -- Extraction and Visualization of Capsular Polysaccharide from Acinetobacter baumannii -- Isolation of Lipid Cell Envelope Components from Acinetobacter baumannii -- Methods for Detecting N-acyl-homoserine Lactone Production in Acinetobacter baumannii -- Isolation and Characterization of the Acinetobactin and Baumannoferrin Siderophores Produced by Acinetobacter baumannii -- Skin and Soft Tissue Models for Acinetobacter baumannii Infection -- Assessing Acinetobacter baumannii Virulence and Persistence in a Murine Model of Lung Infection -- Computational Prediction of sRNA in Acinetobacter baumannii -- Global Metabolic Analyses of Acinetobacter baumannii -- Reverse Vaccinology Approach to Potential Vaccine Candidates against Acinetobacter baumannii
    Abstract: This detailed volume serves clinicians and basic science researchers studying the increasingly antibiotic resistant Gram-negative bacterium Acinetobacter baumannii. Chapters detail microbiological techniques, biochemical techniques, clinical samples, and next generation omics techniques to characterize the organism at the molecular level. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and cutting-edge, Acinetobacter baumannii: Methods and Protocols aims to ensure successful results in the further study of this high priority area of antibiotic study
    Pages: XIV, 338 p. 87 illus., 53 illus. in color. : online resource.
    ISBN: 9781493991181
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  • 2
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In Escherichia coli, a lacZ fusion to the gabT gene is activated by the accumulation of two self-produced extracellular signals, indole and a second unidentified signal (signal-2). Extracellular indole contributes approximately 25% of this activation and signal-2 is responsible for the majority of activation. Using an E. coli strain unable to produce indole and containing a gabT::lacZ fusion, a genetic approach was used to search for genes involved in the production of signal-2. A spontaneous E. coli mutant, MJ1, exhibited significantly less signal-2 activity based on the ability of spent culture supernatants from this mutant to activate the gabT::lacZ fusion. Genetic analysis of MJ1 revealed that it contained two mutations, one in thyA and a second unknown mutation, designated spl1 (signal production locus) that led to loss of signal-2 production. The spl1 second-site mutation arises at high frequency in a thyA− background because it suppresses the loss of viability. This study demonstrates that mutations in deoB and deoC were capable of suppressing the loss of viability in thyA mutants and concomitantly resulted in loss of signal-2 activity in conditioned medium. Interestingly, both deoB and deoC mutations in an otherwise wild-type background resulted in higher levels of gabT::lacZ expression in cells at low density. It is hypothesized that deoB and deoC mutations result in an enhanced rate of signal-2 uptake and thus deplete signal-2 from the external medium.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Using a mini-Tn5lacZ1 reporter transposon, lacZ fusions have been identified in Proteus mirabilis that are activated by the accumulation of self-produced extracellular signals. Genes identified by this approach include putative homologs of pgm, nlpA and two genes of unknown function. The extracellular signal(s) involved in activation were resistant to the effects of acid and alkali. The signal required for activation of (nlpA) cma482::lacZ was sensitive to protease, suggesting the signal is a peptide or small protein. The signals behaved as polar molecules and were not extractable with ethyl acetate. A mini-Tn5Cm insertion was identified in a probable ptsI homolog that blocked activation of the cma134::lacZ fusion by an extracellular signal. The ptsI mutation did not alter extracellular signal production and may have a role in signal response.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The AarP protein in Providencia stuartii encodes a small transcriptional activator which activates the chromosomal aminoglycoside acetyltransferase aac(2′)-Ia gene. In addition, AarP activates genes involved in a multiple antibiotic resistance (Mar) phenotype. Expression of an aarP–lacZ fusion increased in a density-dependent manner and reached peak levels at stationary phase. The expression of an aarP–lacZ fusion could be prematurely activated in cells at early to mid-exponential phase by the addition of spent culture supernatants from stationary phase cultures or by ethyl acetate extracts of these supernatants. Nutrient starvation had a negligible effect on aarP expression. In a search for mutations that block aarP activation at stationary phase, a mini-Tn5Cm insertion has been identified within a gene whose product was 77% identical to SspA, a regulatory protein involved in stationary phase gene expression and virulence. An unmarked sspA null allele (sspA2) was created by allelic replacement to further examine the role of sspA in P. stuartii. The sspA2 allele resulted in substantial decrease in aarP mRNA accumulation at various phases of growth. Furthermore, in an sspA mutant background, the aarP–lacZ fusion was no longer activated by an extracellular signal.