Serum antibody response to proteins of Moraxella (Branhamella) catarrhalis in patients with lower respiratory tract infection

Christensen, Jens Jørgen; Renneberg, J; Bruun, Brita; Forsgren, Andarne

doi:10.1128/cdli.2.1.14-17.1995

Cited by 9 publications

(9 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In spite of this limitation, the prospective design of this study allows us to measure antibodies made specifically to each episode of acquisition of M. catarrhalis because of the availability of prospectively collected preacquisition and postclearance samples. Christensen et al (1995Christensen et al ( , 1996 identified a serum IgG response to an OMP in the 28-kDa range in adults with lower respiratory tract infections with M. catarrhalis. This 28-kDa protein might be OMP G1b.…”

Section: Discussionmentioning

confidence: 99%

Human serum and mucosal antibody responses to outer membrane protein G1b ofMoraxella catarrhalisin chronic obstructive pulmonary disease

Adlowitz¹,

Kirkham

Sethi

et al. 2006

FEMS Immunology &Amp; Medical Microbiology

View full text Add to dashboard Cite

Moraxella catarrhalis is an important human pathogen that causes otitis media, sinusitis, and lower respiratory tract infections in adults with chronic obstructive pulmonary disease. Outer membrane protein G1b is a approximately 29-kDa protein that has a high degree of homology among strains, contains surface-exposed epitopes, and is a potential vaccine candidate. The ompG1b gene was cloned, expressed in Escherichia coli, and purified. To assess the expression of outer membrane protein G1b during human infection, paired serum and sputum supernatants from patients with chronic obstructive pulmonary disease followed prospectively were studied by enzyme-linked immunosorbent assays with recombinant outer membrane protein G1b to detect antibodies made specifically during carriage of M. catarrhalis. Overall, 39% of patients developed either a serum IgG (28.6%) or a sputum supernatant IgA (19.2%) response to outer membrane protein G1b following 100 episodes of acquisition and clearance of M. catarrhalis. A sputum supernatant IgA response was more likely following exacerbations compared with asymptomatic colonizations, whereas a serum IgG response occurred at similar rates. Serum IgG antibodies following natural infection were directed toward surface-exposed epitopes of outer membrane protein G1b. Overall, these studies show that outer membrane protein G1b is expressed during infection of the human respiratory tract and that human antibodies bind to outer membrane protein G1b epitopes on the bacterial surface. These observations indicate that outer membrane protein G1b should be evaluated further as a vaccine antigen.

show abstract

Section: Discussionmentioning

confidence: 99%

Human serum and mucosal antibody responses to outer membrane protein G1b ofMoraxella catarrhalisin chronic obstructive pulmonary disease

Adlowitz¹,

Kirkham

Sethi

et al. 2006

FEMS Immunology &Amp; Medical Microbiology

View full text Add to dashboard Cite

show abstract

“…This epitope is present in all disease-associated isolates of M. catarrhalis tested to date and induces the synthesis of antibodies that, when used to passively immunize mice, enhanced the elimination of M. catarrhalis in a pulmonary clearance model (27). Equally important, the very high molecular weight UspA antigen composed of UspA1 and UspA2 has been shown to be a target for antibodies present in convalescent sera of patients recovering from M. catarrhalis infections (13,25,27), indicating that one or both of these proteins are expressed in vivo.…”

