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At least 109 records · Page 6Linked to original sources
PubMed1999

Cloning of gp-340, a putative opsonin receptor for lung surfactant protein D.

Surfactant protein D (SP-D) is an oligomeric C type lectin that promotes phagocytosis by binding to microbial surface carbohydrates. A 340-kDa glycoprotein (gp-340) has been shown to bind SP-D in the presence of calcium but does so independently of carbohydrate recognition. This protein exists both in a soluble form and in association with the membranes of alveolar macrophages. The primary structure of gp-340 has been established by molecular cloning, which yielded a 7,686-bp cDNA sequence encoding a polypeptide chain of 2, 413 amino acids. The domain organization features 13 scavenger receptor cysteine-rich (SRCR) domains, each separated by an SRCR-interspersed domain, except for SRCRs 4 and 5, which are contiguous. The 13 SRCR domains are followed by two C1r/C1s Uegf Bmp1 domains separated by a 14th SRCR domain and a zona pellucida domain. gp-340 seems to be an alternative spliced form of DMBT1. Reverse transcription-PCR analysis showed that the main sites of synthesis of gp-340 are lung, trachea, salivary gland, small intestine, and stomach. Immunohistochemistry revealed strong staining for gp-340 in alveolar and other tissue macrophages. Immunostaining of the macrophage membrane was either uniform or focal in a way that suggested capping, whereas other macrophages showed strong intracellular staining within the phagosome/phagolysosome compartments. In some macrophages, SP-D and gp-340 were located in the same cellular compartment. Immunoreactive gp-340 was also found in epithelial cells of the small intestine and in the ducts of salivary glands. The distribution of gp-340 in macrophages is compatible with a role as an opsonin receptor for SP-D.

Amino Acid Sequence↗
PubMed1960

Changes in the titre of serum opsonins and phagocytic properties of mouse peritoneal macrophages following injection of endotoxin.

A study has been made of the changes in the opsonic properties of mouse serum and bactericidal activity of mouse peritoneal macrophages at different times following the injection of various doses of lipopolysaccharide. It has been found that changes in the percentage of bacteria phagocytosed and killed within the mouse peritoneal cavity in a given time could be correlated with changes in the opsonic titre of the serum. Macrophages harvested from the peritoneal cavities of mice injected with endotoxin appear to be more efficient in phagocytosing bacteria in the presence of serum opsonins than macrophages obtained from normal mice. The relative importance of these changes in determining an animal's resistance to infection is discussed.

Animals↗
PubMed1967

The interaction in vitro between group B meningococci and rabbit polymorphonuclear leukocytes. Demonstration of type specific opsonins and bactericidins.

The interaction in vitro between group B meningococci and rabbit polymorphonuclear leukocytes has been described. Phagocytosis did not occur in the presence of normal rabbit serum. Antiserum collected 12-21 days following one subcutaneous inoculation of living log phase meningococci exhibited opsonic activity with type specificity; this opsonic action depended on both heat-labile and heat-stable factors. Following ingestion by granulocytes, meningococci were rapidly killed. These studies suggest that group B meningococcal strains contain specific antiphagocytic surface factors of an as yet unknown chemical nature. Antisera obtained 4 or more wk after immunization showed bactericidal activity with the same type specificity as opsonic activity. This bactericidal activity was also lost after heating and restored by the addition of normal serum. Further studies on opsonins and bactericidins for meningococci may shed light on virulence factors in these microorganisms, and may prove useful for a more precise classification of meningococci according to type rather than group specificity.

Animals↗
PubMed1969

Heat labile opsonins to pneumococcus. II. Involvement of C3 and C5.

When encapsulated type 25 pneumococci (Pn25) were opsonized with normal guinea pig serum, they consumed much more C3 than other complement (C) components. Fixation of C3 to the organisms was demonstrated by radio-labeling techniques, and its capsular localization was established by the use of monospecific anti-C3 antibody. Treatment of the serum with an appropriate dose of a purified cobra venom factor (VF) destroyed C3 and all of the opsonic activity, without appreciably affecting the other C components. Addition of purified C3 completely restored the opsonic activity of the VF-treated serum, indicating a requirement for C3. Since purified C3 alone had no opsonic activity, it was concluded that the C3 molecules had to be cleaved (to C3b) to function as opsonins. Experiments with C5-deficient mice revealed that C5 also plays a definite, but quantitatively less impressive, role in antipneumococcal defense.

