Relevant bibliographies by topics / Serum bactericidal activity

Academic literature on the topic 'Serum bactericidal activity'

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Published: 14 March 2023

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Journal articles on the topic "Serum bactericidal activity"

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Dalhoff, A., H. Stass, and S. Obertegger. "Serum Bactericidal Activity of Moxifloxacin." Drugs 58, Supplement 2 (1999): 184–85. http://dx.doi.org/10.2165/00003495-199958002-00054.

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Plouffe, J. F., M. F. Para, and K. A. Fuller. "Serum bactericidal activity against Legionella pneumophila." Journal of Clinical Microbiology 22, no. 5 (1985): 863–64. http://dx.doi.org/10.1128/jcm.22.5.863-864.1985.

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Gordon, David L. "Serum bactericidal activity against Haemophilus influenzae." Pathology 20, no. 2 (1988): 124–29. http://dx.doi.org/10.3109/00313028809066622.

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CIALDELLA, JOYCE I., ROGER G. ULRICH, and VINCENT P. MARSHALL. "Augmentation of serum bactericidal activity by paldimycin." Journal of Antibiotics 41, no. 5 (1988): 660–66. http://dx.doi.org/10.7164/antibiotics.41.660.

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Pramoonjago, P., T. Kinoshita, K. S. Hong, Y. Takata-Kozono, H. Kozono, R. Inagi, and K. Inoue. "Bactericidal activity of C9-deficient human serum." Journal of Immunology 148, no. 3 (February 1, 1992): 837–43. http://dx.doi.org/10.4049/jimmunol.148.3.837.

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Abstract Escherichia coli B/SM, strain 1-1, was killed dose dependently by human hereditary C9-deficient serum (C9DHS), which was shown to contain no C9 Ag by an ELISA method. On the other hand, human hereditary C7-deficient serum did not kill the bacteria under similar conditions. The bactericidal activity of C9DHS was inhibited by rabbit anti-C5 antibody but not by murine anti-C9 mAb. The anti-C9 antibody decreased the bactericidal activity of normal human serum (NHS) to the level of that with C9DHS. Sheep anti-human lysozyme antibody did not affect the bactericidal activity of C9DHS or NHS even when added at more than twice the concentration required to block the serum lysozyme activity on Micrococcus luteus. After treatment with C9DHS and washing, surviving Escherichia coli were killed by C9, but not by lysozyme, transferrin, or both. Other strains of E. coli (K12 W3110, C600, and NIHJ) and Salmonella typhimurium (strain NCTC 74), all maintained in the laboratory, were also killed by C9DHS. However, pathogenic strains recently isolated from patients with traveler's diarrhea and some strains of S. typhimurium were resistant to both C9DHS and NHS, at least at the serum concentration tested. A concentration of 0.1 M Tris did not increase the susceptibility of serum-resistant strains of bacteria to C9DHS, but made one strain of S. typhimurium tested susceptible to NHS, but not to C9DHS. These results clearly showed that C9DHS kills bacteria that are sensitive to NHS through activation of C up to the step of C8 in the same way that C9-deficient C serum lyzed sensitized erythrocytes.
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Dudley, Michael N., Hilary D. Mandler, Kenneth H. Mayer, and Stephen H. Zinner. "Serum Inhibitory and Bactericidal Activity of Ciprofloxacin following Intravenous Administration." DICP 23, no. 6 (June 1989): 456–60. http://dx.doi.org/10.1177/106002808902300603.

