Proteomic analysis of a meningococcal outer membrane vesicle vaccine prepared from the group B strain NZ98/254

Vipond, Caroline; Suker, Janet; Jones, Christopher; Tang, Christoph M.; Feavers, Ian M.; Wheeler, Jun X.

doi:10.1002/pmic.200500821

Cited by 101 publications

(52 citation statements)

References 74 publications

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“…The inactivated BVD vaccine A contained over 3.5 fold more proteins than the live-attenuated vaccine B and still over twice as many compared to a meningococcal vaccine , where 47 proteins were identified by similar proteomic approaches [22]. Total protein quantity of vaccine A and MDBK cells was almost equal, underlining our findings that the protein content of vaccine A and the host cell line surface resemble each other (Figure 1C and D).…”

Section: Discussionsupporting

confidence: 58%

Bovine neonatal pancytopenia - Comparative proteomic characterization of two BVD vaccines and the producer cell surface proteome (MDBK)

Euler¹,

Hauck

Ueffing

et al. 2013

BMC Vet Res

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BackgroundBovine neonatal pancytopenia (BNP) is a disease syndrome in newborn calves of up to four weeks of age, first observed in southern Germany in 2006. By now, cases have been reported in several countries around the globe. Many affected calves die within days due to multiple haemorrhages, thrombocytopenia, leukocytopenia and bone marrow depletion. A certain vaccine directed against Bovine Virus Diarrhoea Virus (BVDV) was recently shown to be associated with BNP pathogenesis. Immunized cows develop alloantibodies that are transferred to newborn calves via colostrum intake. In order to further elucidate BNP pathogenesis, the purpose of this study was to characterize and compare the protein composition of the associated vaccine to another vaccine directed against BVDV not related to BNP and the cell surface proteome of MDBK (Madin-Darby Bovine Kidney) cells, the cell line used for production of the associated vaccine.ResultsBy SDS-PAGE and mass spectrometry, we were able to detect several coagulation-related and immune modulatory proteins, as well as cellular and serum derived molecules being shared between the associated vaccine and MDBK cells. Furthermore, the number of proteins identified in the BNP related vaccine was almost as high as the number of surface proteins detected on MDBK cells and exceeded the amount of proteins identified in the non-BNP related vaccine over 3.5 fold. The great amount of shared cellular and serum derived proteins confirm that the BNP associated vaccine contained many molecules originating from MDBK cells and vaccine production.ConclusionsThe respective vaccine was not purified enough to prevent the development of alloantibodies. To narrow down possible candidate proteins, those most likely to represent a trigger for BNP pathogenesis are presented in this study, giving a fundament for further analysis in future research.

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Section: Discussionsupporting

confidence: 58%

Bovine neonatal pancytopenia - Comparative proteomic characterization of two BVD vaccines and the producer cell surface proteome (MDBK)

Euler¹,

Hauck

Ueffing

et al. 2013

BMC Vet Res

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“…EF-Tu was found in OM fractions of A. baumannii [24]. It also was present in OMVs of N. meningitides [38, 39] and E. coli [40]. However, a former proteomic analysis did not detect EF-Tu in the A. baumannii OMV fraction [25].…”

Section: Discussionmentioning

confidence: 99%

Association ofAcinetobacter baumanniiEF-Tu with Cell Surface, Outer Membrane Vesicles, and Fibronectin

Dallo

Zhang

Denno

et al. 2012

The Scientific World Journal

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A conundrum has long lingered over association of cytosol elongation factor Tu (EF-Tu) with bacterial surface. Here we investigated it with Acinetobacter baumannii, an emerging opportunistic pathogen associated with a wide spectrum of infectious diseases. The gene for A. baumannii EF-Tu was sequenced, and recombinant EF-Tu was purified for antibody development. EF-Tu on the bacterial surface and the outer membrane vesicles (OMVs) was revealed by immune electron microscopy, and its presence in the outer membrane (OM) and the OMV subproteomes was verified by Western blotting with the EF-Tu antibodies and confirmed by proteomic analyses. EF-Tu in the OM and the OMV subproteomes bound to fibronectin as detected by Western blot and confirmed by a label-free real-time optical sensor. The sensor that originates from photonic crystal structure in a total-Internal-reflection (PC-TIR) configuration was functionalized with fibronectin for characterizing EF-Tu binding. Altogether, with a novel combination of immunological, proteomical, and biophysical assays, these results suggest association of A. baumannii EF-Tu with the bacterial cell surface, OMVs, and fibronectin.

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“…26 Furthermore, proteome analysis has demonstrated that EF-Tu is an immunogen that elicits antibody response during infection by several bacteria. 30,32,33 …”

Section: Introductionmentioning

confidence: 99%

Borrelia burgdorferielongation factor EF-Tu is an immunogenic protein during Lyme borreliosis

Carrasco

Yang

Troxell

et al. 2015

Emerging Microbes & Infections

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Borrelia burgdorferi, the etiological agent of Lyme disease, does not produce lipopolysaccharide but expresses a large number of lipoproteins on its cell surface. These outer membrane lipoproteins are highly immunogenic and have been used for serodiagnosis of Lyme disease. Recent studies have shown that highly conserved cytosolic proteins such as enolase and elongation factor Tu (EF-Tu) unexpectedly localized on the surface of bacteria including B. burgdorferi, and surface-localized enolase has shown to contribute to the enzootic cycle of B. burgdorferi. In this study, we studied the immunogenicity, surface localization, and function of B. burgdorferi EF-Tu. We found that EF-Tu is highly immunogenic in mice, and EF-Tu antibodies were readily detected in Lyme disease patients. On the other hand, active immunization studies showed that EF-Tu antibodies did not protect mice from infection when challenged with B. burgdorferi via either needle inoculation or tick bites. Borrelial mouse-tick cycle studies showed that EF-Tu antibodies also did not block B. burgdorferi migration and survival in ticks. Consistent with these findings, we found that EF-Tu primarily localizes in the protoplasmic cylinder of spirochetes and is not on the surface of B. burgdorferi. Taken together, our studies suggest that B. burgdorferi EF-Tu is not surfaced exposed, but it is highly immunogenic and is a potential serodiagnostic marker for Lyme borreliosis.

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Proteomic analysis of a meningococcal outer membrane vesicle vaccine prepared from the group B strain NZ98/254

Cited by 101 publications

References 74 publications

Bovine neonatal pancytopenia - Comparative proteomic characterization of two BVD vaccines and the producer cell surface proteome (MDBK)

Bovine neonatal pancytopenia - Comparative proteomic characterization of two BVD vaccines and the producer cell surface proteome (MDBK)

Association ofAcinetobacter baumanniiEF-Tu with Cell Surface, Outer Membrane Vesicles, and Fibronectin

Borrelia burgdorferielongation factor EF-Tu is an immunogenic protein during Lyme borreliosis

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