Outer membrane protein CD of Branhamella catarrhalis: Sequence conservation in strains recovered from the human respiratory tract

1995 ◽  
Vol 19 (4) ◽  
pp. 215-225 ◽  
Author(s):  
Chiu Bin Hsiao ◽  
Sanjay Sethi ◽  
Timothy F. Murphy
Keyword(s):  
Membrane Protein ◽  
Respiratory Tract ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Sequence Conservation ◽  
Human Respiratory Tract ◽  
Branhamella Catarrhalis

scholarly journals Conservation of Outer Membrane Protein E among Strains of Moraxella catarrhalis

2001 ◽  
Vol 69 (6) ◽  
pp. 3576-3580 ◽  
Author(s):  
Timothy F. Murphy ◽  
Aimee L. Brauer ◽  
Norine Yuskiw ◽  
Erin R. McNamara ◽  
Charmaine Kirkham
Keyword(s):  
Monoclonal Antibodies ◽  
Membrane Protein ◽  
Respiratory Tract ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Moraxella Catarrhalis ◽  
Vaccine Antigen ◽  
Effective Vaccine ◽  
Human Respiratory Tract ◽  
The Stability

ABSTRACT Outer membrane protein E (OMP E) is a 50-kDa protein ofMoraxella catarrhalis which has several features that suggest that the protein may be an effective vaccine antigen. To assess the conservation of OMP E among strains of M. catarrhalis,22 isolates were studied with eight monoclonal antibodies which recognize epitopes on different regions of the protein. Eighteen of 22 strains were reactive with all eight antibodies. The sequences ofompE from 16 strains of M. catarrhalis were determined, including the 4 strains which were nonreactive with selected monoclonal antibodies. Analysis of sequences indicate a high degree of conservation among strains, with sequence differences clustered in limited regions of the gene. To assess the stability ofompE during colonization of the human respiratory tract, the sequences of ompE of isolates collected from patients colonized with the same strain for 3 to 9 months were determined. The sequences remained unchanged. These results indicate that OMP E is highly conserved among strains of M. catarrhalis, and preliminary studies indicate that the gene which encodes OMP E remains stable during colonization of the human respiratory tract.

Comparison of the cell envelope proteins of Micrococcus cryophilus with those of Neisseria and Branhamella species

1976 ◽  
Vol 22 (2) ◽  
pp. 309-312 ◽  
Author(s):  
R. R. B. Russell ◽  
I. J. McDonald
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Gel Electrophoresis ◽  
Cell Envelope ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Composition ◽  
Polyacrylamide Gel ◽  
Outer Membranes ◽  
Branhamella Catarrhalis

In an attempt to elucidate the relation between Micrococcus cryophilus, Neisseria caviae, Neisseria ovis, and Branhamella catarrhalis, fractions derived from outer membranes of a strain of each organism were examined for protein composition by SDS – polyacrylamide gel electrophoresis. Micrococcus cryophilus outer membrane protein showed extensive similarities to that of N. ovis and contained a heat-modifiable protein which behaved almost identically with the corresponding bands previously shown to exist in N. caviae and N. oris. Branhamella catarrhalis protein was distinctly different from those of M. cryophilus and the two 'false neisserias' N. caviae and N. oris.

scholarly journals Human Antibody Response to Outer Membrane Protein G1a, a Lipoprotein of Moraxella catarrhalis

2005 ◽  
Vol 73 (10) ◽  
pp. 6601-6607 ◽  
Author(s):  
Diana G. Adlowitz ◽  
Sanjay Sethi ◽  
Paul Cullen ◽  
Ben Adler ◽  
Timothy F. Murphy
Keyword(s):  
Membrane Protein ◽  
Palmitic Acid ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Moraxella Catarrhalis ◽  
Vaccine Candidate ◽  
Natural Infection ◽  
Chronic Obstructive ◽  
Human Antibody ◽  
Human Respiratory Tract

ABSTRACT Moraxella catarrhalis is an important cause of respiratory infections in adults with chronic obstructive pulmonary disease (COPD) and of otitis media in children. Outer membrane protein (OMP) G1a is an ∼29-kDa surface lipoprotein and is a potential vaccine candidate. The gene that encodes OMP G1a was expressed and purified using a novel plasmid vector. [3H]palmitic acid labeling demonstrated that both native and recombinant OMP G1a contain covalently bound palmitic acid. To assess the expression of OMP G1a during human infection, paired sera and sputum supernatants from adults with COPD followed prospectively were studied by enzyme-linked immunosorbent assays with recombinant lipidated OMP G1a to detect antibodies made specifically during carriage of M. catarrhalis. Overall, 23% of patients developed either a serum immunoglobulin G (IgG) response (9%) or sputum IgA response (21%) to OMP G1a, following 100 episodes of acquisition and clearance of M. catarrhalis. Patients developed antibody responses at similar rates following episodes of clinical exacerbation compared to asymptomatic colonization. Serum IgG antibodies following natural infection were directed predominantly at OMP G1a epitopes that are not exposed on the bacterial surface. These data show that OMP G1a is expressed during infection of the human respiratory tract and is a target of systemic and mucosal antibodies. These observations indicate that OMP G1a, a highly conserved surface protein, should be evaluated further as a vaccine candidate.

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