Comparative analysis of the Hom family of outer membrane proteins in isolates from two geographically distinct regions: The United States and South Korea

Helicobacter ◽  
2018 ◽  
Vol 23 (2) ◽  
pp. e12461 ◽  
Author(s):  
Stephanie L. Servetas ◽  
Aeryun Kim ◽  
Hanfu Su ◽  
Jeong‐Heon Cha ◽  
D. Scott Merrell
Keyword(s):  
United States ◽  
Comparative Analysis ◽  
Membrane Proteins ◽  
South Korea ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
The United States

Potentials for Colonization Control of Campylobacter jejuni in the Chicken

1989 ◽  
Vol 52 (6) ◽  
pp. 427-430 ◽  
Author(s):  
NORMAN J. STERN ◽  
RICHARD J. MEINERSMANN
Keyword(s):  
United States ◽  
Immune Response ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Campylobacter Jejuni ◽  
Intestinal Tract ◽  
Competitive Exclusion ◽  
Outer Membrane Proteins ◽  
The United States ◽  
Background Data

Campylobacter jejuni is a major cause of enteritis in humans. Chicken is the most important vehicle in transmitting the agent to humans in the United States. The organism colonizes the intestinal tract of the chicken and there enters into a non-pathologic, commensal relation. During slaughter and processing the organism can, and does, adulterate the product. Unsuccessful attempts have been made to “clean” the contaminated carcasses or provide pathogen free flocks and rearing facilities. Therefore, the approach to intervene and diminish C. jejuni in the intestinal tract is now being studied. We have been gathering background data on colonization dose, isolate differences regarding colonization, competitive exclusion, expression of outer membrane proteins by the organism, immune response of the chicken to colonization, antibody neutralization of colonization, and how poultry lineage influences susceptibility to colonization. By using this information we hope to diminish colonization of poultry with C. jejuni.

scholarly journals Comparative Analysis of Probabilistic Analysis and Deterministic Analysis by RESRAD Code

Energies ◽  
2020 ◽  
Vol 13 (8) ◽  
pp. 1983
Author(s):  
Sang June Park ◽  
Jihyang Byon ◽  
Seokyoung Ahn
Keyword(s):  
United States ◽  
Comparative Analysis ◽  
South Korea ◽  
Probabilistic Analysis ◽  
The United States ◽  
Exposure Dose ◽  
Nuclear Facilities ◽  
Deterministic Analysis ◽  
Specific Concentration ◽  
Site Release

The decommissioning of nuclear facilities indicates that the site is finally released according to a limited or unlimited site reuse purpose. In this process, the assessment of exposure dose to decommissioning workers and nearby residents is essential. Based on MARSSIM, a widely used decommissioning guideline in the United States, derivation of the exposure dose and derived concentration guideline level (DCGL) is mandatory using the probabilistic analysis of the RESRAD code. Here, DCGL is the radionuclide-specific concentration that satisfies the site release criteria. By applying the priority 1 parameter, which has the greatest effect on the dose, the dose is derived through deterministic and probabilistic analyses. The results were compared and analyzed. The purpose of this study was to provide a basic database that can be applied to the development of parameter lists and distributions suitable for the characteristics of nuclear facilities in South Korea. In addition, the process of deriving the dose by applying the deterministic and probabilistic analyses of RESRAD was assessed.

scholarly journals Immunization with Ehrlichia P28 Outer Membrane Proteins Confers Protection in a Mouse Model of Ehrlichiosis

2011 ◽  
Vol 18 (12) ◽  
pp. 2018-2025 ◽  
Author(s):  
Patricia A. Crocquet-Valdes ◽  
Nagaraja R. Thirumalapura ◽  
Nahed Ismail ◽  
Xuejie Yu ◽  
Tais B. Saito ◽  
...  
Keyword(s):  
T Cells ◽  
Membrane Proteins ◽  
Immune Responses ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
The United States ◽  
Mononuclear Phagocytes ◽  
Specific Cell ◽  
Content Type ◽  
Ifn Γ

ABSTRACTThe obligately intracellular bacteriumEhrlichia chaffeensisthat resides in mononuclear phagocytes is the etiologic agent of human monocytotropic ehrlichiosis (HME). HME is an emerging and often life-threatening, tick-transmitted infectious disease in the United States. Effective primary immune responses againstEhrlichiainfection involve generation ofEhrlichia-specific gamma interferon (IFN-γ)-producing CD4+T cells and cytotoxic CD8+T cells, activation of macrophages by IFN-γ, and production ofEhrlichia-specific antibodies of the Th1 isotype. Currently, there are no vaccines available against HME. We evaluated the ability of 28-kDa outer membrane proteins (P28-OMP-1) of the closely relatedEhrlichia muristo stimulate long-term protective memory T and B cell responses and confer protection in mice. The spleens of mice vaccinated withE. murisP28-9, P28-12, P28-19, or a mixture of these three P28 proteins (P28s) using a DNA prime-protein boost regimen and challenged withE. murishad significantly lower bacterial loads than the spleens of mock-vaccinated mice. Mice immunized with P28-9, P28-12, P28-19, or the mixture inducedEhrlichia-specific CD4+Th1 cells. Interestingly, mice immunized with P28-14, orthologs of which inE. chaffeensisandE. canisare primarily expressed in tick cells, failed to lower the ehrlichial burden in the spleen. Immunization with the recombinant P28-19 protein alone also significantly decreased the bacterial load in the spleen and liver compared to those of the controls. Our study reports, for the first time, the protective roles of theEhrlichiaP28-9 and P28-12 proteins in addition to confirming previous reports of the protective ability of P28-19. Partial protection induced by immunization with P28-9, P28-12, and P28-19 againstEhrlichiawas associated with the generation ofEhrlichia-specific cell-mediated and humoral immune responses.

