Effect of toothpaste with natural calcium carbonate/perlite on extrinsic tooth stain.

OBJECTIVE: The current study was designed to determine the effect of natural calcium carbonate toothpaste containing Perlite and microgranules (Whitening toothpaste) on extrinsic tooth stain compared to a standard commercial toothpaste formulation with precipitated calcium carbonate (PCC) as abrasive and a commercial toothpaste with dicalcium phosphate dihydrate (DCPD) as abrasive. METHODS: The toothpastes were evaluated in a double blind, three-cell, stratified (tobacco use; baseline tooth stain level), parallel group design study involving 600 subjects with extrinsic tooth stain. Subjects brushed twice daily with their allocated toothpaste for four weeks. Extrinsic tooth stain was measured using the Macpherson modification of the Lobene stain index. RESULTS: ANCOVA showed significant differences between toothpastes (p=0.037). Subsequent multiple comparisons using pairwise t-tests, showed the Whitening toothpaste to be superior to the DCPD toothpaste (p=0.014) and the PCC toothpaste (p=0.067). When a Box-Cox transformation was made to the data (y0.6) to improve normality, these two differences were more accurately estimated at p=0.004 and p=0.03 respectively. CONCLUSION: The Whitening toothpaste has been shown to be significantly more effective in tooth stain removal than the two standard commercial toothpaste formulations.

Inhibition of HIV infection by baicalin--a flavonoid compound purified from Chinese herbal medicine.

Baicalin (BA), (formulated as 7-D-glucuronic acid-5,6-dihydroxy-flavone), was purified from the plant Scutellaria Baicalensis Georgi. It has been used as a traditional Chinese herbal medicine. The inhibitory effect of BA against human immunodeficiency virus (HIV-1) infection and replication has been studied in vitro. The compound inhibits HIV-1 infection and replication as measured by: (1) a quantitative focal syncytium formation on CEM-ss monolayer cells; and (2) HIV-1 specific core antigen p24 expression and retroviral reverse transcriptase (RT) activity in the HIV-1-infected H9 cells. We have further demonstrated that the enzymatic activity of purified recombinant HIV-1/RT was inhibited by BA. In addition to lymphoid cell lines, the anti-HIV-1 activity of BA was also observed in cultures of primary human peripheral blood mononuclear cells infected with HIV-1 in vitro. Neither cytotoxic nor cytostatic effects on the indicator cells were found under the assay condition. This data suggests that BA may serve as a useful drug for the treatment and prevention of HIV infections.

Inhibition of human T cell leukemia virus by the plant flavonoid baicalin (7-glucuronic acid, 5,6-dihydroxyflavone).

The ability of baicalin (7-glucuronic acid, 5,6-dihydroxyflavone), a flavonoid compound purified from the Chinese medicinal herb, Scutellaria baicalensis georgi, to inhibit human T cell leukemia virus type I (HTLV-I) was examined. Baicalin produced concentration-dependent inhibition of HTLV-I replication in productively infected T and B cells. Moreover, baicalin treatment selectively reduced the detectable levels of HTLV-I p19 gag protein in infected cells by greater than 70% at concentrations that produced insignificant effects on total cellular protein and DNA synthesis with no loss in cell viability. Resistance to HTLV-I infection and virus-mediated transformation was noted in uninfected peripheral blood lymphocytes pretreated with baicalin before cocultivation with lethally irradiated chronically infected cells. Baicalin inhibited reverse transcriptase activity in HTLV-I-infected cells as well as the activity of purified reverse transcriptase from Moloney murine leukemia virus and Rous-associated virus type 2. These results suggest that baicalin may be a potential therapeutic agent against HTLV-I-associated T cell diseases.

Transcription-inhibition and RNA-binding domains of influenza A virus matrix protein mapped with anti-idiotypic antibodies and synthetic peptides.

