scholarly journals Resistance ofPseudomonas pseudomalleito Normal Human Serum Bactericidal Action

1988 ◽  
Vol 32 (7) ◽  
pp. 645-652 ◽  
Author(s):  
Ghazally Ismail ◽  
Nyonya Razak ◽  
Rahmah Mohamed ◽  
Noor Embi ◽  
Othman Omar
Keyword(s):  
Human Serum ◽  
Normal Human Serum ◽  
Bactericidal Action ◽  
Normal Human

scholarly journals THE PROPERDIN SYSTEM AND IMMUNITY

1956 ◽  
Vol 103 (5) ◽  
pp. 553-575 ◽  
Author(s):  
Alastair C. Wardlaw ◽  
Louis Pillemer
Keyword(s):  
Human Serum ◽  
Bactericidal Activity ◽  
Quantitative Relationship ◽  
Normal Human Serum ◽  
Natural Resistance ◽  
Bactericidal Action ◽  
Individual Strain ◽  
Normal Human ◽  
Resistant Strains ◽  
The Individual

Methods for the preparation and standardization of reagents suitable for studies on the bactericidal action of the properdin system are described. The preparation and properties of serum free of properdin (RPb) are presented in detail because of the necessity for a suitable RPb in these studies. The properdin system is responsible for the bactericidal action of normal human serum against a variety of microorganisms. The present work shows that the removal of properdin from serum also removes bactericidal activity. Addition of properdin to properdin-deficient serum restores bactericidal activity. A quantitative relationship exists between the final properdin concentration and bactericidal activity against sensitive organisms. The possibilities of a bactericidal assay for properdin are discussed. It is demonstrated that, in addition to properdin, the four components of complement (present in RPb) are necessary for the destruction of properdinsensitive bacteria. If any component is missing, bactericidal activity is lost; when the component is replaced, bactericidal activity is restored. Magnesium is also necessary for the bactericidal activity of the properdin system. Maximal bactericidal activity is obtained with magnesium concentrations similar to that of normal human serum (10–3 to 10–4 M). The bactericidal activity of the properdin system occurs only at temperatures above 15°. Resistant strains have been encountered in species of bacteria sensitive to the properdin system. Resistance or sensitivity is a characteristic of the individual strain and not of the species. The widespread occurrence of the properdin system in normal mammalian serum and the variety of bacteria destroyed by it suggest that the properdin system is a factor in natural resistance.

scholarly journals Evaluation of Bactericidal Action of Serum Collected from Paratyphoid Patients and Normal Human against Salmonella Paratyphi

2013 ◽  
Vol 12 (1) ◽  
pp. 71-75
Author(s):  
Md. Chhanaur Rabbee ◽  
Mohammad Shahriar ◽  
Mohiuddin Ahmed Bhuyian ◽  
Rishikesh Islam ◽  
Md. Asraful Islam
Keyword(s):  
Human Serum ◽  
Bactericidal Activity ◽  
Incubation Time ◽  
Normal Human Serum ◽  
Bacterial Suspension ◽  
Bactericidal Action ◽  
Alternative Pathways ◽  
Normal Human ◽  
The Mean ◽  
Paratyphoid Fever

A comparative study of susceptibility of clinical isolates of Salmonella Paratyphi to bactericidal action of S. Paratyphi infected human serum and uninfected human serum was investigated. Bactericidal action of S. Paratyphi infected human serum and uninfected human serum was assessed after incubating the bacterial suspension of S. Paratyphi with 40% of both infected and unifected human serum at various incubation times. Eight samples of S. Paratyphi infected serum from the patients diagnosed with paratyphoid fever were used. The investigation found that the serum killed S. Paratyphi both by classical and alternative pathways. Anti- S. Paratyphi antibodies for the bactericidal action of serum were examined by the assessment of bactericidal activity of non-immune normal human serum. Significant killing of S. Paratyphi by S. Paratyphi infected serum was investigated and the serum mediated killing was increased by increasing the incubation time. The mean growth declines gradually as the incubation time was increased. No noteworthy serum mediated killing was observed for normal human serum and inactivated (heat induced) S. Paratyphi infected serum. Dhaka Univ. J. Pharm. Sci. 12(1): 71-75, 2013 (June) DOI: http://dx.doi.org/10.3329/dujps.v12i1.16303

scholarly journals Phosphoethanolamine Substitution of Lipid A and Resistance of Neisseria gonorrhoeae to Cationic Antimicrobial Peptides and Complement-Mediated Killing by Normal Human Serum

2008 ◽  
Vol 77 (3) ◽  
pp. 1112-1120 ◽  
Author(s):  
Lisa A. Lewis ◽  
Biswa Choudhury ◽  
Jacqueline T. Balthazar ◽  
Larry E. Martin ◽  
Sanjay Ram ◽  
...  
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Human Serum ◽  
Lipid A ◽  
Polymyxin B ◽  
Normal Human Serum ◽  
Bactericidal Action ◽  
Complement Pathway ◽  
Classical Complement Pathway ◽  
Normal Human ◽  
Classical Complement

ABSTRACT The capacity of Neisseria gonorrhoeae to cause disseminated gonococcal infection requires that such strains resist the bactericidal action of normal human serum. The bactericidal action of normal human serum against N. gonorrhoeae is mediated by the classical complement pathway through an antibody-dependent mechanism. The mechanism(s) by which certain strains of gonococci resist normal human serum is not fully understood, but alterations in lipooligosaccharide structure can affect such resistance. During an investigation of the biological significance of phosphoethanolamine extensions from lipooligosaccharide, we found that phosphoethanolamine substitutions from the heptose II group of the lipooligosaccharide β-chain did not impact levels of gonococcal (strain FA19) resistance to normal human serum or polymyxin B. However, loss of phosphoethanolamine substitution from the lipid A component of lipooligosaccharide, due to insertional inactivation of lptA, resulted in increased gonococcal susceptibility to polymyxin B, as reported previously for Neisseria meningitidis. In contrast to previous reports with N. meningitidis, loss of phosphoethanolamine attached to lipid A rendered strain FA19 susceptible to complement killing. Serum killing of the lptA mutant occurred through the classical complement pathway. Both serum and polymyxin B resistance as well as phosphoethanolamine decoration of lipid A were restored in the lptA-null mutant by complementation with wild-type lptA. Our results support a role for lipid A phosphoethanolamine substitutions in resistance of this strict human pathogen to innate host defenses.

Evaluation of a commercially available radioimmunoassay kit for measurement of doxorubicin in plasma.

1982 ◽  
Vol 28 (1) ◽  
pp. 119-121 ◽  
Author(s):  
E Piall ◽  
G W Aherne ◽  
V Marks
Keyword(s):  
Human Serum ◽  
Normal Human Serum ◽  
Nonspecific Effects ◽  
Normal Human ◽  
Doxorubicin Concentration

Abstract We evaluated a commercially available (Diagnostic Biochemistry Inc.) doxorubicin 125I radioimmunoassay kit. This kit gave a high apparent doxorubicin concentration (greater than 12 micrograms/L), which was not linearly related to dilution, for two pools of normal human serum and plasma and also for samples collected from patients before they received the drug. In contrast, a doxorubicin 3H radioimmunoassay developed by us gave a low blank (2 micrograms/L), which was linearly related to dilution, for the same pools and patients' samples. Doxorubicin concentrations in the plasma of patients receiving the drug were compared by the two methods; the kit gave results five- to 10-fold those obtained with our assay. High nonspecific interference by serum and plasma as measured by the 125I radioimmunoassay must therefore be borne in mind by users of the kit, and we suggest that results should be corrected for these nonspecific effects.

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