[Show abstract][Hide abstract] ABSTRACT: An evaluation is made of bacterial species and susceptibility to various antibiotics used in application to odontogenic infections of periapical location and in pericoronitis of the lower third molar, with the aim of optimizing the antibiotherapy of such infections and thus preventing unnecessary side effects and over-treatment.
Sixty-four patients with odontogenic infection were selected on the basis of a series of inclusion and exclusion criteria. Samples were collected from lesions under maximally aseptic conditions, avoiding oral saprophytic contamination. The samples were cultured and incubated under aerobic and anaerobic conditions, followed by bacteriological identification and antibiotic susceptibility testing.
A total of 184 bacterial strains were isolated and identified, comprising grampositive facultative anaerobes (68%), gramnegative strict anaerobes (30%) and grampositive facultative anaerobes (2%). Regardless of the origin of the odontogenic infection, the causal bacteria yielded the best results in terms of increased sensitivity and lesser resistance with amoxicillin / clavulanate and amoxicillin, respectively (p<0.05).
There are increasingly numerous reports in the literature of growing bacterial resistance to antibiotics in infectious processes affecting non-buccodental territories. This same tendency has not been observed in relation to oral infections, though important resistance has been documented for certain concrete antibiotics. According to our results, the common-use antibiotics with the greatest sensitivity and lowest resistance were shown to be amoxicillin/clavulanate followed by amoxicillin alone.
[Show abstract][Hide abstract] ABSTRACT: The cell wall of Corynebacterium glutamicum contains the cation-selective channel (porin) PorA(C.glut) and the anion-selective channel PorB(C.glut) for the passage of hydrophilic solutes. Lipid bilayer experiments with organic solvent extracts of whole C. glutamicum cells cultivated in minimal medium suggested that also another cation-selective channel-forming protein, named PorH(C.glut), is present in C. glutamicum. The protein was purified to homogeneity by fast-protein liquid chromatography across a HiTrap-Q column. The pure protein had an apparent molecular mass of about 12 kDa on SDS-PAGE. Western blot analysis suggested that the cell wall channel is presumably formed by protein oligomers. The purified protein forms cation-selective channels with an average single-channel conductance of about 2.5 nS in 1 M KCl in the lipid bilayer assay. The PorH(C.glut) protein was partially sequenced, and based on the resulting amino acid sequence, the corresponding gene, designated as porH(C.glut), was identified in the published genome sequence of C. glutamicum ATCC13032. PorH(C.glut) contains only the inducer methionine but no N-terminal extension, which suggests that the export and assembly of the protein follow a yet unknown pathway. PorH(C.glut) is coded in the bacterial chromosome by a gene that is localized in the vicinity of porA(C.glut), within a putative operon of 13 genes. RT-PCR revealed that both porins are cotranscribed. They coexist according to immunological detection experiments in the cell wall of C. glutamicum together with PorB(C.glut) and PorC(C.glut).
[Show abstract][Hide abstract] ABSTRACT: A cation-selective channel (porin), designated PorA, facilitates the passage of hydrophilic solutes across the cell wall of the mycolic acid-containing actinomycete Corynebacterium glutamicum. Biochemical and electrophysiological investigations of the cell wall of the mutant strain revealed the presence of an alternative channel-forming protein. This porin was purified to homogeneity and studied in lipid bilayer membranes. It forms small anion-selective channels with a diameter of about 1.4 nm and an average single-channel conductance of about 700 pS in 1 M KCl. The PorBCglut channel could be blocked by citrate in a dose-dependent manner. This result was in agreement with growth experiments in citrate as sole carbon source where growth in citrate was impaired as compared with growth in other carbon sources. The PorBCglut protein was partially sequenced and based on the resulting amino acid sequence of the corresponding gene, which was designated as porB, was identified as an unannotated 381 bp long open reading frame (ORF) in the published genome sequence of C. glutamicum ATCC13032. PorBCglut contains 126 amino acids with an N-terminal extension of 27 amino acids. One hundred and thirty-eight base pairs downstream of porB, we found an ORF that codes for a protein with about 30% identity to PorBCglut, which was named PorCCglut. The arrangement of porB and porC on the chromosome suggested that both genes belong to the same cluster. RT-PCR from overlapping regions between genes from wild-type C. glutamicum ATCC 13032 and its ATCC 13032DeltaporA mutant demonstrated that this is the case and that porB and porC are cotranscribed. The gene products PorBCglut and PorCCglut represent obviously other permeability pathways for the transport of hydrophilic compounds through the cell wall of C. glutamicum.
[Show abstract][Hide abstract] ABSTRACT: The cell wall of the gram-positive bacterium Corynebacterium glutamicum contains a channel (porin) for the passage of hydrophilic solutes. The channel-forming polypeptide PorA is a 45-amino-acid acidic polypeptide with an excess of four negatively charged amino acids, which is encoded by the 138-bp gene porA. porA was deleted from the chromosome of C.glutamicum wild-type strain ATCC 13032 to obtain mutant ATCC 13032deltaporA. Southern blot analysis demonstrated that porA was deleted. Lipid bilayer experiments revealed that PorA was not present in the cell wall of the mutant strain. Searches within the known chromosome of C. glutamicum by using National Center for Biotechnology Information BLAST and reverse transcription-PCR showed that no other PorA-like protein is encoded on the chromosome or is expressed in the deletion strain. The porA deletion strain exhibited slower growth and longer growth times than the C. glutamicum wild-type strain. Experiments with different antibiotics revealed that the susceptibility of the mutant strain was much lower than that of the wild-type C. glutamicum strain. The results presented here suggest that PorA represents a major hydrophilic pathway through the cell wall and that C. glutamicum contains cell wall channels which are not related to PorA.
Journal of Bacteriology 09/2003; 185(16):4779-86. DOI:10.1128/JB.185.16.4779-4786.2003 · 2.69 Impact Factor