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Serum inhibitory and bactericidal titers were measured in nine healthy volunteers following single iv doses of ciprofloxacin 100, 150, and 200 mg. The median peak serum bactericidal titer (5 minutes following completion of a 30-minute infusion) against two highly susceptible strains of Escherichia coli ranged between 1:64 and 1:1024 and titers exceeded 1:8 for six hours for all dose levels. The bactericidal titers against two strains of Pseudomonas aeruginosa and a methicillin-resistant strain of Staphylococcus aureus were considerably lower, the median peak being 1:2 at all dose levels. Measured inhibitory and bactericidal titers at five minutes and one hour postinfusion were significantly greater than those predicted (measured serum ciprofloxacin concentration to minimum inhibitory concentration [MIC] or minimum bactericidal concentration [MBC]) for only one strain of E. coli. Intravenous doses of ciprofloxacin 100–200 mg produce high and sustained serum bactericidal titers against highly susceptible bacteria; considerably lower levels of activity are seen against bacteria having higher MICs and MBCs but still considered susceptible to the drug.
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LeBel, Marc, Michel Pellerin, Michel G. Bergeron, Giselle Rivera, and Marthe Huot. "Serum Bactericidal Activity of Ceftazidime Increased by Netilmicin." Drug Intelligence & Clinical Pharmacy 19, no. 12 (December 1985): 932–36. http://dx.doi.org/10.1177/106002808501901215.

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Desar, I. M. E., M. van Deuren, T. Sprong, J. B. M. J. Jansen, F. Namavar, C. M. Vandenbroucke-Grauls, and J. W. M. van der Meer. "Serum bactericidal activity againstHelicobacter pyloriin patients with hypogammaglobulinaemia." Clinical & Experimental Immunology 156, no. 3 (June 2009): 434–39. http://dx.doi.org/10.1111/j.1365-2249.2009.03909.x.

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BORROW, R., P. BALMER, and E. MILLER. "Meningococcal surrogates of protection?serum bactericidal antibody activity." Vaccine 23, no. 17-18 (March 18, 2005): 2222–27. http://dx.doi.org/10.1016/j.vaccine.2005.01.051.

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Shah, P. M. "Serum bactericidal activity of levofloxacin against Streptococcus pneumoniae." Journal of Antimicrobial Chemotherapy 43, no. 90003 (June 1, 1999): 61–65. http://dx.doi.org/10.1093/jac/43.suppl_3.61.

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Dissertations / Theses on the topic "Serum bactericidal activity"

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Gonzalez, Munoz Beatriz. "Analysis of the bactericidal activity of naive rabbit serum against Staphylococcus aureus." Thesis, University of Sheffield, 2015. http://etheses.whiterose.ac.uk/12302/.

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Staphylococcus aureus is a commensal bacterium that can also act as an opportunistic pathogen, causing a wide range of diseases in humans and in economically important livestock such as cows and rabbits. S. aureus quickly develops resistance against antibiotics and also evades the immune system of the host. As current treatments are difficult and expensive, new antibiotics, vaccines and the use of elements of the immune system are currently being studied as novel control approaches. A novel bactericidal mechanism able to kill S. aureus present in naive rabbit serum (NRS) was previously discovered in our laboratory. The bactericidal activity of the NRS had been characterized and the importance of the wall teichoic acids (WTA) on the bacteria for susceptibility was identified previously, but the mechanism involved in the bacterial killing remained unknown. In this study the role of the WTA as the bacterial receptor that interacts with the ‘killing factor’ present in the NRS was established. The importance of WTA modifications were also determined in pathogen resistance to the NRS killing mechanism. Use of bacterial cell wall material as an affinity matrix led to the identification of secreted phospholipase A2 (sPLA2) as a potential part of the bactericidal mechanism. The use of a range of inhibitors and specific antibodies confirmed sPLA2 as part of the killing mechanism. Purified sPLA2 from a number of species was tested and cobra sPLA2 (cvPLA2) was able to kill S. aureus in buffer but led to bacterial growth when added to NRS. This suggests that cvPLA2 interacts with rabbit serum components and this results in inactivation of both cvPLA2 and the bactericidal activity of the NRS. Annexin A1, a known regulator of PLA2, was identified through mass spectrometry as a serum protein also bound to the cell wall affinity matrix. This protein enhanced the bactericidal activity of cvPLA2 against S. aureus by direct protein-protein interaction. A model of NRS staphylococcal activity is presented.
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Wojno, Justyna Maria. "Serum bactericidal activity of colistin against Acinetobacter baumannii in patients with normal versus impaired renal function." Master's thesis, University of Cape Town, 2011. http://hdl.handle.net/11427/2721.

