Major outer membrane proteins of Pasteurella haemolytica serovars 1–15: comparison of separation techniques and surface-exposed proteins on selected serovars

Morton, Robert; Simons, K R; Confer, A W

doi:10.1016/0378-1135(96)00010-7

Cited by 19 publications

(14 citation statements)

References 15 publications

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“…OMP were isolated from B. quintana JK31 using lauryl sarcosine fractionation. This method has been used to enrich OMP from a number of bacterial species (3,31,39) and was also utilized to separate the OMP from the IMP of B. henselae (42). We initially compared the protein profiles of the subcellular fractions of B. quintana after separation by 1D SDS-PAGE, followed by Coomassie blue staining ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Proteomic and Immunoblot Analyses of Bartonella quintana Total Membrane Proteins Identify Antigens Recognized by Sera from Infected Patients

et al. 2007

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Bartonella quintana is a fastidious, gram-negative, rod-shaped bacterium that causes prolonged bacteremia in immunocompetent humans and severe infections in immunocompromised individuals. We sought to define the outer membrane subproteome of B. quintana in order to obtain insight into the biology and pathogenesis of this emerging pathogen and to identify the predominant B. quintana antigens targeted by the human immune system during infection. We isolated the total membrane proteins of B. quintana and identified 60 proteins by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis and peptide mass fingerprinting. Using the newly constructed proteome map, we then utilized two-dimensional immunoblotting with sera from 21 B. quintana-infected patients to identify 24 consistently recognized, immunoreactive B. quintana antigens that have potential relevance for pathogenesis and diagnosis. Among the outer membrane proteins, the variably expressed outer membrane protein adhesins (VompA and VompB), peptidyl-prolyl cis-trans-isomerase (PpI), and hemin-binding protein E (HbpE) were recognized most frequently by sera from patients, which is consistent with surface expression of these virulence factors during human infection.Bartonella quintana, the agent of trench fever, is a fastidious, gram-negative, rod-shaped organism that can cause prolonged bacteremia in immunocompetent humans and severe infections in immunocompromised individuals. Humans are the only known reservoir for B. quintana (12), and the vector for transmission is the human body louse, Pediculus humanus corporis (38). B. quintana infections have occurred worldwide, and severe, potentially lethal complications, such as endocarditis and bacillary angiomatosis, can develop in immunocompromised patients with AIDS, cancer, and organ transplants. However, little is known about the pathogenesis of B. quintana, and diagnosis of human infection remains extremely challenging. To address this paucity of knowledge, we sought to identify potential membrane-associated virulence factors, as well as protective and diagnostically relevant B. quintana antigens, by characterizing the total membrane fraction and immunome of B. quintana.Bacterial outer membrane proteins (OMP) can be important virulence factors, playing a critical role in adherence, invasion, and immune evasion during infection of the host, as well as during transmission via arthropod vectors. Many outer membrane-associated proteins that are important for pathogenesis also are consistent targets for the host immune system after infection. Workers in our lab previously identified a family of variably expressed outer membrane proteins (Vomp) that play a role in adhesion and autoaggregation (45). To initially identify the Vomp family, we used two-dimensional (2D) sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) to visualize changes in expression of membrane proteins in sequential isolates from animals experimentally infected with B. quintana.To identify additional membrane pr...

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Section: Resultsmentioning

confidence: 99%

Proteomic and Immunoblot Analyses of Bartonella quintana Total Membrane Proteins Identify Antigens Recognized by Sera from Infected Patients

et al. 2007

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“…Sarkosyl method of preparation of outer membrane‐enriched proteins was found to be convenient and also yielded high amount of proteins. This method was previously shown to be effective in the extraction of OMPs of P. haemolytica (Morton et al., 1996), P. multocida type A (Abdullahi et al., 1990; Confer et al., 1996; Marandi and Mittal, 1996; Dabo et al., 1997) as well as P. multocida type B (Tomer et al., 2002; Borkowska‐Opacka and Kedrak, 2003).…”

Section: Discussionmentioning

confidence: 99%

Immunization with Outer Membrane Proteins of Pasteurella multocida (6:B) Provides Protection in Mice

Basagoudanavar

Singh

Varshney

2006

Journal of Veterinary Medicine Series A

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The immunoprotective efficacy of Pasteurella multocida (6:B) outer membrane proteins (OMPs) was examined in the mouse model. Bacterial OMPs were extracted using sarkosyl method and analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and immunoblotting. Prototype vaccines were prepared using OMPs with adjuvants including dioleoyl phosphatidyl choline-based liposome and Montanide ISA206 water-in oil-in water emulsion. Antibody response to the vaccine was monitored using indirect enzyme linked immunosorbent assay. The results of the study showed that immunized mice had high titre with both the formulations. The vaccinated mice were able to survive a live virulent bacterial challenge. Based on the findings of the study it can be inferred that OMPs are important determinants of immunoprotection hence can serve as vaccine candidates against haemorrhagic septicaemia.

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“…However, recent surveys have shown that serotype A6 is increasingly prevalent in the United Kingdom [49] and in the USA [3,143] with about 30% of strains serotyped. Nevertheless, based on lipopolysaccharide profiles and outer membrane proteins within each serotype, it has been concluded that, apart from the nature of their capsules, serotypes A1 and A6 are extremely similar [39,130].…”

Section: Diversitymentioning

confidence: 99%

How Mannheimia haemolytica defeats host defence through a kiss of death mechanism

2005

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-Mannheimia haemolytica induced pneumonias are only observed in goats, sheep and cattle. The bacterium produces several virulence factors,whose principal ones are lipopolysaccharide and leukotoxin. The latter is cytotoxic only for ruminant leukocytes, a phenomenon that is correlated with its ability to bind and interact with the ruminant β2-integrin Lymphocyte Function-associated Antigen 1. This paper globally reviews all the information available on host-pathogen interactions underlying respiratory mannheimiosis (formerly pasteurellosis), from the stable and the Petri dish to the biochemical cascade of events triggered by the leukotoxin inside ruminant leukocytes. One conclusion can be made: the most widespread cattle respiratory disease with the most important impact on beef production worldwide, is probably due to a tiny ruminant-specific focal variation in the CD18-and/or CD11a-expressing genes.

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Major outer membrane proteins of Pasteurella haemolytica serovars 1–15: comparison of separation techniques and surface-exposed proteins on selected serovars

Cited by 19 publications

References 15 publications

Proteomic and Immunoblot Analyses of Bartonella quintana Total Membrane Proteins Identify Antigens Recognized by Sera from Infected Patients

Proteomic and Immunoblot Analyses of Bartonella quintana Total Membrane Proteins Identify Antigens Recognized by Sera from Infected Patients

Immunization with Outer Membrane Proteins of Pasteurella multocida (6:B) Provides Protection in Mice

How Mannheimia haemolytica defeats host defence through a kiss of death mechanism

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