scholarly journals Sequence Stability of the Gene Encoding Outer Membrane Protein P2 of NontypeableHaemophilus influenzaein the Human Respiratory Tract

2002 ◽  
Vol 185 (5) ◽  
pp. 627-631 ◽  
Author(s):  
Thomas J. Hiltke ◽  
Sanjay Sethi ◽  
Timothy F. Murphy
Keyword(s):  
Membrane Protein ◽  
Respiratory Tract ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Human Respiratory Tract ◽  
Gene Encoding

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.

scholarly journals Conservation of msp, the gene encoding the major outer membrane protein of oral Treponema spp.

1997 ◽  
Vol 179 (4) ◽  
pp. 1082-1089 ◽  
Author(s):  
J C Fenno ◽  
G W Wong ◽  
P M Hannam ◽  
K H Müller ◽  
W K Leung ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Major Outer Membrane Protein ◽  
Gene Encoding

scholarly journals Identification of a Siderophore Receptor Required for Ferric Ornibactin Uptake in Burkholderia cepacia

2000 ◽  
Vol 68 (12) ◽  
pp. 6554-6560 ◽  
Author(s):  
P. A. Sokol ◽  
P. Darling ◽  
S. Lewenza ◽  
C. R. Corbett ◽  
C. D. Kooi
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Burkholderia Cepacia ◽  
Parent Strain ◽  
Respiratory Infections ◽  
Infection Model ◽  
Protein Profiles ◽  
Outer Membrane Receptor ◽  
Gene Encoding

ABSTRACT Ornibactins are linear hydroxamate siderophores produced byBurkholderia cepacia with peptide structures similar to that of pyoverdines produced by the fluorescent pseudomonads. The gene encoding the outer membrane receptor (orbA) was identified, sequenced, and demonstrated to have significant homology with hydroxamate receptors produced by other organisms. The orbAprecursor was predicted to be a protein with a molecular mass of 81 kDa. An orbA mutant was constructed and demonstrated to be unable to take up 59Fe-ornibactins or to grow in medium supplemented with ornibactins. Outer membrane protein profiles from the parent strain, K56-2, revealed an iron-regulated outer membrane protein of 78 kDa that was not detectable in the K56orbA::tp mutant. When this mutant harbored a plasmid containing the orbA gene, the 78-kDa protein was present in the outer membrane protein profiles and the mutant was able to utilize ornibactin to acquire iron. The orbA mutant was less virulent in a chronic respiratory infection model than the parent strain, indicating that ornibactin uptake and utilization are important in the pathogenesis of B. cepacia respiratory infections.

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