Lack of immunoglobulin A1 protease production by Branhamella catarrhalis.

Immunoglobulin G (IgG) serological response to Branhamella catarrhalis in patients with acute bronchopulmonary infections.

Over 12 months serum was collected from 45 inpatients, with acute bronchopulmonary infection, in whose sputum Branhamella catarrhalis predominated, or was the sole pathogen. Serum was examined for IgG against B catarrhalis using an immunofluorescence antibody test. Acute and convalescent sera were compared with sera of age and sex matched controls. The convalescent sera had significantly higher...

Author's response to reviews Title: Moraxella catarrhalis acquisition, airway inflammation and protease-antiprotease balance in chronic obstructive pulmonary disease Authors:

Branhamella catarrhalis

A modified oxidation-fermentation medium was developed as a practical medium for highly sensitive and specific detection of acid production from carbohydrates by Neisseria spp. and Branhamella catarrhalis. A total of 756 strains representing 17 Neisseria spp. and Branhamella catarrhalis were tested in this medium, in which the protein concentration was reduced relative to the carbohydrate conce...

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 ...

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...