Protection against Brucella abortus in mice with O-polysaccharide-specific monoclonal antibodies

Montaraz, J A; Winter, A J; Hunter, D.; Sowa, Blair A.; Wu, Albert M.; Adams, L. Garry

doi:10.1128/iai.51.3.961-963.1986

Cited by 110 publications

(60 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…IgG subtypes, IgG1 and IgG2a, are indicative of Th2 and Th1 responses, respectively, but there were no significant differences in either isotype in mice vaccinated with OMVs vs. OMVs + P85. Antibodies have been shown before to provide protection against B. melitensis infection in mouse models (Montaraz et al, 1986;Limet et al, 1987;Adone et al, 2012). Increased levels of IgG could have helped in the clearance of circulating Brucella and enhanced the protection against B. melitensis challenge in OMVs + P85-vaccinated mice.…”

Section: Antibody Titers In Plasmamentioning

confidence: 99%

Pluronic P85 enhances the efficacy of outer membrane vesicles as a subunit vaccine againstBrucella melitensischallenge in mice

Jain-Gupta

Contreras-Rodríguez

Vemulapalli

et al. 2012

FEMS Immunol Med Microbiol

View full text Add to dashboard Cite

Brucellosis is the most common zoonotic disease worldwide and there is no vaccine for human use. Brucella melitensis Rev1, a live attenuated strain, is the commercial vaccine for small ruminants to prevent B. melitensis infections but has been associated with abortions in animals. Moreover, strain Rev1 is known to cause disease in humans and cannot be used for human vaccination. Outer membrane vesicles (OMVs) obtained from B. melitensis have been shown to provide protection similar to strain Rev1 in mice against B. melitensis challenge. In the present work we tested the efficacy of Pluronic P85 as an adjuvant to enhance the efficacy of Brucella OMVs as a vaccine. P85 enhanced the in vitro secretion of TNF-α by macrophages induced with OMVs and P85. Further, P85 enhanced the protection provided by OMVs against B. melitensis challenge. This enhanced protection was associated with higher total IgG antibody production but not increased IFN-γ or IL-4 cytokine levels. Moreover, P85 alone provided significantly better clearance of B. melitensis compared to saline vaccinated mice. Further studies are warranted to find the mechanism of action of P85 that provides non-specific protection and enhances the efficacy of OMVs as a vaccine against B. melitensis.

show abstract

Section: Antibody Titers In Plasmamentioning

confidence: 99%

Pluronic P85 enhances the efficacy of outer membrane vesicles as a subunit vaccine againstBrucella melitensischallenge in mice

Jain-Gupta

Contreras-Rodríguez

Vemulapalli

et al. 2012

FEMS Immunol Med Microbiol

View full text Add to dashboard Cite

show abstract

“…However, we cannot exclude that protective activity by the major OMPs against S Bruce& strains could occur through cell-mediated immunity. The contamination by S-LPS, which has been shown to be protective against S Brucellu strains through antibodymediated immunity [20,22], in purified OMP preparations has prevented us from investigating this point. Availability of recombinant Brucellu OMPs could be of great importance to determine their role in protecting against infection.…”

Section: Introductionmentioning

confidence: 99%

Molecular and immunological characterization of the major outer membrane proteins ofBrucella

