Vaccination with Brucella abortus rough mutant RB51 protects BALB/c mice against virulent strains of Brucella abortus, Brucella melitensis, and Brucella ovis

Bagüés, María Pilar Jiménez de; Elzer, Philip H.; Jones, Siân; Blasco, J.M.; Enright, Frederick M.; Schurig, Gerhardt G.; Winter, A J

doi:10.1128/iai.62.11.4990-4996.1994

Cited by 88 publications

(39 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To overcome this problem two approaches are at present being considered. The first is to use live attenuated R Brucella strains, in particular the R B. abortus strain RB51 (25,40,41,51). Since they are devoid of O-PS they should not induce antibody responses against S-LPS which would be detectable by the conventional serological tests or by an ELISA using S-LPS or O-PS as antigen.…”

Section: Discussionmentioning

confidence: 99%

O-Polysaccharide Epitopic Heterogeneity at the Surface ofBrucellaspp. Studied by Enzyme-Linked Immunosorbent Assay and Flow Cytometry

Cloeckaert

Weynants

Godfroid

et al. 1998

Clin Diagn Lab Immunol

View full text Add to dashboard Cite

Smooth Brucella strains are classified into three serotypes, i.e., A+M−, A−M+, and A+M+, according to slide agglutination with A and M monospecific polyclonal sera. The epitopes involved have been located on the O-polysaccharide (O-PS) moiety of the smooth lipopolysaccharide (S-LPS), which represents the most exposed antigenic structure on the surface ofBrucella spp. By use of monoclonal antibodies (MAbs) a number of epitope specificities on the O-PS have been reported: A, M, and epitopes shared by both A and M dominant strains, which have been named common (C) epitopes. The latter have been further subdivided, according to relative MAb binding in enzyme-linked immunosorbent assays (ELISA) to A- and M-dominant Brucella strains and to cross-reacting Yersinia enterocolitica O:9, into five epitopic specificities: C (M>A), C (M=A), C/Y (M>A), C/Y (M=A), and C/Y (A>M). In the present study, we studied the occurrence of these epitopes at the surface of representatives of all Brucellaspecies and biovars including the live vaccine strains by analyzing the levels of MAb binding to whole Brucella cells in ELISA and flow cytometry assays. In ELISA, the level of MAb binding correlated well with the previously defined epitope specificity and the serotype defined by polyclonal sera for each Brucella species, biovar, or strain. However, MAbs to the C (M=A) and C (M>A) epitopes showed insignificant binding to B. suis biovar 2 strains and bound at lower titers to B. suis biovar 3 and B. neotomae than to the other Brucella strains. Some of the flow cytometry results were contradictory to those obtained by ELISA. In fact, it appeared by flow cytometry that all O-PS epitopes, including the A and M epitopes, are shared to different degrees byBrucella spp. which nevertheless show a high degree of O-PS heterogeneity according to MAb binding intensities. The subdivision of MAb specificities and Brucella serotypes was therefore less evident by flow cytometry than by ELISA. Whereas in ELISA the MAb specific for the A epitope showed insignificant binding to Y. enterocolitica O:9, this MAb bound strongly to Y. enterocolitica O:9 in flow cytometry. One of the two MAbs specific to the C (M=A) epitope also bound at a low but significant level to B. suis biovar 2 strains. However, as in ELISA the MAb specific for the C (M>A) epitope did not bind at all to B. suis biovar 2 strains in flow cytometry. Flow cytometry provided new information regarding specificity of the MAbs and may further explain some aspects of the capacity of passive protection of some MAbs against smooth Brucella infection in mice. As shown in the present study the occurrence of Brucella strains apparently completely devoid of one specific C O-PS epitope (e.g., B. suis biovar 2 devoid of the C [M>A] epitope) offers the possibility of obtaining vaccine strains devoid of a diagnostic O-PS epitope, which could further help to resolve the problem of discriminating infected from vaccinated animals that remains a major goal in brucellosis research.

show abstract

Section: Discussionmentioning

confidence: 99%

O-Polysaccharide Epitopic Heterogeneity at the Surface ofBrucellaspp. Studied by Enzyme-Linked Immunosorbent Assay and Flow Cytometry