mentioning

confidence: 99%

Phenotypic Effect of IsogenicuspA1anduspA2Mutations onMoraxella catarrhalis035E

Aebi

Lafontaine²,

Cope³

et al. 1998

Infect Immun

147

View full text Add to dashboard Cite

The UspA surface antigen of Moraxella catarrhalis was recently shown to be comprised of two different proteins (UspA1 and UspA2) which share an internal region containing 140 amino acids with 93% identity (C. Aebi, I. Maciver, J. L. Latimer, L. D. Cope, M. K. Stevens, S. E. Thomas, G. H. McCracken, Jr., and E. J. Hansen, Infect. Immun. 65:4367–4377, 1997). Isogenic uspA1, uspA2, and uspA1 uspA2 mutants were tested in a number of in vitro systems to determine what effect these mutations, either individually or together, might exert on the phenotype of M. catarrhalis 035E. Monoclonal antibodies specific for UspA1 or UspA2 were used in an indirect antibody accessibility assay to prove that both of these proteins were expressed on the surface of M. catarrhalis. All three mutants grew in vitro at the same rate and did not exhibit autoagglutination or hemagglutination properties that were detectably different from those of the wild-type parent strain. When tested for the ability to adhere to human epithelial cells, the wild-type parent strain and the uspA2 mutant readily attached to Chang conjunctival cells. In contrast, theuspA1 mutant and the uspA1 uspA2 double mutant both attached to these epithelial cells at a level nearly 2 orders of magnitude lower than that obtained with the wild-type parent strain, a result which suggested that expression of UspA1 byM. catarrhalis is essential for attachment to these epithelial cells. Both the wild-type parent strain and theuspA1 mutant were resistant to the bactericidal activity of normal human serum, whereas the uspA2 mutant and theuspA1 uspA2 double mutant were readily killed by this serum. This latter result indicated that the presence of UspA2 is essential for expression of serum resistance by M. catarrhalis.

show abstract

“…Second, children develop serum antibodies to M. catarrhalis after age 4 (14), and this appears to correlate with a decrease in the frequency of otitis media caused by M. catarrhalis. Third, antibodies to M. catarrhalis antigens have been detected in both the acute-phase and convalescent-phase sera of adult patients (7,15). These data suggest that an appropriate humoral response to the surface antigens of this bacterium is likely to provide protection.…”

mentioning

confidence: 89%

“…Passive immunization with one of these MAbs, 17C7, enhanced pulmonary clearance of both homologous and heterologous isolates in a murine pulmonary challenge model (17). The observation that human convalescent-phase sera contain antibodies to UspA indicates that this protein is expressed by M. catarrhalis in vivo (7,15,17). M. catarrhalis gains entry to the host by attachment to and colonization on the epithelial cell surface of the respiratory tract (1,2).…”

mentioning

confidence: 99%

Evaluation of purified UspA from Moraxella catarrhalis as a vaccine in a murine model after active immunization

et al. 1996

View full text Add to dashboard Cite

Moraxella catarrhalis causes otitis media, laryngitis, and respiratory infections in humans. A high-molecularweight outer membrane protein from this bacterium named ubiquitous surface protein A (UspA) is present on all isolates. A monoclonal antibody (MAb) to UspA that recognizes a conserved epitope of this protein has been shown to promote pulmonary clearance of bacteria in passively immunized mice. In the present study, M. catarrhalis heterologous isolates were screened by dot blot with a panel of four additional MAbs specific for surface-exposed epitopes of UspA from M. catarrhalis isolate O35E. Three of the MAbs were specific for O35E, and the fourth reacted with 17 (74%) of the 23 isolates tested. Thus, UspA contains highly conserved, semiconserved, and variable surface-exposed epitopes. The UspA was purified from the O35E isolate by ion-exchange and size-exclusion chromatography, formulated with the adjuvant QS-21, and used to immunize BALB/c mice. Upon pulmonary challenge with either O35E or the heterologous isolate TTA24, significantly fewer bacteria were recovered from the lungs of immunized mice 6 h postchallenge than from control mice. The immune sera from mice or guinea pigs contained high titers of antibodies to the homologous isolate and heterologous isolates in a whole-bacterial-cell enzyme-linked immunosorbent assay. Sera against UspA, whether prepared in mice or guinea pigs, had complement-dependent bactericidal activity toward homologous and 11 heterologous M. catarrhalis isolates. These results indicate that the conserved epitopes of the UspA are highly immunogenic and elicit broadly reactive and biologically functional antibodies. UspA may offer protection against M. catarrhalis infections and is being further evaluated as a vaccine candidate.

show abstract

Serum antibody response to proteins of Moraxella (Branhamella) catarrhalis in patients with lower respiratory tract infection

Cited by 9 publications

References 19 publications

Human serum and mucosal antibody responses to outer membrane protein G1b ofMoraxella catarrhalisin chronic obstructive pulmonary disease

Human serum and mucosal antibody responses to outer membrane protein G1b ofMoraxella catarrhalisin chronic obstructive pulmonary disease

Phenotypic Effect of IsogenicuspA1anduspA2Mutations onMoraxella catarrhalis035E

Evaluation of purified UspA from Moraxella catarrhalis as a vaccine in a murine model after active immunization

Contact Info

Product

Resources

About