Cloeckaert

Verger

Grayon

et al. 1996

FEMS Microbiology Letters

View full text Add to dashboard Cite

The major outer membrane proteins (OMPs) of Brucella spp. were initially identified in the early 1980s by selective extraction techniques and classified according to their apparent molecular mass as 36-38 kDa OMPs or group 2 porin proteins and 31-34 kDa and 25-27 kDa OMPs which belong to the group 3 proteins. Variation in apparent molecular mass is essentially due to association with peptidoglycan subunits of different sizes. Two genes, omp2a and omp2b, which are closely linked in the Brucella genome, and which share a great degree of homology (> 85%), encode the 36 kDa porin proteins, now named Omp2a and Omp2b proteins respectively. Two genes code for the group 3 OMPs and are named omp25 and omp31. The predicted amino acid sequences of omp25 and omp31 share 34% identity. Furthermore, all Brucella major OMPs share amino acid sequence homology with the major OMPs RopA or RopB of Rhizobium leguminosarum, which supports the close genetic relationship of brucellae with members of the alpha-2 subdivision of the class Proteobacteria. Another characteristic common to the major OMPs of R. leguminosarum and Brucella is that they are tightly, probably covalently, associated with the peptidoglycan. The major OMP genes display diversity among Brucella species, biovars and strains allowing their differentiation, and the polymorphic markers identified have brought new insights into the evolutionary development of the genus Brucella, antigenic variability of brucellae, and future prospects in the field of vaccine development.

show abstract

“…Microorganisms belonging to the genus Brucella are facultative intracellular parasites that cause brucellosis in animals and man. Studies conducted to improve knowledge of the mechanisms inducing protection against brucellosis have demonstrated, in the mouse model, that both humoral [1][2][3][4][5][6][7] and cell-mediated (both CD4 + and CD8 + T cells subsets) [8,9] immune responses * Corresponding author. Tel.…”

Section: Introductionmentioning

confidence: 99%

“…Antibodies with specificity for the Brucella spp. smooth lipopolysaccharide (S-LPS) [5,6] and specially those O-polysaccharide-specific [1][2][3][4]7] have been demonstrated, in the mouse model, to play a crucial role in protective immunity. Brucella spp.…”

Section: Introductionmentioning

confidence: 99%

“…It has been suggested that the protection against Brucella spp. infection conferred by passively transferred polyclonal antisera or monoclonal antibodies [1][2][3][4][6][7][8][9] would be due to an increased ingestion and intracellular killing of the microorganisms in phagocytic cells [7]. Monoclonal antibodies (mAb) with specificity for the A epitope have been shown to confer protection in mice against infection by Brucella strains bearing the homologous A antigenic determinant as the major epitope on the O-polysaccharide chain [1,2].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Protection and suppression of the humoral immune response in mice mediated by a monoclonal antibody against the M epitope of Brucella

Vizcaı́no¹

1994

FEMS Immunology and Medical Microbiology

View full text Add to dashboard Cite

The capacity of the BmE10-5 monoclonal antibody (mAb), with specificity for the Brucella spp. M epitope, to confer protection against infection with B. abortus 2308 (A-dominant strain) has been evaluated. Injected before infection, the BmE10-5 mAb diminished the bacterial counts in spleen from week 1 to week 8 postinfection and in liver from week 4 to week 7. Thus, protection mediated by the BmE10-5 mAb, as measured by a reduction in the bacterial counts in both spleen and liver, was demonstrated from week 2 to week 8 postinfection. The humoral immune response of IgG, IgM, IgG1 and IgG3 antibodies, specific against the B. abortus 2308 smooth lipopolysaccharide, was clearly suppressed in all the mice protected with the BmE10-5 mAb, thus demonstrating the importance, in protecting against infection, of the existence in serum of M-epitope-specific antibodies at the same time the infection is acquired. The development of subcellular vaccines including the Brucella M epitope could constitute an interesting alternative to attenuated living vaccines.

show abstract

Protection against Brucella abortus in mice with O-polysaccharide-specific monoclonal antibodies

Cited by 110 publications

References 15 publications

Pluronic P85 enhances the efficacy of outer membrane vesicles as a subunit vaccine againstBrucella melitensischallenge in mice

Pluronic P85 enhances the efficacy of outer membrane vesicles as a subunit vaccine againstBrucella melitensischallenge in mice

Molecular and immunological characterization of the major outer membrane proteins ofBrucella

Protection and suppression of the humoral immune response in mice mediated by a monoclonal antibody against the M epitope of Brucella

Contact Info

Product

Resources

About