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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Murine monoclonal and rabbit, murine, and human polyclonal antibodies against chlamydial lipopolysaccharide (LPS) were characterized by the passive hemolysis and passive hemolysis inhibition assays and by absorption experiments with LPSs of Chlamydia psittaci, Chlamydia trachomatis, and a recombinant strain of Salmonella minnesota Re (r595-207) expressing the chlamydia-specific LPS epitope, as well as natural and synthetic partial structures of chlamydial LPS. Eleven monoclonal antibodies of the immunoglobulin M and G classes were characterized as chlamydia-specific by their failure to react with Re-type LPS, binding to a similar epitope for which the trisaccharide alpha-3-deoxy-D-manno-2-octulosonic acid (KDO)-(2-8)-alpha-KDO-(2-4)-alpha-KDO was an absolute prerequisite. For optimal binding, parts of the lipid A moiety were also involved; however, phosphoryl and ester-linked acyl groups and the reducing glucosamine residue of lipid A were dispensable. A similar antibody specificity was detected in lapine and murine hyperimmune sera after immunization with chlamydia, in addition to those recognizing more complex (e.g., those requiring the presence of phosphoryl residues) and less complex epitopes. Among the latter were those cross-reacting with Re-type LPS, which could be removed by absorption. The titers of different antibody specificities, in particular the ratio of chlamydia-specific to cross-reactive antibodies, present in murine polyclonal antisera depended on the immunization protocol. The preferential formation of chlamydia-specific antibodies was observed after immunization with liposome-incorporated immunogens. Human sera from patients with suspected genital chlamydial infections were also found to contain chlamydia-specific and cross-reactive antibodies, the latter of which could be removed by absorption with Re-type LPS.
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PMID:Characterization of murine monoclonal and murine, rabbit, and human polyclonal antibodies against chlamydial lipopolysaccharide. 229 50

The polymerase chain reaction was used to detect the presence of a plasmid essential for the growth of Chlamydia trachomatis. As few as 10 copies of the plasmid in the initial reaction mix were detectable using this technique. In contrast, chlamydial DNA was not detectable in the knee joints of nine patients with definite sexually acquired reactive arthritis (SARA) or nine patients with suspected SARA. Five patients with an undifferentiated seronegative lower limb oligoarthropathy, one with Crohn's disease and another with post-enteric reactive arthritis had evidence of intra-articular chlamydial antigens as judged by fluorescein-labelled monoclonal antibody staining of joint material but, again, no chlamydia plasmid DNA was detected. The nature of the immunofluorescent staining seen in some of these samples remains to be elucidated. It could be due to the presence of chlamydial outer membrane protein or lipopolysaccharide antigens in the joints, either free or in immune complexes, or it may be artefactual. Our results indicate that viable C. trachomatis is not present in the joints of the patients in this study even in the presence of chlamydial antigen detected by fluorescence antibody testing.
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PMID:Chlamydial DNA is absent from the joints of patients with sexually acquired reactive arthritis. 235 4

Female guinea pigs were immunized with viable or UV light-inactivated chlamydiae (agent of guinea pig inclusion conjunctivitis), belonging to the species Chlamydia psittaci, by intravenous, subcutaneous, oral, or ocular routes. All animals were then inoculated vaginally with viable chlamydiae to determine the extent of protection against challenge infection induced by the various regimens. The course of genital infection was significantly reduced in intensity in all groups of animals except the unimmunized controls and those animals immunized orally with inactivated antigen. Guinea pigs immunized with viable antigen were more likely to develop resistance to challenge infection and, in general, had a significantly greater degree of protection than animals immunized with inactivated antigen. No one route seemed superior in producing a protective response. Animals in all groups demonstrating protection developed serum and secretion immunoglobulin G antibody responses to chlamydiae. Lymphocyte proliferative reactions to chlamydial antigen were variable among groups. Immunoblot analysis of serum and secretions indicated a wide range of antibody specificities, but most protected animals produced antibodies to the major outer membrane protein, lipopolysaccharide, and the 61-kilodalton protein. No definitive associations could be made between the increased ability of immunization with viable organisms to produce resistance to challenge infection and a particular immune parameter. These data indicate that viable chlamydiae given by various routes are able to induce a strong immune response which can provide resistance against reinfection in some cases or at least reduce the degree of infection to a greater degree than inactivated antigen. However, complete resistance to genital tract infection may be difficult to obtain and alternate immunizations strategies may have to be developed.
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PMID:Immunization against chlamydial genital infection in guinea pigs with UV-inactivated and viable chlamydiae administered by different routes. 237 Jan 10