Animals↗
PubMed1987

Opsonin-independent ligation of Fc gamma receptors. The 3G8-bearing receptors on neutrophils mediate the phagocytosis of concanavalin A-treated erythrocytes and nonopsonized Escherichia coli.

We report that phagocytosis by human neutrophils of Con A-treated erythrocytes (E-Con A) and nonopsonized Escherichia coli with mannose-binding adhesions is mediated by the Fc gamma receptor bearing the 3G8 epitope. Modulation of Fc receptors by pretreating with aggregated-IgG or with 3G8 anti-Fc gamma receptor mAb markedly inhibited internalization of E-Con A and E. coli without altering their cell surface attachment. Phagocytosis of these probes was specifically blocked by alpha-methylmannoside and D-mannose and not by other monosaccharides. Thus, recognition of E-Con A and E. coli by the Fc receptor is dependent upon the mannose-specific interaction with lectin or lectin-like adhesions. These data demonstrate that ligands other than the classical IgG opsonins can bind to classical immune receptors for IgG through lectin-carbohydrate interactions.

Concanavalin A↗
PubMed1980

Luminol-enhanced chemiluminescence for evaluation of type III group B streptococcal opsonins in human sera.

A luminol-enhanced chemiluminescence (CL) assay was developed to evaluate type III group B streptococcal opsonins. Sera from 11 adults that contained high (greater than 25 microgram/ml), intermediate (3-24 microgram/ml), or low (less than 2 microgram/ml) antibody concentrations were assessed by CL, indirect immunofluorescence (IF), and bactericidal assays. Total CL activity correlated with antibody concentration (P less than 0.005), IgG- and C3-IF values, and phagocytic and bactericidal indices. Heat-stable CL activity correlated with antibody concentration (P less than 0.0001) and was related to IgG-IF values and phagocytic indices. Significant bactericidal activity was demonstrated in all sera containing greater than 2 microgram of antibody/ml, but no bactericidal activity was observed in heat-inactivated sera. Adsorption of heated sera with type III group B Streptococcus abolished CL activity, whereas CL values of MgEGTA-chelated sera were approximately 80% of untreated sera. Thus, type-specific antibody in addition to heat-labile serum factors, including those of the alternative complement pathway, contribute to opsonization of type III group B Streptococcus.

Antigen-Antibody Reactions↗
PubMed1993

Cross-reacting serum opsonins to meningococci after vaccination.

The opsonic activity of sera from healthy volunteers immunized with an outer membrane vesicle vaccine prepared from a Neisseria meningitidis (class 3, 44/76, B:15:P1.7,16), characteristic of the present Norwegian epidemic, has been examined. A marked increase in the phagocytosis of class 3 and nontypeable strains of different serogroups, serotypes, and serosubtypes was demonstrated in the presence of postvaccination sera. Sera from vaccinees also caused a significant increase in leukocyte oxidative metabolism as measured by luminol-enhanced chemoluminescence during phagocytosis of class 3 and nontypeable meningococci. An increase in serum opsonins cross-reacting with class 2 (type 2a) meningococci of different serogroups was not observed, suggesting that future meningococcal outer membrane vesicle vaccine preparations should contain both class 2 and class 3 porins in geographic areas where both class 2 and class 3 strains cause disease.

Antibodies, Bacterial↗
PubMed2004

Granularin, a novel molluscan opsonin comprising a single vWF type C domain is up-regulated during parasitation.

Snails are intermediate hosts to schistosome parasites, some of which are the main cause of human schistosomiasis (bilharzia), and have been used as models for parasite-host interactions for a long time. Here, we have characterized a novel internal defense peptide of the snail Lymnaea stagnalis, of which the relative abundance in brain tissue increases upon infection with the avian schistosome Trichobilharzia ocellata. This protein, named granularin, is secreted by granular cells, which are numerous in the connective tissue surrounding the brain. The protein is unique because it comprises only a single Von Willebrand factor type C domain that is normally found in large transmembrane and secreted extracellular matrix proteins. The granularin gene is twice up-regulated during parasitation. Purified granularin stimulates phagocytosis of foreign particles by blood hemocytes. Together, our data indicate that granularin represents a novel protein that acts as an opsonin in the molluscan internal defense response.