Cloeckaert

Weynants

Godfroid

et al. 1998

Clin Diagn Lab Immunol

View full text Add to dashboard Cite

show abstract

“…Accordingly, our results emphasize the need to study the immune response elicited by infection of various animals with Brucella spp. Ab recognition of B. abortus surface proteins such as OMPs may offer some protection against brucellosis caused by S LPS-producing species (20,34). Humoral immune recognition following S Brucella infection is only partially protective, and the highest level of protection is achieved with serum plus T cells (1,2).…”

Section: Discussionmentioning

confidence: 99%

“…Resistance to infection by B. abortus requires both cellular and humoral immunity (1,2,20,34,40,41,44). Humoral immunity in brucellosis is primarily due to antibodies (Abs) which react with the O region of the lipopolysaccharide (LPS) (20,28,40); however, this is not true in all individuals (41). Also, the use of LPS as a general vaccine for brucellosis is further compromised by the fact that Brucella ovis and Brucella canis are rough (R) and therefore lack the protective O polysaccharide of the LPS (9).…”

mentioning

confidence: 99%

Cloning of a Brucella melitensis group 3 antigen gene encoding Omp28, a protein recognized by the humoral immune response during human brucellosis

et al. 1996

View full text Add to dashboard Cite

Brucella group 3 antigens (Ags) are outer membrane proteins (OMPs) with a molecular mass ranging from 25 to 30 kDa. The OMPs are of interest partially because of their potential use as vaccine and diagnostic reagents. We used human convalescent antibody (Ab) to clone a gene that encoded a 28-kDa protein from a gt11 library of Brucella melitensis 16M genomic DNA. DNA sequence analysis revealed a single open reading frame that would encode a protein of 26,552 Da. The 28-kDa protein had a primary amino acid sequence that was 43% similar to a previously described Brucella abortus group 3 Ag, Omp25 (P. de Wergifosse, P. Lintermans,

show abstract

“…The predominant mechanism by which WR201 induces immunity is unknown. Studies by a number of investigators (1,3,14,18,23,24,35,38) have shown that the adoptive transfer of immune CD4, CD8, or mixed T cells and the passive transfer of the anti-OPS antibody from immunized mice to naive animals all mediate an antibacterial effect in animals challenged with strains that express OPS. Our demonstration of WR201induced antibacterial immunity against intraperitoneal challenge is consistent with our finding that immunization with this live, attenuated, strain induces both humoral (anti-OPS and antiprotein antibody) and cellular (production of IL-2 and IFN-␥) immune responses.…”

Section: Discussionmentioning

confidence: 99%

Protection of Mice against Brucellosis by Vaccination withBrucella melitensisWR201(16MΔpurEK)

Hoover

Crawford²,

Verg

et al. 1999

Infect Immun

View full text Add to dashboard Cite

Human brucellosis can be acquired from infected animal tissues by ingestion, inhalation, or contamination of the conjunctiva or traumatized skin by infected animal products. A vaccine to protect humans from occupational exposure or from zoonotic infection in areas where the disease is endemic would reduce an important cause of morbidity worldwide. Vaccines currently used in animals are unsuitable for human use. We tested a live, attenuated, purine-auxotrophic mutant strain of Brucella melitensis, WR201, for its ability to elicit cellular and humoral immune responses and to protect mice against intranasal challenge with B. melitensis 16M. Mice inoculated intraperitoneally with WR201 made serum antibody to lipopolysaccharide and non-O-polysaccharide antigens. Splenocytes from immunized animals released interleukin-2 (IL-2), gamma interferon, and IL-10 when cultured with Brucella antigens. Immunization led to protection from disseminated infection but had only a slight effect on clearance of the challenge inoculum from the lungs. These studies suggest that WR201 should be further investigated as a vaccine to prevent human brucellosis.

show abstract

Vaccination with Brucella abortus rough mutant RB51 protects BALB/c mice against virulent strains of Brucella abortus, Brucella melitensis, and Brucella ovis

Cited by 88 publications

References 35 publications

O-Polysaccharide Epitopic Heterogeneity at the Surface ofBrucellaspp. Studied by Enzyme-Linked Immunosorbent Assay and Flow Cytometry

O-Polysaccharide Epitopic Heterogeneity at the Surface ofBrucellaspp. Studied by Enzyme-Linked Immunosorbent Assay and Flow Cytometry

Cloning of a Brucella melitensis group 3 antigen gene encoding Omp28, a protein recognized by the humoral immune response during human brucellosis

Protection of Mice against Brucellosis by Vaccination withBrucella melitensisWR201(16MΔpurEK)

Contact Info

Product

Resources

About