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Whitters, Deborah. "The role of impaired serum bactericidal activity in chronic Pseudomonas aeruginosa infection in non cystic fibrosis bronchiectasis." Thesis, University of Birmingham, 2018. http://etheses.bham.ac.uk//id/eprint/8548/.

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Non Cystic Fibrosis bronchiectasis is characterised by perpetual neutrophilic inflammation in the lungs. The ongoing vicious cycle of bronchiectasis leads to further damage to already damaged airways and is a culmination of repeated infection, inflammation and failure of the host response to maintain sterility of the airway, despite a sophisticated innate and adaptive immune system. Pseudomonas aeruginosa commonly colonises the lungs of patients with bronchiectasis. I hypothesised that the concept of inhibitory antibodies in the serum may be a feature of Pseudomonas aeruginosa colonisation through a specific interaction between the host adaptive immune system and strain specific features. Here I have identified a mechanism where some patients colonised with Pseudomonas aeruginosa produce IgG2 antibodies specifically against the O antigen of bacterial LPS, which rather than promote complement-mediated killing actually inhibits it.
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Attia, Ahmed Sherif. "The USPA2 protein and serum resistance of Moraxella Catarrhalis." Access to abstract only; dissertation is embargoed until after 5/15/2007, 2006. http://www4.utsouthwestern.edu/library/ETD/etdDetails.cfm?etdID=145.

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NDONI, ENEA. "Characterization of the immune response and cross protection activity elicited by the Neisserial Heparin Binding Antigen (NHBA), a component of the 4CMenB vaccine." Doctoral thesis, Università di Siena, 2017. http://hdl.handle.net/11365/1011542.

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Invasive disease caused by capsular group B Neisseria meningitidis (MenB) is life threating disease causing hundred thousands of deaths every year, still remaining an unmet medical need in many countries. Although disease can be observed at all age groups, infants and adolescents are the most at risk populations showing the highest incidence in case numbers. Since the MenB capsule was not-immunogenic the development of a MenB vaccine which makes the use of other antigens becomes necessary. 4CMenB is a multicomponent vaccine against serogroup B N. meningitidis composed by three major protein antigens, factor H-binding protein (fHbp), Neisserial Heparin-Binding Antigen (NHBA) and Neisserial adhesin A (NadA), combined with outer membrane vesicles (OMVs) from the New-Zealand epidemic strain (NZ98/254). Neisserial Heparin Binding Antigen (NHBA) is a surface-exposed lipoprotein expressed by all N. meningitidis strains analyzed so far and is composed of two major domains, a highly variable amino-terminal (N-term) domain which anchors the protein on the bacterial outer membrane through the lipobox motif, and a highly conserved carboxyl-terminal (C-term) domain. These domains are separated by a short and quite conserved Arginine-rich (Arg-rich) motif which has been reported to be involved in different mechanisms that mediate meningococci adhesion, infection and survival within the host’s blood stream. NHBA is susceptible to cleavage by NalP, a bacterial protease which has its cleavage site upstream of the arginine region. Moreover human proteases such as human lactoferrin (hLf) and kallikrein are able to process NHBA downstream the the Arg-rich region. Both bacterial and human proteases-mediated cleavage releases the C-term of NHBA in the supernatant, while the N-term of the protein remains anchored on the bacterial surface. NalP cleavage did not impact SBA titers elicited by anti-NHBA antibodies but little is known about the impact that host’s proteases have on bactericidal titers. Based on sequence analysis it has been reported that NHBA has two major alleles, the so called “short” and “long” variants, which differentiate by the presence or absence of a 190 bp long fragment. Despite its sequence variability, NHBA is able to induce a robust and broad immune response against meningococcal strains expressing vaccine homologous and heterologous variants. Although anti-NHBA antibodies are able to induce bacterial killing when tested in serum bactericidal activity assay (SBA), the regions involved in eliciting cross protective immune response remain still unknown. Aims of this study were to use monoclonal antibodies (mAbs) raised against the NHBA vaccine variant peptide 2 (NHBAp2) to (i) map the NHBA regions involved in eliciting the functional response, (ii) test their ability to induce cross protection against strains expressing epidemiologically relevant homologous and heterologous NHBA variants, and (iii) investigate the molecular mechanism of NHBA-mediated bactericidal activity. To this end we used a panel of anti-NHBA mAbs selected to recognize different regions of the protein. Our results showed that only anti-N-term mAbs were able to induce killing of bacterial strains expressing the homologous NHBAp2 and closely related heterologous NHBA variants. Synergy between monoclonal antibodies targeting the N-term and the C-term of NHBA resulted in a significant increase of bactericidal titers but cross protection remained restricted to closely phylogenetic NHBA variants. Anti C-term mAbs were not able to induce SBA activity when tested individually, but surprisingly they became bactericidal when tested in combination. Moreover they were able to induce full cross protection against a panel of strains expressing phylogenetically distant heterologous NHBA variants. Our results suggest that the partial release of the NHBA C-terminal portion upon NalP and serum proteases could explain why anti-C-term mAbs are not able to induce complement mediated bactericidal killing when tested individually. However, the simultaneous binding of C-term mapping mAbs on the same NHBA molecule can induce the formation of a very stable ternary complex that probably allows a more efficient C1q engagement and C3 deposition, thus leading to the observed co-operative bactericidal activity. These results suggest that synergy between anti-NHBA antibodies is at the basis of the mechanism of NHBA-induced bactericidal activity, which could explain the robust and cross-protective immune response elicited by anti-NHBA polyclonal antibodies following immunization. Collectively, the body of experimental data suggests that both domains of NHBA are required to elicit complement mediated bactericidal activity against strains expressing the vaccine homologous and heterologous NHBA variants.
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Book chapters on the topic "Serum bactericidal activity"