Amino Acid Sequence↗
PubMed1996

Opsonin-independent adherence and phagocytosis of Listeria monocytogenes by murine peritoneal macrophages.

Listeria monocytogenes adhered to and multiplied intracellularly in murine peritoneal macrophages in the absence of opsonins. The infective process in these cells was evaluated by viable bacterial cell colony counts of intracellular organisms and documented by transmission and scanning electron microscopy. Adherence of listeriae to macrophages involved surface interactions of the prokaryotic cell surface and eukaryotic cell membranes. Subsequent phagocytosis was seen to occur through a process in which host cell-derived pseudopodia surrounded and engulfed organisms leaving them within phagosomes in the cytoplasm of infected cells. This process of uptake of L. monocytogenes by macrophages occurred at 4 degrees C. Following invasion of the cell, escape of L. monocytogenes from the phagosome into the cytoplasm was initiated as early as 10 min into the infective process. Intracellular multiplication of bacteria continued for 8 h after inoculation at which point loss of adherent macrophages due to cell lysis was evident. The mean generation time of the organism in these cells was 58 min. The cellular and ultrastructural events of L. monocytogenes adherence to and phagocytosis by murine macrophages in the absence of antibody or complement have been defined.

Animals↗
PubMed1999

Enterococcus faecalis aggregation substance promotes opsonin-independent binding to human neutrophils via a complement receptor type 3-mediated mechanism.

Enterococcus faecalis aggregation substance (AS) mediates efficient adhesion between bacteria, thereby facilitating plasmid exchange as an integral part of a bacterial sex pheromone system. We examined the interaction of AS-bearing E. faecalis with human neutrophils (PMNs), an important component of the host defense system. AS promoted a markedly increased opsonin-independent bacterial binding to PMNs. Adhesion was dependent on the expression of the enterococcal Asc10 protein, which contains two Arg-Gly-Asp (RGD) sequences, and addition of exogenous RGD-containing peptides inhibited AS-mediated binding by 66%. AS-mediated adhesion was inhibited by 85% by anti-human complement receptor type 3 (CR3) monoclonal antibodies or by use of PMNs from a patient with leukocyte adhesion deficiency. However, AS-bearing E. faecalis cells were unable to bind to CHO-Mac-1 cells, expressing functionally active CR3, suggesting the potential need for additional PMN surface receptors for bacterial adhesion. Monoclonal antibodies against integrin-associated protein (CD47) and L-selectin, both of which may interact with CR3 and bind to ligands on E. faecalis, also inhibited AS-dependent binding. The non-opsonic binding of E. faecalis to PMNs may play an important role in this organism's pathogenesis.

Adhesins, Bacterial↗
PubMed1987

Serum opsonins to group B meningococci.

The production of serum opsonins and other antibodies to serogroup B serotype 15 meningococci was examined in 7 patients with serogroup B serotype 15 meningococcal disease and 7 volunteers immunized with a vaccine containing outer membrane proteins from serogroup B serotype 2b and 15 meningococcal strains complexed with polysaccharides from serogroups A, C, Y and W-135 meningococci. Serum opsonic activity was measured by a flow cytometric phagocytosis technique, using unfixed serogroup B Neisseria meningitidis labelled with fluorescein isothiocyanate. Serum antibodies to outer membrane complexes prepared from the meningococcal test strain, B:15:P1.16, were measured by an enzyme linked immunosorbent assay. The mean number of bacteria per phagocyte increased from 9.7 to 17.3 (mean difference 7.6, p less than 0.001) when the meningococci were opsonized with convalescent sera compared to sera obtained during the acute illness, and from 8.0 to 15.4 (mean difference 7.4, p less than 0.001) when opsonized with sera from immunized versus pre-immunized volunteers. The patients had insignificant amounts of serum antibodies to the group B meningococcal test strain on admission to hospital. Two weeks later all had a marked increase in IgG, IgM and IgA serum antibodies. Vaccination caused a marked increase in serum IgG antibodies. Serum opsonic activity and IgG levels were still high 6 weeks after the acute illness/immunization. A correlation was observed between serum opsonic activity and IgG antibody levels (r = 0.883, p less than 0.001).(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗
PubMed1974

Opsonin system of the group B streptococcus.

