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1.
Ann Plast Surg ; 89(6): 679-683, 2022 12 01.
Artigo em Inglês | MEDLINE | ID: mdl-36416700

RESUMO

BACKGROUND: In implant-based breast surgery, infections remain a clinically challenging complication. Surgeons often prophylactically address this risk by irrigating the implant at the time of placement. However, there remain few data on the ideal irrigant for gram-negative species. METHODS: The authors assessed the relative efficacy of 10% povidone-iodine, triple-antibiotic solution, Prontosan, Clorpactin, and normal saline (negative control) against 3 gram-negative bacterial backgrounds: Escherichia coli , Pseudomonas aeruginosa , and Proteus species. A laboratory-adapted strain and a clinical isolate were selected for each group of bacteria. Sterile, smooth implant discs were immersed in each irrigant solution and then incubated in suspensions of each bacterial strain overnight at 37°C. Each disc was then rinsed and sonicated to displace biofilm-forming bacteria from the implant surface. The displaced bacteria were enumerated by plating, and normalized values were calculated for the bacterial counts of each irrigant. RESULTS: Povidone-iodine resulted in the greatest reduction of bacterial load for all 6 strains by a factor of 10 1 to 10 6 . Prontosan had a lesser, yet significant reduction in all bacterial strains. Triple-antibiotic solution demonstrated the greatest reduction in one Proteus species strain, and Clorpactin reduced bacterial counts in only half of the bacterial strains. When comparing laboratory strains to clinical isolates, significant differences were seen in each bacterial species in at least 2 irrigant solutions. CONCLUSIONS: Povidone-iodine has been proven the most effective at reducing bacterial contamination of E. coli, P. aeruginosa , and Proteus species in both laboratory-adapted strains and clinical isolates. CLINICAL RELEVANCE: This study proves that povidone-iodine is the most effective at preventing gram-negative infections in breast implant surgery.


Assuntos
Implante Mamário , Implantes de Mama , Humanos , Povidona-Iodo/farmacologia , Escherichia coli , Antibacterianos
2.
Vaccine ; 35(24): 3178-3185, 2017 05 31.
Artigo em Inglês | MEDLINE | ID: mdl-28479174

RESUMO

The lipoprotein OspA is produced by the Lyme disease spirochetes primarily in unfed ticks. OspA production is down-regulated by the blood meal and it is not produced in mammals except for possible transient production during late stage infection in patients with Lyme arthritis. Vaccination with OspA elicits antibody (Ab) that can target spirochetes in the tick midgut during feeding and inhibit transmission to mammals. OspA was the primary component of the human LYMErix™ vaccine. LYMErix™ was available from 1998 to 2002 but then pulled from the market due to declining sales as a result of unsubstantiated concerns about vaccination induced adverse events and poor efficacy. It was postulated that a segment of OspA that shares sequence similarity with a region in human LFA-1 and may trigger putative autoimmune events. While evidence supporting such a link has not been demonstrated, most efforts to move forward with OspA as a vaccine component have sought to eliminate this region of concern. Here we identify an OspA linear epitope localized within OspA amino acid residues 221-240 (OspA221-240) that lacks the OspA region suggested to elicit autoimmunity. A peptide consisting of residues 221-240 was immunogenic in mice. Ab raised against OspA221-240 peptide surface labeled B. burgdorferi in IFAs and displayed potent Ab mediated-complement dependent bactericidal activity. BLAST analyses identified several variants of OspA221-240 and a closely related sequence in OspB. It is our hypothesis that integration of the OspA221-240 epitope into a multivalent-OspC based chimeric epitope based vaccine antigen (chimeritope) could result in a subunit vaccine that protects against Lyme disease through synergistic mechanisms.


Assuntos
Anticorpos Antibacterianos/sangue , Antígenos de Superfície/imunologia , Proteínas da Membrana Bacteriana Externa/imunologia , Vacinas Bacterianas/imunologia , Borrelia burgdorferi/imunologia , Epitopos/imunologia , Lipoproteínas/imunologia , Vacinas contra Doença de Lyme/imunologia , Peptídeos/imunologia , Animais , Antígenos de Bactérias/imunologia , Antígenos de Superfície/química , Antígenos de Superfície/genética , Proteínas da Membrana Bacteriana Externa/química , Proteínas da Membrana Bacteriana Externa/genética , Vacinas Bacterianas/química , Vacinas Bacterianas/genética , Borrelia burgdorferi/química , Borrelia burgdorferi/genética , Borrelia burgdorferi/crescimento & desenvolvimento , Descoberta de Drogas , Epitopos/química , Imunoglobulina G/sangue , Ixodes/microbiologia , Lipoproteínas/química , Lipoproteínas/genética , Doença de Lyme/prevenção & controle , Camundongos , Peptídeos/administração & dosagem , Peptídeos/química , Reação em Cadeia da Polimerase , Ensaios de Anticorpos Bactericidas Séricos , Vacinação , Vacinas de Subunidades Antigênicas/administração & dosagem , Vacinas de Subunidades Antigênicas/imunologia
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