Induction of Immune Responses by Two Recombinant Proteins of Brucella abortus, Outer Membrane Proteins 2b Porin and Cu/Zn Superoxide Dismutase, in Mouse Model

2014 ◽  
Vol 24 (6) ◽  
pp. 854-861 ◽  
Author(s):  
Kyung Yong Sung ◽  
Myunghwan Jung ◽  
Min-Kyoung Shin ◽  
Hyun-Eui Park ◽  
Jin Ju Lee ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Membrane Proteins ◽  
Mouse Model ◽  
Immune Responses ◽  
Outer Membrane ◽  
Recombinant Proteins ◽  
Brucella Abortus ◽  
Outer Membrane Proteins

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 DEVELOPMENT OF THE VACCINE BASED ON THE RECOMBINANT ANTIGENS OF PSEUDOMONAS AERUGINOSA

2019 ◽  
Vol 1 (1) ◽  
pp. 74-80
Author(s):  
N. A. Mihailova ◽  
E. M. Zimina ◽  
A. V. Soldatenkova ◽  
A. A. Kaloshin
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Membrane Proteins ◽  
Fusion Protein ◽  
Outer Membrane ◽  
Recombinant Proteins ◽  
Fusion Proteins ◽  
Outer Membrane Proteins ◽  
Recombinant Fusion Protein ◽  
Recombinant Antigens ◽  
Recombinant Fusion Proteins

Aim. The aim is obtaining, investigation and selection of recombinant antigens for inclusion theirs into the against Pseudomonas vaccine. Materials and methods. The genes encoding of the outer  membrane proteins F, L and I and Exotoxin A were synthesized by PCR with the genomic DNA of Pseudomonas aeruginosa. The amplified sequences were cloned into plasmid vectors for expression in cells of Escherichia coli. As the result of expression were the synthesized recombinant proteins that were purified in columns with a nickel-activated sorbent. The authenticity of the recombinant antigens was assessed by electrophoresis and immunoblotting. For assessing the immunogenicity of the recombinant proteins,they were sorbed on aluminum hydroxide and used for intraperitoneal immunization of mice. After a course of immunization, mice were injected intraperitoneally with a live virulent culture or еxotoxin A. Results. The obtained recombinant outer membrane proteins OprF, OprL and OprI, as well as the deletion variant of еxotoxin A (toxoid) stimulated immune reactions and protected the experimental animals from the virulent culture of P. aeruginosa. Using of the complexes of the recombinant proteins, as well as immunization with the fusion proteins consisting from sequences of two or three recombinant antigens, produced an additive increase in protective effects. The combination of the recombinant OprF protein and the recombinant toxoid (efficiency index of protective properties (EI 3.0) and two recombinant fusion proteins (EI 3.5) were the most effective. The first recombinant fusion protein (OprF-aTox-OprI) consisted from fused polypeptide sequences of OprF, toxoid and OprI. The second recombinant fusion protein (OprF-OprI) consisted from fused polypeptide sequences of OprF and OprI. Conclusion. The data obtained showed the fundamental possibility of using recombinant fusion proteins OprF-aTox-OprI and OprF-OprI as well as the complex of the recombinant OprF protein and the recombinant toxoid as the candidated vaccines against Pseudomonas aeruginosa.

scholarly journals Outer membrane proteins of Brucella abortus: isolation and characterization.

1982 ◽  
Vol 35 (3) ◽  
pp. 979-989 ◽  
Author(s):  
D R Verstreate ◽  
M T Creasy ◽  
N T Caveney ◽  
C L Baldwin ◽  
M W Blab ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Brucella Abortus ◽  
Outer Membrane Proteins ◽  
Isolation And Characterization

Protective immune responses of recombinant outer membrane proteins OmpF and OmpK of Aeromonas hydrophila in European eel ( Anguilla anguilla )

2019 ◽  
Vol 50 (12) ◽  
pp. 3559-3566
Author(s):  
Weini Zhang ◽  
Zichao Liao ◽  
Fengxiao Hu ◽  
Xinhua Chen ◽  
Xiaohong Huang
Keyword(s):  
Membrane Proteins ◽  
Immune Responses ◽  
Outer Membrane ◽  
Aeromonas Hydrophila ◽  
Outer Membrane Proteins ◽  
Anguilla Anguilla ◽  
European Eel

scholarly journals Protective Immunity and Reduced Renal Colonization Induced by Vaccines Containing Recombinant Leptospira interrogans Outer Membrane Proteins and Flagellin Adjuvant

2015 ◽  
Vol 22 (8) ◽  
pp. 965-973 ◽  
Author(s):  
D. Monaris ◽  
M. E. Sbrogio-Almeida ◽  
C. C. Dib ◽  
T. A. Canhamero ◽  
G. O. Souza ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Immune Responses ◽  
Outer Membrane ◽  
Protective Immunity ◽  
Outer Membrane Proteins ◽  
Protein A ◽  
Leptospira Interrogans ◽  
Renal Tubules ◽  
Subunit Vaccines ◽  
Content Type

ABSTRACTLeptospirosis is a global zoonotic disease caused by differentLeptospiraspecies, such asLeptospira interrogans, that colonize the renal tubules of wild and domestic animals. Thus far, attempts to develop effective leptospirosis vaccines, both for humans and animals, have failed to induce immune responses capable of conferring protection and simultaneously preventing renal colonization. In this study, we evaluated the protective immunity induced by subunit vaccines containing seven different recombinantLeptospira interrogansouter membrane proteins, including the carboxy-terminal portion of the immunoglobulinlike protein A (LigAC) and six novel antigens, combined with aluminum hydroxide (alum) orSalmonellaflagellin (FliC) as adjuvants. Hamsters vaccinated with the different formulations elicited high antigen-specific antibody titers. Immunization with LigAC, either with alum or flagellin, conferred protective immunity but did not prevent renal colonization. Similarly, animals immunized with LigACor LigACcoadministered with six leptospiral proteins with alum adjuvant conferred protection but did not reduce renal colonization. In contrast, immunizing animals with the pool of seven antigens in combination with flagellin conferred protection and significantly reduced renal colonization by the pathogen. The present study emphasizes the relevance of antigen composition and added adjuvant in the efficacy of antileptospirosis subunit vaccines and shows the complex relationship between immune responses and renal colonization by the pathogen.

scholarly journals Outer Membrane Proteins Omp10, Omp16, and Omp19 of Brucella spp. Are Lipoproteins

1999 ◽  
Vol 67 (9) ◽  
pp. 4960-4962 ◽  
Author(s):  
Anne Tibor ◽  
Béatrice Decelle ◽  
Jean-Jacques Letesson
Keyword(s):  
Monoclonal Antibodies ◽  
Membrane Proteins ◽  
Palmitic Acid ◽  
Outer Membrane ◽  
Brucella Abortus ◽  
Outer Membrane Proteins ◽  
Specific Inhibitor ◽  
Signal Peptidase ◽  
Processing Sequence ◽  
Triton X

ABSTRACT The deduced sequences of the Omp10, Omp16, and Omp19 outer membrane proteins of Brucella spp. contain a potential bacterial lipoprotein processing sequence. After extraction with Triton X-114, these three proteins partitioned into the detergent phase. Processing of the three proteins is inhibited by globomycin, a specific inhibitor of lipoprotein signal peptidase. The three proteins were radioimmunoprecipitated from [3H]palmitic acid-labeledBrucella abortus lysates with monoclonal antibodies. These results demonstrate that Omp10, Omp16, and Omp19 are lipoproteins.

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