Outer membrane protein OlpA contributes to Moraxella catarrhalis serum resistance via interaction with factor H and the alternative pathway.

The outer membrane protein OlpA contributes to Moraxella catarrhalis serum

The UspA2 protein of Moraxella catarrhalis is directly involved in the expression of serum resistance.

Many strains of Moraxella catarrhalis are resistant to the bactericidal activity of normal human serum. Previous studies have shown that mutations involving the insertion of an antibiotic resistance cartridge into the M. catarrhalis uspA2 gene resulted in the conversion of a serum-resistant strain to a serum-sensitive phenotype. In the present study, the deletion of the entire uspA2 gene from t...

Antigenic structure of outer membrane protein E of Moraxella catarrhalis and construction and characterization of mutants.

Outer membrane protein E (OMP E) is a 50-kDa protein of Moraxella catarrhalis which possesses several characteristics indicating that the protein will be an effective vaccine antigen. To study the antigenic structure of OMP E, eight monoclonal antibodies were developed and characterized. Three of the antibodies recognized epitopes which are present on the bacterial surface. Fusion peptides corr...

Immunization with the Truncated Adhesin Moraxella catarrhalis Immunoglobulin D–Binding Protein (MID) Is Protective against M. catarrhalis in a Mouse Model of Pulmonary Clearance

Most Moraxella catarrhalis isolates express the outer membrane protein MID. In addition to its specific affinity for immunoglobulin D, MID functions as an adhesin and binds to human epithelium. The adhesive part is localized within MID. Two mid-deficient M. catarrhalis isolates were constructed and examined in a mouse model of pulmonary clearance. M. catarrhalis devoid of MID was cleared more e...

MID and UspA1/A2 of the human respiratory pathogen Moraxella catarrhalis, and interactions with the human host as basis for vaccine development.

Moraxella catarrhalis IgD-binding protein MID is a 200 kDa autotransporter protein that exists as a oligomer and is governed at the transcriptional level. The majority of M. catarrhalis clinical isolates expresses MID. Two functional domains have been attributed to MID; MID764-913 functions as an adhesin and promotes the bacteria to attach to epithelial cells, whereas the IgD-binding domain is ...