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In a search for genes involved in regulation of the 2′-N-acetyltransferase in Providencia stuartii, a mini-Tn5 Cm insertion has been isolated in a locus designated aarD. The aarD1::mini-Tn5 Cm mutation resulted in a 4.7-fold increase in the levels of β-galactosidase accumulation from an aac(2′)–lacZ transcriptional fusion and a 32-fold increase in the levels of gentamicin resistance in P. stuartii. The wild-type aarD locus was cloned on a 5.0 kb Cla I fragment and complemented the aarD1 mutation. Nucleotide sequence analysis of this fragment identified two large open reading frames whose deduced products displayed significant amino acid identity, 64% and 64%, respectively, to the CydD and CydC proteins of Escherichia coli, which are involved in formation of the cytochrome d oxidase complex. Physical mapping indicated the aarD1::mini-Tn5 Cm insertion was within the open reading homologous to CydD. The strain containing the aarD1 mutation was unable to grow in the presence of toluidine blue or on glycerol minimal media in the presence of zinc, suggesting that aarD is functionally equivalent to cydD. Additional phenotypes resulting from the aarD1 mutation included: altered cell morphology, a reduced growth rate and the inability of cells to grow beyond early log phase. Further examination of this phenomenon revealed that the aarD1 mutant was unable to grow in the presence of a self-produced extracellular factor(s). This novel phenotype was not limited to P. stuartii as E. coli cydD and ΔcydAB::kan mutants were also sensitive to a self-produced extracellular factor.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In a search for Proteus mirabilis genes that were regulated by cell-to-cell signalling, a lacZ fusion (cmr437::mini-Tn5lacZ) was identified that was repressed 10-fold by a self-produced extracellular signal from wild-type cells. However, the cmr437::mini-Tn5lacZ insertion itself led to a marked reduction in this extracellular repressing signal. The cmr437::mini-Tn5lacZ insertion was mapped to a speA homologue in P. mirabilis. Sequence analysis indicated that a speB homologue was encoded downstream of speA. Products of the SpeA and SpeB enzymes (agmatine and putrescine) were tested for repression of cmr437::lacZ. Agmatine did not have repressing activity. However, putrescine was an effective repressing molecule at concentrations down to 30 µM. A second prominent phenotype of the cmr437 (speA)::mini-Tn5lacZ insertion was a severe defect in swarming motility. This swarming defect was also observed in a strain containing a disruption of the downstream speB gene. Differentiation of the speB mutant to swarmer cells was delayed by two hours relative to wild-type cells. Furthermore, the speB mutant was unable to migrate effectively across agar surfaces and formed very closely spaced swarming rings. Exogenous putrescine restored both the normal timing of swarmer cell differentiation and the ability to migrate to speB mutants.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A recessive mutation, aarG1, has been identified that resulted in an 18-fold increase in the expression of β-galactosidase from an aac(2′)–lacZ fusion. Transcriptional fusions and Northern blot analysis demonstrated that the aarG1 allele also resulted in a large increase in the expression of aarP, a gene encoding a transcriptional activator of aac(2′)-Ia. The effects of aarG1 on aac(2′)-Ia expression were mediated by aarP-dependent and -independent mechanisms. The aarG1 allele also resulted in a multiple antibiotic resistance (Mar) phenotype, which included increased chloramphenicol, tetracycline and fluoroquinolone resistance. This Mar phenotype also resulted from aarP-dependent and -independent mechanisms. Sequence analysis of the aarG locus revealed the presence of two open reading frames, designated aarR and aarG, organized in tandem. The putative AarR protein displayed 75% amino acid identity to the response regulator PhoP, and the AarG protein displayed 57% amino acid identity to the sensor kinase PhoQ. The aarG1 mutation, a C to T substitution, resulted in a threonine to isoleucine substitution at position 279 (T279I) in the putative sensor kinase. The AarG product was functionally similar to PhoQ, as it was able to restore wild-type levels of maganin resistance to a Salmonella typhimurium phoQ mutant. However, expression of the aarP and aac(2′)-Ia genes was not significantly affected by the levels of Mg2+ or Ca2+, suggesting that aarG senses a signal other than divalent cations.
    Type of Medium: Electronic Resource
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