scholarly journals Genetic Similarity of Gonococcal Homologs to Meningococcal Outer Membrane Proteins of Serogroup B Vaccine

mBio ◽  
2019 ◽  
Vol 10 (5) ◽  
Author(s):  
Henju Marjuki ◽  
Nadav Topaz ◽  
Sandeep J. Joseph ◽  
Kim M. Gernert ◽  
Ellen N. Kersh ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Vaccine Development ◽  
Membrane Vesicle ◽  
Outer Membrane Proteins ◽  
The United States ◽  
Cross Protection ◽  
Outer Membrane Vesicle ◽  
Content Type ◽  
Sequence Identity

ABSTRACT The human pathogens Neisseria gonorrhoeae and Neisseria meningitidis share high genome identity. Retrospective analysis of surveillance data from New Zealand indicates the potential cross-protective effect of outer membrane vesicle (OMV) meningococcal serogroup B vaccine (MeNZB) against N. gonorrhoeae. A licensed OMV-based MenB vaccine, MenB-4C, consists of a recombinant FHbp, NhbA, NadA, and the MeNZB OMV. Previous work has identified several abundantly expressed outer membrane proteins (OMPs) as major components of the MenB-4C OMV with high sequence similarity between N. gonorrhoeae and N. meningitidis, suggesting a mechanism for cross-protection. To build off these findings, we performed comparative genomic analysis on 970 recent N. gonorrhoeae isolates collected through a U.S surveillance system against N. meningitidis serogroup B (NmB) reference sequences. We identified 1,525 proteins that were common to both Neisseria species, of which 57 proteins were predicted to be OMPs using in silico methods. Among the MenB-4C antigens, NhbA showed moderate sequence identity (73%) to the respective gonococcal homolog, was highly conserved within N. gonorrhoeae, and was predicted to be surface expressed. In contrast, the gonococcal FHbp was predicted not to be surface expressed, while NadA was absent in all N. gonorrhoeae isolates. Our work confirmed recent observations (E. A. Semchenko, A. Tan, R. Borrow, and K. L. Seib, Clin Infect Dis, 2018, https://doi.org/10.1093/cid/ciy1061) and describes homologous OMPs from a large panel of epidemiologically relevant N. gonorrhoeae strains in the United States against NmB reference strains. Based on our results, we report a set of OMPs that may contribute to the previously observed cross-protection and provide potential antigen targets to guide the next steps in gonorrhea vaccine development. IMPORTANCE Gonorrhea, a sexually transmitted disease, causes substantial global morbidity and economic burden. New prevention and control measures for this disease are urgently needed, as strains resistant to almost all classes of antibiotics available for treatment have emerged. Previous reports demonstrate that cross-protection from gonococcal infections may be conferred by meningococcal serogroup B (MenB) outer membrane vesicle (OMV)-based vaccines. Among 1,525 common proteins shared across the genomes of both N. gonorrhoeae and N. meningitidis, 57 proteins were predicted to be surface expressed (outer membrane proteins [OMPs]) and thus preferred targets for vaccine development. The majority of these OMPs showed high sequence identity between the 2 bacterial species. Our results provide valuable insight into the meningococcal antigens present in the current OMV-containing MenB-4C vaccine that may contribute to cross-protection against gonorrhea and may inform next steps in gonorrhea vaccine development.

scholarly journals Comparative analysis of diagnostic colonoscopy in symptomatic young adults from South Korea and the United States

Medicine ◽  
2017 ◽  
Vol 96 (35) ◽  
pp. e7504
Author(s):  
Min Seob Kwak ◽  
Jae Myung Cha ◽  
Jeong-Sik Byeon ◽  
Otto S. Lin ◽  
Richard A. Kozarek
Keyword(s):  
United States ◽  
Young Adults ◽  
Comparative Analysis ◽  
South Korea ◽  
The United States ◽  
Diagnostic Colonoscopy

Analysis of the Membrane proteins of an Antarctic Bacterium Pseudomonas Syringae

2011 ◽  
Vol 4 ◽  
pp. PRI.S5383 ◽  
Author(s):  
M.V. Jagannadham ◽  
S. Saranya
Keyword(s):  
Comparative Analysis ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Pseudomonas Syringae ◽  
Cold Adaptation ◽  
Outer Membrane Proteins ◽  
Protein Preparation ◽  
Preparation Methods ◽  
Outer Membranes ◽  
Antarctic Bacterium

The proteins of an Antarctic bacterium Pseudomonas syringae Lz4W, identified earlier by different membrane protein preparation methods, were combined together and the redundant identities removed. In total, 1479 proteins including 148 outer membrane proteins from this bacterium were predicted by the algorithm PSORTb3.0. A detailed analysis on their subcellular localization was undertaken which was determined using TMHMM, TMB-hunt and BOMP. A comparison of PSORTb predicted outer membrane proteins with BOMP, revealed that most of the proteins predicted by the former, contained β–barrels in the outer membranes. A comparative analysis of PSORTb, TMHMM and TMB-hunt reveals that most of the outer membranes proteins of this bacterium could be identified using this approach. Thus, by using a combination of biochemical and different bioinformatics algorithms, the membrane proteins of P. syringae are analyzed. In particular, PSORTb results are compared and supported by other algorithms, to improve the strength of OM proteins prediction. Several proteins, having an important role in cold adaptation of the organism, could also be identified.

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