Brucella Immunogenic BP26 Forms a Channel-like Structure

Kim, Daegeun; Park, Jihye; Kim, Soo Jin; Soh, Young‐Min; Kim, Ho Min; Oh, Byung‐Ha; Song, Ji‐Joon

doi:10.1016/j.jmb.2013.01.015

Cited by 15 publications

(10 citation statements)

References 29 publications

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“…suis, B. ovis, B. canis, B. neotomae and B. melitensis. Recombinant OMP28 was sensitive and specific for diagnosis of Brucella infection in animals by indirect enzyme-linked immunosorbent assay (I-ELISA) (Kumar et al, 2008;Gupta et al, 2010;Thavaselvam et al, 2010;Liu et al, 2011;Dong-Bao et al, 2012;Lim et al, 2012;Qiu et al, 2012;Azizpour et al, 2013;Kim et al, 2013;Xin et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Expression, purification and immunochemical characterization of recombinant OMP28 protein of <i>Brucella</i> species

Manat¹,

Shustov²,

Evtehova³

et al. 2016

Open Vet J.

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Brucellosis is the lion's share of infectious disease of animals and it has a particular socio-economic importance for the Republic of Kazakhstan. Sixty percent of epizootic outbreaks of brucellosis identified in the Commonwealth of Independent States (CIS) originated from Kazakhstan in recent years. Definitive diagnosis of brucellosis remains a difficult task. Precisely for this reason, we evaluated a purified recombinant out membrane protein 28 (rOMP28) of Brucella species (Brucella spp.) produced in Escherichia coli (E. coli) as a diagnostic antigen in an Indirect ELISA (I-ELISA) for bovine brucellosis. The gene encoding OMP28 was synthesized using a two-round PCR procedure. In order to produce the rOMP28, the de novo synthesized DNA was cloned into the expression vector pET-22b(+). Then, the rOMP28 was expressed in E. coli system and characterized in the present study. We further estimated the diagnostic potential of purified rOMP28 of Brucella spp. for screening bovine sera. To determine if rOMP28 has a valuable benefit for use in the serodiagnosis of bovine brucellosis, rOMP28-based I-ELISA was performed. Brucella spp. positive (n=62) and Brucella spp. negative (n=28) samples from tube agglutination test (TAT) were positive (n=59) and negative (n=27) by I-ELISA, respectively. These findings show that the rOMP28 of Brucella spp. could be a good candidate for improving serological diagnostic methods for bovine brucellosis.

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Section: Introductionmentioning

confidence: 99%

Expression, purification and immunochemical characterization of recombinant OMP28 protein of <i>Brucella</i> species

Manat¹,

Shustov²,

Evtehova³

et al. 2016

Open Vet J.

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“…To gain insight into the binding sites for the ECM molecules and anti-Bp26 mouse serum, we mapped the binding peptides onto the crystal structure of Bp26 (PDB4HVZ) [22]. Bp26 forms a barrel-like homohexadecameric complex (Fig.…”

Section: Resultsmentioning

confidence: 99%

Binding of Brucella protein, Bp26, to select extracellular matrix molecules

ElTahir

Al-Araimi

Nair

et al. 2019

BMC Mol and Cell Biol

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BackgroundBrucella is a facultative intracellular pathogen responsible for zoonotic disease brucellosis. Little is known about the molecular basis of Brucella adherence to host cells. In the present study, the possible role of Bp26 protein as an adhesin was explored. The ability of Brucella protein Bp26 to bind to extracellular matrix (ECM) proteins was determined by enzyme-linked immunosorbent assay (ELISA) and biolayer interferometry (BLI).ResultsELISA experiments showed that Bp26 bound in a dose-dependent manner to both immobilized type I collagen and vitronectin. Bp26 bound weakly to soluble fibronectin but did not bind to immobilized fibronectin. No binding to laminin was detected. Biolayer interferometry showed high binding affinity of Bp26 to immobilized type I collagen and no binding to fibronectin or laminin. Mapping of Bp26 antigenic epitopes by biotinylated overlapping peptides spanning the entire sequence of Bp26 using anti Bp26 mouse serum led to the identification of five linear epitopes. Collagen and vitronectin bound to peptides from several regions of Bp26, with many of the binding sites for the ligands overlapping.The strongest binding for anti-Bp26 mouse serum, collagen and vitronectin was to the peptides at the C-terminus of Bp26. Fibronectin did not bind to any of the peptides, although it bound to the whole Bp26 protein.ConclusionsOur results highlight the possible role of Bp26 protein in the adhesion process of Brucella to host cells through ECM components. This study revealed that Bp26 binds to both immobilized and soluble type I collagen and vitronectin. It also binds to soluble but not immobilized fibronectin. However, Bp26 does not bind to laminin.These are novel findings that offer insight into understanding the interplay between Brucella and host target cells, which may aid in future identification of a new target for diagnosis and/or vaccine development and prevention of brucellosis.

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“…La amplificación de un fragmento del gen bp26, que codifica para la proteína periplasmática e inmunodominante BP26 de Brucella spp. (34), con una sensibilidad de 92,6 % y una especificidad de 90,0 % frente al hemocultivo, puede ser la prueba de elección o complementaria para el diagnóstico de la infección por B. canis (35).…”

Section: Colombiaunclassified

Seroprevalencia de Brucella canis en perros de un refugio para animales de compañía en Bogotá, Colombia

et al. 2021

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Introducción. El riesgo de infección con Brucella canis en humanos y perros aumenta con la exposición constante a perros portadores asintomáticos. En Colombia hay evidencia de infección con B. canis en personas que conviven con perros. Una preocupación adicional en Bogotá es la falta de información actualizada sobre la prevalencia de la infección en perros destinados a programas de adopción.Objetivo. Establecer la seroprevalencia de la infección por B. canis en perros de un refugio para animales de compañía destinados a la adopción en Bogotá.Materiales y métodos. Se hizo un estudio descriptivo de corte transversal en un refugio ara animales de Bogotá. Se detectaron anticuerpos contra B. canis en el suero de 51 perros (28 hembras y 23 machos) mediante una prueba inmunocromatográfica de flujo lateral. Asimismo, los individuos positivos se analizaron con PCR para la detección del ADN de Brucella spp.Resultado. La seroprevalencia de B. canis fue del 1,96 % (1/51). El perro seropositivo correspondió a una hembra asintomática de tres años de edad en la cual no se detectó ADN bacteriano en sangre mediante la PCR.Conclusiones. La seroprevalencia representada por un solo perro con IgG anti-B. canis puede considerarse un riesgo potencial para las poblaciones de perros y humanos, ya que podría tratarse de un animal con infección persistente capaz de diseminar la bacteria.

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Brucella Immunogenic BP26 Forms a Channel-like Structure

Cited by 15 publications

References 29 publications

Expression, purification and immunochemical characterization of recombinant OMP28 protein of <i>Brucella</i> species

Expression, purification and immunochemical characterization of recombinant OMP28 protein of <i>Brucella</i> species

Binding of Brucella protein, Bp26, to select extracellular matrix molecules

Seroprevalencia de Brucella canis en perros de un refugio para animales de compañía en Bogotá, Colombia

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