Rough mutants from Salmonella typhimurium and Salmonella minnesota were transformed with a plasmid containing a 6.5-kilobase insert of DNA from Chlamydia trachomatis assumed to encode a glycosyltransferase. Transformation resulted in the expression of a genus-specific chlamydial epitope on the lipopolysaccharide (LPS) of the recombinant strains. Proteinase K-digested whole-cell lysates of the recombinants and of controls were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by silver staining or Western blot analysis. Two LPS populations were detected in the recombinants, the parent LPS and a faster-migrating component. The latter stained with monoclonal antibody against the genus-specific chlamydial epitope and was not seen in the controls. LPS was extracted and purified from recombinants of S. minnesota R595 and R4 and characterized by the passive hemolysis and passive hemolysis inhibition assays and by hydrolysis kinetics. Different antigenic determinants could be distinguished from each other by the passive hemolysis inhibition test with monospecific antigen-antibody reactions. Rabbits were immunized with heat-killed recombinant bacteria to study the immunogenic properties of the recombinants. In all animals, antibodies were raised against the parent core specificity and against the chlamydia-specific epitope. The data show that the recombinant bacteria are useful as immunogens to prepare polyclonal antisera against chlamydiae and that LPS isolated from them exhibits the same antigenic determinants as chlamydial LPS and may thus be used as a substitute for chlamydial LPS in serological assays.
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PMID:Antigenic and immunogenic properties of recombinants from Salmonella typhimurium and Salmonella minnesota rough mutants expressing in their lipopolysaccharide a genus-specific chlamydial epitope. 243 22

Members of the bacterial genus Chlamydia are responsible for widespread disease among humans and animals, including endemic trachoma in developing countries, venereal disease in developed countries, and a variety of other diseases such as infantile pneumonia and lymphogranuloma venereum. Although there is little genetic relatedness between and large antigenic diversity between and among the two chlamydial species, one antigenic determinant has been preserved among all serovars: the genus-specific lipopolysaccharide epitope. In this report, the tools of molecular genetics, monoclonal antibodies, and analytical and synthetic chemistry have been combined to determine the structure of this epitope. This epitope is attributed to the presence of a trisaccharide of 3-deoxy-D-manno-octulosonic acid (KDO) of the sequence KDOp-(2----8)-KDOp-(2----4)-KDO. The structure includes a unique linkage of two KDO residues through a 2.8-linkage.
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PMID:Chemical and serological investigations on the genus-specific lipopolysaccharide epitope of Chlamydia. 243 32

Purified elementary bodies (EBs) of Chlamydia trachomatis serovar L2 were analyzed by chemical cross-linking with disuccinimidyl selenodipropionate. The effect of the cross-linking was analyzed by immunoblotting sodium dodecyl sulfate-polyacrylamide gel electrophoresis-separated components which were reacted with monoclonal antibodies against major outer membrane protein (MOMP) and lipopolysaccharide (LPS). It was shown that in EBs, MOMP was cross-linked to the LPS component of the outer membrane. Migration analysis of the cross-linked components showed that with extensive cross-linking, most of the MOMP became cross-linked to LPS, changing the migration rate from 40 to 42.5 kilodaltons. A small fraction of MOMP associated with LPS was shown to be present in bands with migration rates of 100 and 110 kilodaltons. No association of MOMP or LPS to other proteins, or to dimer or multimer forms of MOMP without LPS, was observed. A totally different membrane structure must be present in reticulate bodies, since there, MOMP was so heavily cross-linked that it did not enter the polyacrylamide gel and thus became impossible to analyze. Furthermore, the monoclonal antibody, which reacted with LPS associated with MOMP in the cross-linked EBs, did not react with reticulate bodies.
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PMID:Chemical cross-linking of Chlamydia trachomatis. 244 99

