Expression of a modified Mannheimia haemolytica GS60 outer membrane lipoprotein in transgenic alfalfa for the development of an edible vaccine against bovine pneumonic pasteurellosis

Lee, Raymond W.H.; Cornelisse, Mette; Ziauddin, A.; Slack, Penelope J.; Hodgins, Douglas C.; Strommer, Judith; Shewen, Patricia E.; Lo, Reggie Y.C.

doi:10.1016/j.jbiotec.2008.03.006

Cited by 28 publications

(18 citation statements)

References 34 publications

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“…Pandher and Murphy 57 cloned and sequenced a 38‐kDa surface‐exposed outer membrane lipoprotein that is in low concentration in the outer membrane of M. haemolytica S1 and did not appear to have immunological significance. Lee et al 58 recently demonstrated high antibodies against the GS60 outer membrane lipoprotein in calves vaccinated with a commercial M. haemolytica vaccine. Potter et al 59 identified two iron‐regulated OMPs as transferrin‐binding proteins A and B. Vaccination of cattle with those iron‐regulated OMPs enhanced resistance against experimental challenge.…”

Section: Resultsmentioning

confidence: 99%

Immunoproteomic analyses of outer membrane proteins ofMannheimia haemolyticaand identification of potential vaccine candidates

et al. 2010

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Immunoproteomic analyses were used to characterize the outer membrane proteome of Mannheimia haemolytica, formerly Pasteurella haemolytica, serotype 1, and determine potential vaccine candidate proteins. 2-DE of M. haemolytica outer membranes was followed by immunoblot analyses using naïve and convalescent bovine sera. Proteins were identified using MALDI-TOF and LC-MS/MS. Spectral data was used to mine M. haemolytica protein database and 132 immunoreactive proteins were identified. Bioinformatic analysis using PSORTb, SubLoc, LipoP, BOMP, MCMBB, and TMB-Hunt/BBTM to predict subcellular localization of immunoreactive proteins and beta-barrels narrowed the list down to 55 candidates. Functional characterization of 55 proteins predicted 16 (29%) are involved in cell structure, 13 (23.6%) in transport/virulence, ten (18.2%) as unknown, six (10.9%) in general metabolism, four (7.27%) in cell process, two (3.64%) in translation, and one (1.8%) each in DNA replication, regulation, transcription, and virulence. Prediction of beta-barrel formation was between 11 and 31 immunoreactive proteins depending on the bioinformatic tool employed. Some of these proteins have potentials to be developed into stand-alone vaccines or components of vaccines. Of those proteins, several have already been characterized. Finally, although characteristics of many of M. haemolytica immunoreactive proteins identified in this study were obtained from published data and predictions using bioinformatics tools, five proteins previously listed in the published M. haemolytica sequence as unidentified were found to have correlates with functional proteins in other bacterial species.

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Section: Resultsmentioning

confidence: 99%

Immunoproteomic analyses of outer membrane proteins ofMannheimia haemolyticaand identification of potential vaccine candidates

et al. 2010

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“…The incorporation of iron-regulated proteins into a vaccine was shown to enhance protection against experimental pasteurellosis in lambs (34). An edible vaccine that expresses a fragment of the outer membrane antigen GS60 has also been developed (46). Immune sera from cattle vaccinated with live or killed M. haemolytica cells (50), and immune sera from naturally infected cattle (81), contain antibodies that recognize OmpA.…”

Section: Discussionmentioning

confidence: 99%

Outer Membrane Protein A of Bovine and Ovine Isolates of Mannheimia haemolytica Is Surface Exposed and Contains Host Species-Specific Epitopes

et al. 2011

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Mannheimia haemolytica is the etiological agent of pneumonic pasteurellosis of cattle and sheep; two different OmpA subclasses, OmpA1 and OmpA2, are associated with bovine and ovine isolates, respectively. These proteins differ at the distal ends of four external loops, are involved in adherence, and are likely to play important roles in host adaptation. M. haemolytica is surrounded by a polysaccharide capsule, and the degree of OmpA surface exposure is unknown. To investigate surface exposure and immune specificity of OmpA among bovine and ovine M. haemolytica isolates, recombinant proteins representing the transmembrane domain of OmpA from a bovine serotype A1 isolate (rOmpA1) and an ovine serotype A2 isolate (rOmpA2) were overexpressed, purified, and used to generate anti-rOmpA1 and anti-rOmpA2 antibodies, respectively. Immunogold electron microscopy and immunofluorescence techniques demonstrated that OmpA1 and OmpA2 are surface exposed, and are not masked by the polysaccharide capsule, in a selection of M. haemolytica isolates of various serotypes and grown under different growth conditions. To explore epitope specificity, anti-rOmpA1 and anti-rOmpA2 antibodies were cross-absorbed with the heterologous isolate to remove cross-reacting antibodies. These cross-absorbed antibodies were highly specific and recognized only the OmpA protein of the homologous isolate in Western blot assays. A wider examination of the binding specificities of these antibodies for M. haemolytica isolates representing different OmpA subclasses revealed that cross-absorbed anti-rOmpA1 antibodies recognized OmpA1-type proteins but not OmpA2-type proteins; conversely, cross-absorbed antirOmpA2 antibodies recognized OmpA2-type proteins but not OmpA1-type proteins. Our results demonstrate that OmpA1 and OmpA2 are surface exposed and could potentially bind to different receptors in cattle and sheep.

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“…The four proteins belong to porin (OmpU), lipoprotein (VA1061), iron-regulated protein (VPA1435) and transport protein (VPA0860). The immune protection of porins, lipoproteins, iron-regulated proteins, transport proteins has been reported in bacteria including porins V. alginolyticus OmpW [19], and P. aeruginosa OmpF [14,15], Neisseria lactamica PorB [13], lipoproteins Mannheimia haemolytica GS60 [20], and Neisseria meningitidis serogroup B NMB0928 [21], transport proteins E. coli Hma [22], iron-regulated OM proteins V. parahaemolyticus PsuA and PvuA [23], Salmonella Enteritidis IroN [24]. In the present study, we cannot conclude that more protective immunogens could be identified from these OM proteins in response to NaCl and iron than others, but our approach is efficient in the screen and identification of vaccine candidates since 40% immune protective immunogens were identified.…”

Section: Discussionmentioning

confidence: 99%

Identification of vaccine candidates from differentially expressed outer membrane proteins of Vibrio alginolyticus in response to NaCl and iron limitation

Xiong

Zhang

Yang

et al. 2010

Fish & Shellfish Immunology

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Expression of a modified Mannheimia haemolytica GS60 outer membrane lipoprotein in transgenic alfalfa for the development of an edible vaccine against bovine pneumonic pasteurellosis

Cited by 28 publications

References 34 publications

Immunoproteomic analyses of outer membrane proteins ofMannheimia haemolyticaand identification of potential vaccine candidates

Immunoproteomic analyses of outer membrane proteins ofMannheimia haemolyticaand identification of potential vaccine candidates

Outer Membrane Protein A of Bovine and Ovine Isolates of Mannheimia haemolytica Is Surface Exposed and Contains Host Species-Specific Epitopes

Identification of vaccine candidates from differentially expressed outer membrane proteins of Vibrio alginolyticus in response to NaCl and iron limitation

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