We have undertaken by biochemical and immunological experiments to locate the region of the matrix (M1) protein responsible for down-regulating endogenous transcription of A/WSN/33 influenza virus. A more refined map of the antigenic determinants of the M1 protein was obtained by binding of epitope-specific monoclonal antibodies (MAbs) to chemically cleaved fragments. Epitope 2-specific MAb 289/4 and MAb 7E5 reverse transcription inhibition by M1 protein and react with a 4-kilodalton cyanogen bromide fragment extending from amino acid Gly-129 to Gln-164. Anti-idiotype serum immunoglobulin G prepared in rabbits immunized with MAb 289/4 or MAb 7E5 mimicked the action of M1 protein by inhibiting transcription in vitro of influenza virus ribonucleoprotein cores. This transcription-inhibition activity of anti-MAb 7E5 immunoglobulin G and anti-MAb 289/4 immunoglobulin G could be reversed by MAb 7E5 and MAb 289/4 or could be removed by MAb 7E5-Sepharose affinity chromatography. Transcription of influenza virus ribonucleoprotein was inhibited by one of three synthetic oligopeptides, a nonodecapeptide SP3 with an amino acid sequence corresponding to Pro-90 through Thr-108 of the M1 protein. Of all the structural proteins of influenza virus, only NP and M1 showed strong affinity for binding viral RNA or other extraneous RNAs. The 4-kilodalton cyanogen bromide peptide (Gly-129 to Gln-164), exhibited marked affinity for viral RNA, the binding of which was blocked by epitope 2-specific MAb 7E5 but not by MAbs directed to three other epitopes. Viral RNA also bound strongly to the nonodecapeptide SP3 and rather less well to anti-idiotype anti-MAb 7E5; these latter viral RNA-binding reactions were only slightly blocked by preincubation of anti-MAb 7E5 or SP3 with MAb 7E5. These experiments suggest the presence of at least two RNA-binding sites, which also serve as transcription-inhibition sites, centered around amino acid sequences 80 through 109 (epitope 4?) and 129 through 164 (epitope 2) of the 252 amino acid M1 protein of A/WSN/33 influenza virus. A hydropathy plot of the M1 protein calculated by free-energy transfer suggests that the two hydrophilic transcription-inhibition RNA-binding domains are brought into close proximity by an alpha-helix-forming intervening hydrophobic domain.

Transient expression and sequence of the matrix (M1) gene of WSN influenza A virus in a vaccinia vector.

A cDNA encoding the entire amino acid sequence of the matrix (M1) protein of influenza A/WSN/33 virus was cloned, sequenced, and expressed in a vaccinia virus system consisting of the T7 bacteriophage RNA polymerase and a plasmid carrying the M1 gene flanked by T7 polymerase promoter and terminator sequences. The transiently expressed M1 gene product comigrated on SDS-polyacrylamide gels with the endogenous WSN virus M1 protein and was recognized in Western blot analysis by three epitope-specific monoclonal antibodies directed to the M1 protein. The nucleotide sequence and the predicted amino acid sequence of the cloned WSN virus M1 coding region was found to be more than 97% homologous to that of the M1 gene of influenza virus A/PR/8/34 reported by G. Winter and S. Fields (Nucleic Acids Res. 8, 1965-1974, 1980).

Molecular characterization of ilvC specialized transducing phages of Escherichia coli K-12.

A series of lambda defective ilvC specialized transducing phage has been isolated which carry regions of isoleucine and valine structural and regulatory genes derived from the ilv cluster at minute 83 on the linkage map of the chromosome of Escherichia coli K-12. The ilv genes carried by these phages and their order have been determined by transduction of auxotrophs. The ilvC+ lysogen of an ilvC- strain gave rise, after heat induction of the lysogen, to transducing particles which carried the wild-type allele of the cya-marker. Further experiments have shown that the lambda defective ilvC phages were able to cotransduce a rho-15ts mutation as well as a rep-5 mutation. Hence, the order of the clockwise excision of the ilv cluster was found to be ilvC-rho-rep-cya. Enzyme levels in strains carrying the lambda defective ilvC phages indicated the the ilvC gene was not altered by the insertion of lambda into the ilv cluster. The isolation and digestion of lambda defective ilvC DNA by EcoRI and HindIII restriction endonucleases demonstrated that the specialized transducing phages carried part of the genome from the E. coli K-12 chromosome.

Evidence for the site of lambda insertion in the ilv gene cluster of Escherichia coli K-12.

The experiments reported herein provide evidence that the secondary site of lambda is in the ilvC instead of the ilvA gene.