We used monoclonal antibodies (MAbs) to examine the antigenic specificity and biologic function of several Chlamydia trachomatis antigens. Thirteen distinct MAbs to eight C. trachomatis antigens were produced. Six MAbs reacted with unique epitopes on the major outer membrane protein (MOMP) and two of these had neutralizing activity. MAbs were produced to each of the chlamydial antigens with molecular masses of 10, 29, 32, 57, 60, 70, and 75 kilodaltons (kDa). These MAbs showed species and genus specificity in an immunoblot assay. None of the MAbs had neutralizing activity. The epitopes recognized on MOMP, 29-, and 10-kDa (presumably lipopolysaccharide) antigens were surface exposed. MAbs to the 75-kDa, 57-kDa, and MOMP antigens were used for immunoaffinity purification of these antigens to produce monospecific antisera in mice. With polyclonal sera, we found that the 75-kDa antigen was also immunoaccessible and that antibody to MOMP and 75-kDa antigens neutralized C. trachomatis infectivity. We conclude that, in addition to MOMP and lipopolysaccharide, antigens with molecular masses of 75 and 29 kDa are surface exposed. Antibodies to MOMP and 75-kDa antigens can neutralize the organism in vitro.
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PMID:Characterization of Chlamydia trachomatis antigens with monoclonal and polyclonal antibodies. 245 51

Using purified elementary bodies of 14 Chlamydia trachomatis serovars in an in vitro assay, we compared the staining characteristics of six commercially available monoclonal antibody reagents used for direct immunofluorescent staining of patient smears. Considerable variation in the degree of brightness, consistency of staining, and specificity of the six reagents was found. Monoclonal antibodies against the major outer membrane proteins of C. trachomatis produced brighter fluorescence, more consistent elementary body morphology, and less nonspecific staining than did monoclonal antibodies directed against chlamydial lipopolysaccharide.
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PMID:Staining characteristics of six commercially available monoclonal immunofluorescence reagents for direct diagnosis of Chlamydia trachomatis infections. 246 Apr 95

A serosurvey revealed intense cross-reactivity between Bartonella bacilliformis and Chlamydia psittaci. One of the cross-reacting Bartonella antigens was identified as lipopolysaccharide which reacted with Bartonella as well as with Chlamydia serum antibodies. A monoclonal Bartonella antibody bound to Bartonella lipopolysaccharide as well as to the surfaces of Bartonella bacilliformis and Chlamydia psittaci. It was thus demonstrated that Chlamydia psittaci carries a surface epitope identical to an epitope of Bartonella lipopolysaccharide. The lipopolysaccharide was preliminarily characterized by polyacrylamide gel electrophoresis and by a lectin-binding assay. The lipopolysaccharides of Bartonella bacilliformis and Chlamydia psittaci are not identical.
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PMID:Common surface epitope of Bartonella bacilliformis and Chlamydia psittaci. 246 60

The presence of a chlamydia-specified antigen associated with the plasma membrane of infected cell lines was demonstrated by indirect immunofluorescence staining with a monoclonal antibody, designated 47A2, specific for the chlamydial genus-specific lipopolysaccharide (LPS) antigen. Staining of HeLa, L-929, and McCoy cells infected with the L2 or F serovar of Chlamydia trachomatis was observed either without fixation or following aldehyde fixation and brief drying. The 47A2-reactive antigen appeared to be present on the plasma membrane, on bleb-like structures on the host cell surface, and on proximal processes of neighboring uninfected cells. Antibodies to chlamydial protein antigens such as the major outer membrane protein produced no surface staining under similar conditions. Membrane vesicles elaborated from infected cells were enriched for the 47A2-reactive antigen. Superinfection of chlamydia-infected cells with vesicular stomatitis virus, an enveloped virus which buds from the plasma membrane, allowed purification of progeny virions that were enriched with chlamydial LPS. These results are consistent with the presence of chlamydial LPS in the plasma membranes of infected host cells.
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PMID:Accumulation of chlamydial lipopolysaccharide antigen in the plasma membranes of infected cells. 247 Jun 79


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