Results 21 to 30 of about 3,523 (182)
TlyC, a conserved hemolysin in Rickettsia, contributes to spotted fever pathogenesis in mice [PDF]
Microbiology SpectrumRickettsia circulates between mammalian hosts and hematophagous arthropod vectors by exploiting their intracellular environment. With advances in rickettsial genetic tools, recent studies have identified novel molecular mechanisms involved in Rickettsia ...
Luke Helminiak +3 more
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Adipose tissue serves as a reservoir for recrudescent Rickettsia prowazekii infection in a mouse model. [PDF]
PLoS ONE, 2010 Brill-Zinsser disease, the relapsing form of epidemic typhus, typically occurs in a susceptible host years or decades after the primary infection; however, the mechanisms of reactivation and the cellular reservoir during latency are poorly understood ...
Yassina Bechah +4 more
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Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents. [PDF]
Bioorg Med Chem, 2017 Methionine aminopeptidase (MetAP) is a class of ubiquitous enzymes essential for the survival of numerous bacterial species. These enzymes are responsible for the cleavage of N-terminal formyl-methionine initiators from nascent proteins to initiate post ...
Helgren TR +11 more
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Analysis of the peptidoglycan of Rickettsia prowazekii [PDF]
Journal of Bacteriology, 1994 In the present study, peptidoglycan from Rickettsia prowazekii, an obligate intracellular bacterium, was purified. The rickettsial peptidoglycan is like that of gram-negative bacteria; that is, it is sodium dodecyl sulfate insoluble, lysozyme sensitive, and composed of glutamic acid, alanine, and diaminopimelic acid in a molar ratio of 1.0:2.3:1.0. The
H, Pang, H H, Winkler
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Transport of AMP by Rickettsia prowazekii [PDF]
Journal of Bacteriology, 1985 Rickettsia prowazekii possesses an exchange transport system for AMP. Chromatographic analysis of the rickettsiae demonstrated that transported AMP appeared intracellularly as AMP, ADP, and ATP, and no hydrolytic products appeared in either the intracellular or extracellular compartments.
W H, Atkinson, H H, Winkler
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Mariner-based transposon mutagenesis of Rickettsia prowazekii. [PDF]
Appl Environ Microbiol, 2007 Rickettsia prowazekii, the causative agent of epidemic typhus, is an obligate intracellular bacterium that grows directly within the cytoplasm of its host cell, unbounded by a vacuolar membrane.
Liu ZM, Tucker AM, Driskell LO, Wood DO.
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Permeability of Rickettsia prowazekii to NAD [PDF]
Journal of Bacteriology, 1989 Rickettsia prowazekii accumulated radioactivity from [adenine-2,8-3H]NAD but not from [nicotinamide-4-3H]NAD, which demonstrated that NAD was not taken up intact. Extracellular NAD was hydrolyzed by rickettsiae with the products of hydrolysis, nicotinamide mononucleotide and AMP, appearing in the incubation medium in a time- and temperature-dependent ...
W H, Atkinson, H H, Winkler
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Proline transport and metabolism in Rickettsia prowazekii [PDF]
Journal of Bacteriology, 1984 Purified Rickettsia prowazekii cells were able to transport L-proline. The influx of this amino acid had a Kt of 14 microM and a Vmax of about 64 pmol/min per mg of protein. Proline could not be transported by heat-killed or metabolically poisoned rickettsiae or at 0 degrees C. The uptake of proline was linear for almost 2 h.
H H, Winkler, R M, Daugherty
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Transformation of Rickettsia prowazekii to Rifampin Resistance [PDF]
Journal of Bacteriology, 1998 ABSTRACT Rickettsia prowazekii , the causative agent of epidemic typhus, is an obligate intracellular parasitic bacterium that grows directly within the cytoplasm of the eucaryotic host cell. The absence of techniques for genetic manipulation hampers the study of this organism’s unique biology and pathogenic ...
L I, Rachek +3 more
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Isolation and characterization of the Rickettsia prowazekii recA gene [PDF]
Journal of Bacteriology, 1994 The recA gene has been isolated from Rickettsia prowazekii, an obligate intracellular bacterium. Comparison of the amino acid sequence of R. prowazekii RecA with that of Escherichia coli RecA revealed that 62% of the residues were identical. The highest identity was found with RecA of Legionella pneumophila, in which 69% of the residues were identical.
S M, Dunkin, D O, Wood
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