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Humoral immunity and regulation of intrapulmonary growth of Legionella pneumophila in the immunocompetent host.
Brieland JK, Heath LA, Huffnagle GB, Remick DG, McClain MS, Hurley MC, Kunkel RK, Fantone JC, Engleberg C
(1996) J Immunol 157: 5002-8
MeSH Terms: Animals, Antibodies, Bacterial, Complement System Proteins, Female, Immunocompetence, Legionella pneumophila, Legionnaires' Disease, Lung, Macrophages, Alveolar, Mice, Mice, Inbred A, Opsonin Proteins, Phagocytosis, Time Factors
Show Abstract · Added May 20, 2014
The potential role of humoral immunity in regulating intrapulmonary growth of Legionella pneumophila in the immunocompetent host was investigated using a murine model of Legionnaires' disease. Intratracheal inoculation of A/J mice with a virulent strain of L. pneumophila (10(6) bacteria per mouse) resulted in the recruitment of B lymphocytes into the lung and the development of anti-L. pneumophila Ab. Opsonization of L. pneumophila in vitro with anti-L. pneumophila-specific mAb resulted in a significant decrease in intrapulmonary growth of the bacteria at 24 to 72 h postinfection. Transmission electron microscopic analysis of lung tissue from L. pneumophila- infected mice demonstrated that while there was no significant difference between phagocytosis of the unopsonized and opsonized L. pneumophila by alveolar macrophages at 24 h postinfection, phagocytosis of opsonized bacteria by alveolar mononuclear phagocytic cells was significantly enhanced at 48 h postinfection. Depletion of A/J mice of complement before intratracheal inoculation of opsonized L. pneumophila (10(6) bacteria per mouse) did not significantly alter intrapulmonary growth of L. pneumophila. These results suggest that anti-L. pneumophila Ab, produced during replicative L. pneumophila lung infections, may regulate intrapulmonary growth of L. pneumophila in the immunocompetent host by decreasing the viability of extracellular L. pneumophila and by enhancing phagocytosis of the bacteria by alveolar mononuclear phagocytic cells by a complement-independent mechanism.
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14 MeSH Terms
Persistence of Campylobacter fetus bacteremia associated with absence of opsonizing antibodies.
Neuzil KM, Wang E, Haas DW, Blaser MJ
(1994) J Clin Microbiol 32: 1718-20
MeSH Terms: Agammaglobulinemia, Antibodies, Bacterial, Bacteremia, Blood Bactericidal Activity, Campylobacter fetus, Humans, Immunization, Passive, Male, Middle Aged, Opsonin Proteins, Recurrence, Treatment Failure
Show Abstract · Added March 13, 2015
Campylobacter fetus causes systemic infections in immunocompromised hosts. We describe a case in which C. fetus bacteremia apparently relapsed after 7 years in a patient with hypogammaglobulinemia and characterize the serum resistance of the patient's C. fetus strain and the inability of the patient's serum, with and without commercial intravenous immunoglobulin, to opsonize this and another C. fetus strain effectively. The probable presence of a sequestered site of infection in bone, the intrinsic serum resistance of the C. fetus strain, and the absence of specific antibody may account for the persistent infection in this patient. These studies suggest that intravenous immunoglobulin treatment is not useful in eradicating C. fetus bacteremia.
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12 MeSH Terms
Different preparations of zymosan induce glycogenolysis independently in the perfused rat liver. Involvement of mannose receptors, peptide-leukotrienes and prostaglandins.
Kimura K, Shiota M, Mochizuki K, Ohta M, Sugano T
(1992) Biochem J 283 ( Pt 3): 773-9
MeSH Terms: Animals, Chromones, Glycogen, Hot Temperature, Ibuprofen, Isoproterenol, Liver, Male, Mannans, Masoprocol, Opsonin Proteins, Platelet Activating Factor, Prostaglandins, Rats, Rats, Inbred Strains, Receptors, Immunologic, Receptors, Leukotriene, Solubility, Zymosan
Show Abstract · Added December 10, 2013
Zymosan (non-boiled) induced glycogenolysis biphasically, with no lag time, in the perfused rat liver. After the zymosan was boiled, it could be separated into two fractions, both of which stimulated glycogenolysis independently. The soluble fraction of boiled zymosan (zymosan sup) showed homologous desensitization, indicating that zymosan sup-induced glycogenolysis is a receptor-mediated event. Mannan (polymannose), which is known to be a biologically active component of zymosan, induced a glycogenolytic response similar to that produced by zymosan sup, and desensitized the response to the latter. Preinfusion of platelet-activating factor (PAF, 20 nM) or isoprenaline (10 microM) did not extinguish the glycogenolytic response to zymosan sup, while the response to a secondary infusion of PAF was blocked. The glycogenolytic response to zymosan sup was completely inhibited by nordihydroguaiaretic acid (NDGA, 10 microM), a lipoxygenase inhibitor, and by ONO-1078 (100 ng/ml), a leukotriene (LT) D4 receptor antagonist. On the other hand, the glycogenolytic effect of zymosan pellet (the particulate fraction of boiled zymosan) was not affected by preinfusion of zymosan sup, and was inhibited by ibuprofen (20 microM), a cyclo-oxygenase inhibitor. Prostaglandins (PGs) detected in the perfusate were augmented with infusion of zymosan pellet. Opsonization of the zymosan pellet by serum (complement) enhanced the glycogenolytic response without a lag period, and with a concomitant enhancement of PG output. Correlations between glucose production and PGs were r = 0.832 (PGD2), r = 0.872 (PGF2 alpha), r = 0.752 (PGE2) and r = 0.349 (6-oxo-PGF1 alpha). The glycogenolytic response to non-boiled zymosan was delayed and the biphasic glycogenolytic response was not observed when mannan was infused first. NDGA mimicked the effects of the preinfusion of mannan, while ibuprofen had no effect on the non-boiled-zymosan-induced glycogenolysis. These results suggest: (1) that non-boiled zymosan stimulates glycogenolysis through a mannose receptor-dependent, but unidentified, pathway, (2) that zymosan sup induces glycogenolysis via mannose receptor activation through the production of peptide-LTs but not PAF, and (3) that zymosan pellet causes glycogenolysis through the production of prostanoids, which is enhanced in the presence of complement.
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19 MeSH Terms