Serological typing of Branhamella catarrhalis strains on the basis of lipopolysaccharide antigens

Vaneechoutte, Mario; Verschraegen, Gerda; Claeys, Geert; Abeele, A M Van den

doi:10.1128/jcm.28.2.182-187.1990

Cited by 82 publications

(37 citation statements)

References 25 publications

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“…The outer-membrane glycolipids of M. catarrhalis lack the repeating O-antigen polysaccharides of LPS and are hence designated lipo-oligosaccharides (LOS) [38]. These occur commonly in nonenteric Gram-negative bacteria, such as those that colonize the mucosal surfaces of the upper respiratory tract [39].…”

Section: Discussionmentioning

confidence: 99%

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

Nordström

Jendholm

Samuelsson

et al. 2005

Journal of Leukocyte Biology

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Moraxella catarrhalis immunoglobulin D (IgD)‐binding protein (MID) is an outer membrane protein with specific affinity for soluble and cell‐bound human IgD. Here, we demonstrate that mutated M. catarrhalis strains devoid of MID show a 75% decreased activation of human B cells as compared with wild‐type bacteria. In contrast to MID‐expressing Moraxella, the MID‐deficient Moraxella mutants did not bind to human CD19+ IgD+ B cells. The smallest MID fragment with preserved IgD‐binding capacity comprises 238 amino acids (MID962‐1200). To prove the specificity of MID962‐1200 for IgD, a Chinese hamster ovary (CHO) cell line expressing membrane‐anchored human IgD was manufactured. MID962‐1200 bound strongly to the recombinant IgD on CHO cells. Moreover, MID962‐1200 stimulated peripheral blood lymphocyte (PBL) proliferation 5‐ and 15‐fold at 0.1 and 1.0 μg/ml, respectively. This activation could be blocked completely by antibodies directed against the CD40 ligand (CD154). MID962‐1200 also activated purified B cells in the presence of interleukin (IL)‐2 or IL‐4. An increased IL‐6 production was seen after stimulation with MID962‐1200, as revealed by a human cytokine protein array. MID962‐1200 fused to green fluorescent protein (GFP) bound to human B cells and activated PBL to the same degree as MID962‐1200. Taken together, MID is the only IgD‐binding protein in Moraxella. Furthermore, the novel T cell‐independent antigen MID962‐1200 may, together with MID962‐1200–GFP, be considered as promising reagents in the study of IgD‐dependent B cell activation.

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Section: Discussionmentioning

confidence: 99%

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

Nordström

Jendholm

Samuelsson

et al. 2005

Journal of Leukocyte Biology

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“…Data concerning the infectious process of M. catarrhalis and the mechanisms involved in the host protection are therefore limited. The targets for a protective immune response have not been identified, but the homogeneous composition of the outer membrane proteins and the lipopolysaccharide of M. cutarrhalis suggest that an antibody response to one strain may protect against others (1,24). However, the immune response to the organism seems to be poor, and young children fail to develop a systemic antibody response in a uniform manner after a middle ear infection (5,15).…”

mentioning

confidence: 99%

Moraxella catarrhalis‐induced purulent otitis media in the rat middle earL

Westman

Melhus

Hellström

et al. 1999

APMIS

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To study the effects of viable and heat‐killed Moraxella catarrhalis bacteria on the middle ear mucosa and to evaluate the protection after whole‐cell immunizations, Sprague‐Dawley rats were challenged and rechallenged with four different M. catarrhalis strains. The animals were monitored by clinical observations, bacterial and histological samples from middle ears, and serum IgG levels. Only viable bacteria at a high concentration induced purulent otitis media, which was culture positive in 58% of the cases on day 4. The infection was characterized by a mild acute reaction lasting otomicroscopically about 8 days, together with quantitative and qualitative changes of the goblet cells. Structurally the mucosal effects of the heat‐killed bacteria were less pronounced in the early phase compared to the viable bacteria, but similar at the end of the experiment at 6 months. The intrabullar and subcutaneous immunizations evoked an IgG antibody response in all animals, and the protection rate after immunization was 50% or more. The induced protection was not strain‐specific. The study showed the rat to be a possible alternative for the study of different aspects of M. catarrhalis otitis media, an infection that is clinically and structurally different from that elicited by Streptococcus pneumoniae and Haentophilus influenzae in the rat.

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“…21-30) may depend on cross-reactions with LPS of other bacteria, which makes the use of LPS-ELISA less specific. It has previously been shown that the LPS of M. catarrhalis displays different antigenic specificities (22). However, as we have shown in an earlier study, the human antibody response to the LPS antigens of M. cutarrhalis appears to be of low specificity (2 1).…”

Section: Discussionmentioning

confidence: 60%

“…A cross-reaction with Streptococcus pyugenes, which was demonstrated with rabbit antisera against nine strains of M. catarrhalis, was less pronounced with this strain than with most other strains (16). The LPS antigen was prepared from a reference strain belonging to type A (22), since this is the most common serotype. Based on previous studies (21) the inclusion of other serotype LPS preparations was not considered necessary, since the human antibody response to the M .…”

Section: Discussionmentioning

confidence: 99%

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Human immunoglobulin isotype and IgG subclass response to different antigens of Moraxella catarrhalis

Rahman

Holme

Jönsson

et al. 1997

APMIS

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Enzyme immunoassays were tested for the determination of antibodies of different isotypes and IgG subclasses to Moraxella catarrhalis in human sera. An assay based on an outer membrane protein preparation (OMP) as antigen was compared to assays using whole bacterial cells and a purified lipopolysaccharide preparation. There was a good correlation between the results obtained with the OMP preparation and the whole‐cell antigen. In paired sera, optimal sensitivity was obtained by using the OMP preparation as coating antigen and testing for a rise in IgG3 antibodies. However, patients with high levels of antibodies in acute serum had no or only an insignificant antibody response during infection.

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Serological typing of Branhamella catarrhalis strains on the basis of lipopolysaccharide antigens

Cited by 82 publications

References 25 publications

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

Moraxella catarrhalis‐induced purulent otitis media in the rat middle earL

Human immunoglobulin isotype and IgG subclass response to different antigens of Moraxella catarrhalis

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