Having studied in vitro the effect of UVR on the two species of microorganisms which are most common as agents of surgical infection, we realized the closer the distance from the irradiation lamp and the longer the irradiation time, the stronger the bactericidal effect of UVR. When UVR is applied for air disinfection within the distance of more than 2 meters from the sunlamp irradiation, it can also reduce significantly the number of microorganisms in the air. It is due to the fact that there is a continuous air exchange between the upper and the lower part of the room. Previous studies and the experiments on petri dishes show that the use of UVR for cleaning infected wounds and preventing infection is an effective, simple and safe measure
Ultraviolet Rays ; Blood Bactericidal Activity

AIMTo report the detection in vitro of secretory inhibitor of platelet microbicidal protein (SIPMP) phenotypes of urethral isolates along with a comparison with isolates from patients with or without chronic bacterial prostatitis (CBP).

METHODSUrethral isolates of Staphylococcus spp. (n=4), diphtheroids (n=28), micrococci (n=15), streptococci (n=21), Enterobacteriaceae (n=9) and Enterococcus faecalis (n=19) from patients with or without CBP were tested. SIPMP production was tested by inhibition of platelet microbicidal protein (PMP) bioactivity against Bacillus subtilis and was expressed as percentage of inhibition of PMP bactericidal activity.

RESULTSA significantly higher proportion of CBP-strains (57.78% vs. 16.67%) reduced PMP-induced killing of Bacillus subtilis than non-CBP strains did (P<0.01). SIPMP levels of staphylococci and Enterococcus faecalis from the CBP group were significantly higher than those of the control group.

CONCLUSIONThese results suggest that SIPMP production is associated with the CBP source. Data from the present study might have significant implications for the understanding of the pathogenesis of CBP.

Blood Bactericidal Activity ; physiology ; Blood Platelets ; metabolism ; Chronic Disease ; Humans ; In Vitro Techniques ; Male ; Phenotype ; Prostatitis ; metabolism ; microbiology ; Urethra ; microbiology ; beta-Thromboglobulin ; antagonists & inhibitors

OBJECTIVETo construct pBV-BPI600-Fcgamma1(700) recombinant expression vector, to transform it into Escherichia coli DH5alpha, and to induce the expression of BPI23-Fcgamma1 anti-bacterial recombinant protein.

METHODSGenes coding for BPI23 and Fcgamma1 were amplified by RT-PCR from mRNA extracted from HL-60 cell and normal human leukocytes; recombinant cloning vector and recombinant expression vector were then constructed. pBV-BPI600-Fcgamma1(700) recombinant expression vector was transformed into the competent Escherichia coli DH5alpha and BPI23-Fcgamma1 recombinant protein was expressed by a temperature-induced method.

RESULTS(1) Expected amplified products BPI600hp and Fcgamma1(700bp) were obtained by RT-PCR method. (2) pUC18-BPI180, pUC18-BPI420 and pUC18-Fcgamma1(700) recombinant cloning vector were successfully constructed, and sequences were identical with the reported ones. 3) pBV-BPI600-Fcgamma1(700) recombinant expression vector was successfully constructed, and the enzyme digestion analysis showed an expected result. (4) The expression level of BPI23-Fcgamma1 recombinant protein accounted for 20% of total bacterial proteins. (5) The renatured BPI23-Fcgamma1 recombinant protein showed bacteriocidal activity and biological function of complement fixation, and opsonization.

CONCLUSIONpBV-BPI600-Fcgamma1(700) recombinant expression vector was successfully constructed, and BPI23-Fcgamma1 recombinant protein with double biological activity of BPI and IgGFc was expresed in Escherichia coli.

Antimicrobial Cationic Peptides ; Blood Bactericidal Activity ; drug effects ; Blood Proteins ; biosynthesis ; genetics ; pharmacology ; Carrier Proteins ; biosynthesis ; genetics ; pharmacology ; Cell Adhesion Molecules ; Escherichia coli ; genetics ; metabolism ; Genetic Vectors ; HL-60 Cells ; Humans ; Membrane Proteins ; Recombinant Fusion Proteins ; biosynthesis ; genetics ; pharmacology

OBJECTIVETo develop and investigate GLL-37, a substitution analogue of the human antimicrobial peptide LL-37 with anti-enzymatic degradation activity and improved efficacy.

METHODSThe bactericidal activities of LL-37 and newly developed GLL-37 against 6 Gram-negative and -positive bacteria were determined by Broth microdilution assays. The minimum inhibitory concentrations of LL-37 and GLL-37 against E.coli ATCC 25922 in different NaCl concentration medium were also detected. Both peptides were co-incubated with elastase, and then analyzed by PAGE electrophoresis and bactericidal activity determination.

RESULTGLL-37 showed a stronger elastase resistance ability than LL-37, and was significantly more effective than LL-37 under high-salt condition.

CONCLUSIONThe antimicrobial peptide GLL-37 derived form LL-37 has the potential as a new therapeutic agent for bacterial infections.

Animals ; Anti-Bacterial Agents ; pharmacology ; therapeutic use ; Antimicrobial Cationic Peptides ; pharmacology ; therapeutic use ; Blood Bactericidal Activity ; drug effects ; Cathelicidins ; Cell Membrane Permeability ; drug effects ; Escherichia coli ; drug effects ; Female ; Humans ; Membrane Proteins ; metabolism ; Monocytes ; drug effects ; Pseudomonas Infections ; drug therapy