Disease relevance of Bdellovibrio

• Chloramphenicol, added at various times after initiation of bdellovibrio intraperiplasmic growth on normal or on heated E. coli, which have inactivated deoxyribonucleases, inhibited further breakdown and solubilization of substrate cell DNA [1].
• Toxin production, bacteriophages, and Bdellovibrio sp. did not cause the disappearance of the two bacterial species [2].

High impact information on Bdellovibrio

• The lipopolysaccharide moiety of the cell membrane of target microorganisms appears to contain the principal receptor site for bdellovibrio attachment [3].
• Metabolism of periplasmic membrane-derived oligosaccharides by the predatory bacterium Bdellovibrio bacteriovorus 109J [4].
• They showed that a major protein appearing in the Bdellovibrio Triton X-100-insoluble outer membrane was coded for by the bdellovibrios [5].
• Outer membrane preparations of Bdellovibrio bacteriovorus grown intraperiplasmically on Escherichia coli containing OmpF were prepared by the Triton X-100 procedure of Schnaitman (J. Bacteriol. 108:545-552, 1971) [6].
• The Braun lipoprotein was removed from the bdelloplast wall early, and OmpA was lost in the terminal part of the bdellovibrio growth cycle [7].

Chemical compound and disease context of Bdellovibrio

• Since gonococci also contain lipopolysaccharide that is similar in many respects to that contained within gram-negative rods, studies were conducted to determine the extent of gonococcal interaction with a variety of bdellovibrio species [3].
• An early event in the predatory lifestyle of Bdellovibrio bacteriovorus 109J is the attachment of diaminopimelic acid (DAP) to the peptidoglycan of its prey [8].
• Effects of methotrexate on intraperiplasmic and axenic growth of Bdellovibrio bacteriovorus [9].
• The change in hydrophobicity was inhibited by chloramphenicol, suggesting that bdellovibrio protein synthesis was required [10].
• Exogenous thymidine-5'-monophosphate competed effectively with [3H]thymine residues of E. coli as a precursor for bdellovibrio deoxyribonucleic acid; exogenous thymidine competed less effectively and thymine and uridine not at all [11].

Biological context of Bdellovibrio

• Downregulation of the motA gene delays the escape of the obligate predator Bdellovibrio bacteriovorus 109J from bdelloplasts of bacterial prey cells [12].

Anatomical context of Bdellovibrio

• With intraperiplasmic growth in the presence of added U-14C-labeled CMP, GMP, or UMP, radioactivity was found both in the respired CO2 and incorporated into the bdellovibrio cell components [13].

Gene context of Bdellovibrio

• These data show that the original cytoplasmic and periplasmic compartmentalization of the substrate cell ceases to exist with respect to small hydrophilic molecules during bdellovibrio attack [7].
• Growth of bdellovibrios on mutant prey which were defective in the expression of outer membrane proteins revealed that Bdellovibrio sp. could acquire the OmpC protein in the absence of the OmpF protein [14].
• Axenically grown Bdellovibrio stolpii (i.e., grown independently of the host) was examined for superoxide dismutase, catalase, and peroxidase activities [15].
• The results from the Bdellovibrio system provide that the 25-s and 17.5-S pre-rRNAs are normal stages of rRNA modification and are part of a multiple step maturation process, and therefore are not aberrations associated with the RNase III deficient mutation [16].

References