The opsonization by polymorphonuclear leukocytes of group B streptococcal serotypes associated with neonatal sepsis and delayed meningitis was studied. A specific BIa opsonizing antibody (not related to the antipolysaccharide typing antibody) was present in only 10% of the population tested. Serotype BIa was not opsonized in the absence of this specific antibody. BIa antibody specificity was demonstrated by macroagglutination and absorption with BIa streptococci and extracts, but not by gel diffusion. The binding of complement by the BIa opsonin increased the mean phagocytic activity by 60%; complement was manifested via the classic and/or alternate C3-related pathway, but seldom by both concurrently. Serotypes BIb, BIc, BII, and BIII were naturally and nonspecifically opsonized in 95% of the human and baboon sera or plasma tested. Although similar levels of opsonization were present in hyperimmune rabbit sera, heat inactivation and homologous bacterial absorption did not reduce the level of phagocytic activity in the rabbit, human, or primate groups studied. These immunological studies confirmed previous findings that serotype BIa presents a serious hazard for neonatal sepsis, with a nearly 100% mortality. Exclusive isolation of BIII in delayed meningitis suggests that ingestion and subsequent killing by polymorphonuclear leukocytes of type III may differ from the other serotypes.

Absorption↗
PubMed1979

Immunological specificity of natural opsonins and their role in the cross-reactivity between Staphylococcus aureus Mardi and Escherichia coli 101.

The immunochemical specificity of the observed cross-reactivity between Escherichia coli strain 101 and Staphylococcus aureus strain Mardi was examined. The cross-reactivity was shown to be dependent upon mucopeptide antibodies which are present in normal and immune sera. Although both organisms contained surface antigens with immunodominant glucuronic acid residues, in vitro phagocytosis studies indicated that antibodies directed against these antigens were not significantly involved in the opsonization process. Rather, antibodies with mucopeptide specificity were shown to be involved in the in vitro phagocytosis of these organisms by polymorphonuclear leukocytes. The mucopeptide antibodies, which were found in both nonimmune and immune sera, were shown to be effective in opsonizing both the S. aureus strain and the E. coli strain. The ubiquitous distribution of E. coli strains containing mucopeptide antigens common to most bacteria suggests that these organisms may be responsible for the wide prevalence of natural staphylococcal opsonins with mucopeptide specificity in normal sera.

Antibodies, Bacterial↗
PubMed1981

Pulmonary opsonins in Klebsiella pneumoniae pneumonia in rats.

Klebsiella pneumoniae was inoculated intrabronchially into rats, and bronchoalveolar lavage fluid and sera were obtained during the ensuring pneumonia. Klebsiellae recovered by lavage were not maximally coated with C3, as judged by studies with fluorescent antibody, whereas the organisms could be coated fully with C3 by a brief incubation in rat serum. The levels of C1 and C3 in lavage fluid obtained during infection were only a small fraction of the levels in the serum, and klebsiellae were not opsonized during incubation with concentrated lavage fluid. Systemic decomplementation did not affect the severity of K. pneumoniae pneumonia, as judged by the measurement of lung weight or by the numbers of klebsiellae in the lungs, but decomplemented rats had a larger number of klebsiellae in the blood at 24 h of infection than did controls. There were fewer klebsiellae in the lungs 4 h after inoculation of preopsonized organisms than after inoculation of organisms which were incubated in control (heat-inactivated) sera. These studies indicate that the concentration of complement and heat-labile opsonins within the alveoli is lower than that in the systemic circulation and is not adequate for effective opsonization of klebsiellae.

Animals↗
PubMed1982

Evaluation of Streptococcus pneumoniae type XIV opsonins by phagocytosis-associated chemiluminescence and a bactericidal assay.

