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  • 1
    Language: English
    In: The Journal of Infectious Diseases, 06/15/2010, Vol.201(S2), pp.114-125
    Description: Although the pathologic consequences of C. trachomatis genital infection are well-established, the mechanism(s)that result in chlamydia-induced tissue damage are not fully understood. We reviewed in vitro, animal, and human data related to the pathogenesis of chlamydial disease to better understand how reproductive sequelae result from C. trachomatis infection. Abundant in vitro data suggest that the inflammatory response to chlamydiae is initiated and sustained by actively infected nonimmune host epithelial cells. The mouse model indicates a critical role for chlamydia activation of the innate immune receptor, Toll-like receptor 2, and subsequent inflammatory cell influx and activation, which contributes to the development of chronic genital tract tissue damage. Data from recent vaccine studies in the murine model and from human immunoepidemiologic studies support a role for chlamydia-specific CD4 Th1-interferon-g-producing cells in protection from infection and disease. However, limited evidence obtained using animal models of repeated infection indicates that, although the adaptive T cell response is a key mechanism involved in controlling or eliminating infection, it may have a double-edged nature and contribute to tissue damage. Important immunologic questions include whether anamnestic CD4 T cell responses drive disease rather than protect against disease and the role of specific immune cells and inflammatory mediators in the induction of tissue damage with primary and repeated infections. Continued study of the complex molecular and cellular interactions between chlamydiae and their host and large-scale prospective immunoepidemiologic and immunopathologic studies are needed to address gaps in our understanding of pathogenesis that thwart development of optimally effective control programs, including vaccine development.
    Keywords: Medicine ; Biology;
    ISSN: 0022-1899
    E-ISSN: 1537-6613
    Source: CrossRef
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  • 2
    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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  • 3
    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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  • 4
    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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  • 5
    Language: English
    In: The Journal of Infectious Diseases, 1 June 1998, Vol.177(6), pp.1608-1613
    Description: Human subjects were infected with Haemophilus ducreyi. All subjects developed papules and were randomized to treatment with a single dose of azithromycin (1 g) or ciprofloxacin (500 mg). At weekly intervals, volunteers were reinoculated with H. ducreyi, and drug concentrations were measured in peripheral blood mononuclear cells (PBMC). When papules developed, the subjects were treated with antibiotics and dismissed from the study. Eight of the ciprofloxacin-treated subjects developed papules 1 week after the initial treatment, and the ninth subject developed disease 2 weeks after treatment. The 9 azithromycin-treated subjects developed papules 4-10 weeks (mean, 6.8) after the initial treatment (P 〈 .001). Azithromycin was detected in PBMC for 3-6 weeks (mean, 4). Pre-and posttreatment lesions had histology typical of experimental chancroid or were culture positive. Azithromycin prevents experimental chancroid for nearly 2 months. These findings have implications for strategies to prevent chancroid.
    Keywords: Health sciences -- Medical conditions -- Infections -- Haemophilus ducreyi ; Health sciences -- Medical sciences -- Pharmacology -- HIV ; Health sciences -- Medical conditions -- Infections -- HIV ; Health sciences -- Medical diagnosis -- Diagnostic methods -- HIV ; Biological sciences -- Biology -- Microbiology -- HIV ; Biological sciences -- Biology -- Microbiology -- HIV ; Biological sciences -- Biology -- Microbiology -- HIV ; Health sciences -- Medical specialties -- Pathology -- HIV ; Health sciences -- Medical conditions -- Physical trauma -- HIV ; Physical sciences -- Physics -- Microphysics -- HIV
    ISSN: 00221899
    E-ISSN: 15376613
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  • 6
    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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  • 7
    Language: English
    In: Cell, 28 July 2016, Vol.166(3), pp.755-765
    Description: To provide a detailed analysis of the molecular components and underlying mechanisms associated with ovarian cancer, we performed a comprehensive mass-spectrometry-based proteomic characterization of 174 ovarian tumors previously analyzed by The Cancer Genome Atlas (TCGA), of which 169 were high-grade serous carcinomas (HGSCs). Integrating our proteomic measurements with the genomic data yielded a number of insights into disease, such as how different copy-number alternations influence the proteome, the proteins associated with chromosomal instability, the sets of signaling pathways that diverse genome rearrangements converge on, and the ones most associated with short overall survival. Specific protein acetylations associated with homologous recombination deficiency suggest a potential means for stratifying patients for therapy. In addition to providing a valuable resource, these findings provide a view of how the somatic genome drives the cancer proteome and associations between protein and post-translational modification levels and clinical outcomes in HGSC. Layering proteomic and genomic data from ovarian tumors provides insights into how signaling pathways correspond to specific genome rearrangements and points to the benefit of using protein signatures for assessing prognosis and treatment stratification.
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
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  • 8
    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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  • 9
    Language: English
    In: Methods in molecular biology (Clifton, N.J.), 2016, Vol.1410, pp.223-36
    Description: The Clinical Proteomic Tumor Analysis Consortium (CPTAC) of the National Cancer Institute (NCI) has launched an Assay Portal (http://assays.cancer.gov) to serve as an open-source repository of well-characterized targeted proteomic assays. The portal is designed to curate and disseminate highly characterized, targeted mass spectrometry (MS)-based assays by providing detailed assay performance characterization data, standard operating procedures, and access to reagents. Assay content is accessed via the portal through queries to find assays targeting proteins associated with specific cellular pathways, protein complexes, or specific chromosomal regions. The position of the peptide analytes for which there are available assays are mapped relative to other features of interest in the protein, such as sequence domains, isoforms, single nucleotide polymorphisms, and posttranslational modifications. The overarching goals are to enable robust quantification of all human proteins and to standardize the quantification of targeted MS-based assays to ultimately enable harmonization of results over time and across laboratories.
    Keywords: Harmonization ; Mrm ; Multiple Reaction Monitoring ; PRM ; Quantitative Assay Database ; Quantitative Proteomics ; Srm ; Selected Reaction Monitoring ; Standardization ; Targeted Mass Spectrometry ; Proteomics -- Methods
    E-ISSN: 1940-6029
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  • 10
    In: Nature Biotechnology, 2009, Vol.27(7), p.633
    Description: Verification of candidate biomarkers relies upon specific, quantitative assays optimized for selective detection of target proteins, and is increasingly viewed as a critical step in the discovery pipeline that bridges unbiased biomarker discovery to preclinical validation. Although individual laboratories have demonstrated that multiple reaction monitoring (MRM) coupled with isotope dilution mass spectrometry can quantify candidate protein biomarkers in plasma, reproducibility and transferability of these assays between laboratories have not been demonstrated. We describe a multilaboratory study to assess reproducibility, recovery, linear dynamic range and limits of detection and quantification of multiplexed, MRM-based assays, conducted by NCI-CPTAC. Using common materials and standardized protocols, we demonstrate that these assays can be highly reproducible within and across laboratories and instrument platforms, and are sensitive to low mug/ml protein concentrations in unfractionated plasma. We provide data and benchmarks against which individual laboratories can compare their performance and evaluate new technologies for biomarker verification in plasma.
    Keywords: Blood Proteins -- Analysis ; Mass Spectrometry -- Methods;
    ISSN: 1087-0156
    E-ISSN: 15461696
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