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  • Bacterial Outer Membrane Proteins
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  • 1
    Language: English
    In: The Journal of infectious diseases, 01 March 2002, Vol.185(5), pp.627-31
    Description: Nontypeable Haemophilus influenzae (NTHI) is an important cause of lower respiratory tract infections in patients with chronic obstructive pulmonary disease. Recent findings suggest that the major outer membrane protein P2 should be reconsidered as a vaccine candidate for NTHI. A P2-based vaccine would require a relative degree of sequence stability of the gene encoding P2 (ompP2) during colonization. To characterize the sequence stability of ompP2 during colonization of the human respiratory tract, ompP2 genes from 13 sets of isolates that persisted in patients with chronic obstructive pulmonary disease (mean colonization, 7 months) were sequenced. In 9 sets of isolates, ompP2 did not change. Sequence changes were noted in 4 sets of isolates. Most of these changes occurred within areas of repetitive DNA, suggesting that this type of DNA has a role in antigenic variation of P2. The sequence of ompP2 is relatively stable during persistence of NTHI in the human host.
    Keywords: Bacterial Proteins ; Genetic Variation ; Sequence Analysis, DNA ; Bacterial Outer Membrane Proteins -- Genetics ; Haemophilus Influenzae -- Classification ; Porins -- Genetics ; Respiratory Tract Infections -- Microbiology
    ISSN: 0022-1899
    E-ISSN: 15376613
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  • 2
    Language: English
    In: The Journal of infectious diseases, 01 July 2003, Vol.188(1), pp.114-7
    Description: An adult with chronic obstructive pulmonary disease was monitored prospectively for 2 years. Nontypeable Haemophilus influenzae was isolated from sputum cultures at 22 of 23 monthly clinic visits. Analysis of the isolates, by pulsed-field gel electrophoresis (PFGE), revealed that the patient was colonized by 3 different strains during the 2-year period. The gene encoding outer-membrane protein (OMP) P2, ompP2, was amplified from sputum samples and selected strains obtained from this patient. Analysis of the ompP2 sequences, in combination with the PFGE patterns, indicated that ompP2 horizontal transfer between 2 strains occurred in the respiratory tract, between clinic visits 13 and 14. Observation of ompP2 horizontal transfer in the human respiratory tract has important implications for both the understanding of ompP2 diversity among strains and the future design of OMP P2-based vaccines.
    Keywords: Bacterial Outer Membrane Proteins -- Genetics ; Gene Transfer, Horizontal -- Genetics ; Haemophilus Infections -- Complications ; Haemophilus Influenzae -- Genetics ; Pulmonary Disease, Chronic Obstructive -- Complications
    ISSN: 0022-1899
    E-ISSN: 15376613
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  • 3
    In: Journal of Bacteriology, March, 1997, Vol.179(5-6), p.1764(10)
    Description: The nucleotide sequence of the gene encoding the major outer membrane protein (MOMP) of Haemophilus ducreyi was analyzed by sodium dodecyl sulfate-polyacrilamide gel electrophoresis. Nucleotide sequence analysis of the MOMP gene of Haemophilus ducreyi indicated the presence of two OmpA homologs that were encoded by momp and ompA2 genes. Southern blot analysis also indicated the high degree of similarity between MOMP and OmpA2 which existed in tandem in the different strains of Haemophilus ducreyi.
    Keywords: Pathogenic Bacteria -- Genetic Aspects ; Membrane Proteins -- Analysis ; Bacterial Proteins -- Analysis
    ISSN: 0021-9193
    E-ISSN: 10985530
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  • 4
    Language: English
    In: Microbial Pathogenesis, February 1999, Vol.26(2), pp.93-102
    Description: A bactericidal assay was developed in order to test the effect of hyperimmune rabbit sera on the viability of serum-resistant Haemophilus ducreyi 35000HP. Testing of several lots of rabbit complement and time course experiments showed that the serum-sensitive H. ducreyi CIPA77 was killed efficiently by 25% complement at 35°C in 3 h. We hypothesized that incubation of 35000HP under these conditions with the appropriate bactericidal antibody would kill this strain. A panel of high titre rabbit antisera was developed and tested against 35000HP. The panel included antisera raised to whole cells, total membranes, Sarkosyl-insoluble outer membrane proteins, the H. ducreyi lipoprotein, and the peptidoglycan-associated lipoprotein. None of the antisera convincingly showed bactericidal activity. The bactericidal assay was also used to determine the effect of normal human serum (NHS) on isogenic mutants of 35000HP. 35000HP-RSM2, an kan insertion mutant that expresses a truncated lipooligosaccharide, was as resistant to NHS as its parent. A mutant deficient in expression of the major outer membrane protein (35000.60) was sensitive to NHS. We conclude that 35000HP is relatively resistant to normal and hyperimmune sera, and that the major outer membrane protein contributes to this resistance. Copyright 1999 Academic Press
    Keywords: Haemophilus Ducreyi, Bactericidal Activity, Chancroid ; Biology ; Chemistry
    ISSN: 0882-4010
    E-ISSN: 1096-1208
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  • 5
    Language: English
    In: Vaccine, 2004, Vol.22(20), pp.2533-2540
    Description: Moraxella catarrhalis is an important cause of otitis media, sinusitis, and lower respiratory tract infections in patients with chronic obstructive pulmonary disease. The purified outer membrane of M. catarrhalis contains a 29 kDa band, previously named outer membrane protein G1 (OMP G1). Polyclonal antiserum to the OMP G1 band was used to screen a genomic lambda phage library and the gene for OMP G1a was cloned and sequenced. Analysis of outer membrane by isoelectric focusing and amino-terminal protein sequence of the 29 kDa band revealed that the band is actually two individual proteins designated OMP G1a and OMP G1b. OMP G1a is a lipoprotein with an isoelectric point of 4. OMP G1b contains an unblocked amino-terminus and has an isoelectric point of 9. Analysis of the sequence of OMP G1a and OMP G1b from 25 clinical isolates revealed a high degree of conservation among strains. The sequence conservation of OMP G1a and OMP G1b among strains, combined with previous observations that OMP G1a and OMP G1b contain epitopes on the bacterial surface, indicate that OMP G1a and OMP G1b are potential vaccine antigens for M. catarrhalis .
    Keywords: Moraxella Catarrhalis ; Outer Membrane Protein ; Vaccine ; Medicine ; Biology ; Veterinary Medicine ; Pharmacy, Therapeutics, & Pharmacology
    ISSN: 0264-410X
    E-ISSN: 1873-2518
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