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Semchenko, Evgeny A., Freda E. C. Jen, Michael P. Jennings, and Kate L. Seib. "Assessment of Serum Bactericidal and Opsonophagocytic Activity of Antibodies to Gonococcal Vaccine Targets." In Methods in Molecular Biology, 363–72. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1900-1_19.

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Kuevda, Tatyana, Tatiana Sataieva, Pavel Ostapchuk, Elena Usmanova, Denis Zubochenko, Alla Zubochenko, Anna Pikhtereva, Olga Postnikova, Ludmila Shevkoplyas, and Tatyana Logadyr. "Satureja Montana L. Essential Oil Influence on the Blood Component Composition and the Serum Bactericidal Activity." In XV International Scientific Conference “INTERAGROMASH 2022”, 1724–31. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-21432-5_185.

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Conference papers on the topic "Serum bactericidal activity"

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Seidler, Tassilo, Thomas Alter, Monika Krüger, and Karsten Fehlhaber. "Transport stress - consequences for bacterial translocation, endogenous contamination and bactericidal activity of serum of slaughter pigs." In Fourth International Symposium on the Epidemiology and Control of Salmonella and Other Food Borne Pathogens in Pork. Iowa State University, Digital Press, 2001. http://dx.doi.org/10.31274/safepork-180809-1163.

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Ovcharova, A. N. "Use of probiotic lactobacilli to increase non-specific resistance and productivity of rabbits." In CURRENT STATE, PROBLEMS AND PROSPECTS OF THE DEVELOPMENT OF AGRARIAN SCIENCE. Federal State Budget Scientific Institution “Research Institute of Agriculture of Crimea”, 2020. http://dx.doi.org/10.33952/2542-0720-2020-5-9-10-136.

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The article presents the results of the effectiveness of probiotic lactobacilli on the productivity and non-specific resistance of rabbits. The phagocytic activity of neutrophils increased by 10 %, which turns out to be statistically significant. The bactericidal activity of blood increased by 8 % in comparison with the control group; the phagocytic index was also higher in the experimental group by 2.02. The content of lysozyme in the blood serum of rabbits in the experimental group was significantly higher than the control parameters by 18.6 micrograms/ml. As tentative results, we report an increase in the live weight and growth rate in the experimental group of rabbits.
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Desai, Himanshu, Catherine Wrona, Timothy F. Murphy, and Sanjay Sethi. "Mechanisms Of Decline In Serum Bactericidal Activity For Nontypeable Haemophilus Influenzae (NTHI) In COPD Patients Chronically Colonized With NTHI." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2911.

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