The relative roles of serum factors required for opsonization of type XIV Streptococcus pneumoniae were investigated by means of luminol-enhanced chemiluminescence (CL), bactericidal, and immunofluorescence assays employing adult sera containing high (>1,000 ng of antibody nitrogen per ml) or low (<200 ng of antibody nitrogen per ml) antibody concentrations as determined by radioimmunoassay. Specific antibody concentration correlated directly with both total and heat-labile CL activity (P < 0.005) and with the bactericidal index (P < 0.05) at a serum concentration of 10%. The importance of specific antibody as an opsonin was confirmed by the abolition of CL activity and immunoglobulin immunofluorescence observed after absorption of heated sera with type XIV pneumococcal cells and by the dose response in CL and bactericidal activity observed with the addition of immunoglobulin G to hypogammaglobulinemic serum. A role for the classical complement pathway in opsonization was indicated by significantly greater CL integrals for high-antibody sera than for low-antibody sera depleted of factor D and by the bactericidal activity noted for untreated, but not magnesium ethylene glycol-bis(beta-aminoethyl ether)-N,N-tetraacetic acid-chelated low-antibody sera. The alternative pathway contributed more than half of the CL activity of both high- and low-antibody sera. However, after magnesium ethylene glycol-bis(beta-aminoethyl ether)-N,N-tetraacetic acid chelation, only sera with high antibody concentrations or agammaglobulinemic serum reconstituted with immunoglobulin G with high specific antibody levels supported significant bactericidal activity. Therefore, type-specific antibody and complement promote opsonization of type XIV S. pneumoniae, and this may occur via either complement pathway. These results suggest that CL is a suitable tool to delineate serum factors and their contribution to opsonization, but results must be related to other functional assays.

Antibodies, Bacterial↗
PubMed1971

Serum factors and the reticuloendothelial uptake of Staphylococcus aureus. II. Role of a zymosan-adsorbable serum opsonin.

A heat-stable factor in the serum of normal rabbits adsorbed by zymosan at 16 C in the presence of ethylenediaminetetraacetic acid has been found to enhance the uptake of an encapsulated strain of Staphylococcus aureus (Smith diffuse) by the isolated perfused rabbit liver. This opsonin does not appear to be a rate-limiting component of the hemolytic complement system, properdin, immunoglobulins G or M. It does, however, require the presence of a heat-labile cofactor(s) for expression of its activity.

Adsorption↗
PubMed1985

Vibrio vulnificus resists phagocytosis in the absence of serum opsonins.

Invasive disease caused by Vibrio vulnificus may result partially from resistance to phagocytic host defense mechanisms. The present studies show that V. vulnificus resists phagocytosis by murine peritoneal macrophages in the absence of serum opsonins and extracellular bacterial products, apparently through the anti-phagocytic properties of the bacterial surface.

Animals↗
PubMed1985

Correlation of serum opsonins with in vitro phagocytosis of Streptococcus pneumoniae.

C-reactive protein (CRP), an acute-phase reactant which binds to phosphocholine (PC) in the pneumococcal cell wall, and anti-PC antibodies are protective against experimental pneumococcal bacteremia in mice. To determine the relative opsonic capacities of CRP and anti-PC compared with those of antibodies against pneumococcal capsular polysaccharides (anti-PCP), we correlated in vitro opsonic activity for serotype 7F Streptococcus pneumoniae with concentrations of CRP, anti-PC, and anti-type 7F PCP in human sera from 10 normal subjects and 38 patients with sickle cell (SS) disease, a high-risk group for pneumococcal infection. Opsonic activity, measured by a radiolabeled bacterial uptake assay, correlated with anti-PCP levels but not with CRP or anti-PC in both the normal subjects and patients with SS disease. Addition of CRP to normal sera did not increase opsonic activity for serotypes 4 and 7F S. pneumoniae, although it did so for serotype 27, a nonpathogenic strain unique for having PC in its capsule. CRP and anti-PC were not effective opsonins when they bound to the pneumococcal cell wall rather than the capsule. The protective effects of CRP or anti-PC against these serotypes may be produced by means other than complement-dependent opsonization.

Adult↗