Antigenic characterization of the P6 protein of nontypable Haemophilus influenzae

Murphy, Timothy F.; Bartos, L C; Campagnari, Anthony A.; Nelson, Michael; Apicella, Michael A.

doi:10.1128/iai.54.3.774-779.1986

Cited by 89 publications

(77 citation statements)

References 19 publications

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“…They employed shearing of whole cells to remove the OMs. Baeteroides intermedius OMs possessed a 20 kD protein similar to the ompH protein of Pseudomottas aertigitiosa (26), and Haemophihis ittfhiertzctc (31). High molecular weight (120 to 130 kD) OMPs were also observed in these B. intermedius OMs.…”

Section: Discussionmentioning

confidence: 92%

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Comparative studies of the outer membranes of Bacteroides gingivalis, strains ATCC 33277, W50, W83,381

Kennell

Holt

1990

Oral Microbiology and Immunology

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Outer membrane fractions from Bacteroides gingivalis strains ATCC 33277, 381, W50, and W83 were isolated by French pressure cell disruption and the distribution of major and minor proteins was determined by SDS-PAGE electrophoresis after treatment with 2% Sarkosyl and 2% Triton X-100. Heat-modifiability of the outer membrane proteins (OMPs) from these B. gingivalis strains was also determined after treatment at 100 degrees C and analysis by both 1- and 2-dimensional SDS-PAGE. The distribution of the OMPs on the surface of these B. gingivalis strains was determined by 125I labelling. For the most part of the OMPs of B. gingivalis presented a complex distribution, with OMPs observed between 123 kD and 13 kD. While the distribution of the OMPs was strain specific, OMPs common to all of the strains were observed. Two percent Sarkosyl treatment of the OMs at room temperature resulted in the solubilization of approximately 60% of the OMP. The Sarkosyl-insoluble MOMPs had relative molecular weights between 110 kD and 20 kD. Many of the OMPs which were separated at room temperature were heat-modified at either 65 degrees C or 100 degrees C. Heating of the OMs at 100 degrees C resulted in the heat modification of the majority of those OMPs observed at room temperature. Sarkosyl-100 degrees C OMs displayed MOMPs at apparent molecular weights between 90 kD and 15 kD. Radioiodination of the B. gingivalis strains ATCC 33277, 381, W83 and W50 revealed between 7 and 14 MOMPs at the cell surface depending upon the strain. The complexity of the OM of these B. gingivalis strains indicated the possibility of identifying and separating those OMPs involved in a variety of biological functions, including virulence, transport, and cell interaction.

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Section: Discussionmentioning

confidence: 92%

“…4, Lane 2). A total of 10 MOMPs were observed after heating at 65''C with relative molecular weights of 46,42,37,35,31,30,27,24,20, and 18 kD. At lOO^C (Fig.…”

Section: Resultsmentioning

confidence: 99%

Comparative studies of the outer membranes of Bacteroides gingivalis, strains ATCC 33277, W50, W83,381

Kennell

Holt

1990

Oral Microbiology and Immunology

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“…This indicated that even stnall amounts of these proteins (24 and 16.5 kDa) were sufficient to produce a strong immunologie reaction, and that the 24 kDa protein seemed to be a particularly potent antigen. It is interesting that a 16.6 kDa OMP, referred to as P6, has been identified so far in all examined strains of Haemophilus itrflttenzae (14), an important pathogen in both adults and ehildren. P6, being a target for baeterieidal antibodies, may be an itnportant surfaee antigen with regard to host immunity and vaccine development towards this organistn.…”

Section: Discussionmentioning

confidence: 99%

“…They have many important functions, serving as phage receptors (6), diffusion pores, proteases, mitogens (7) or taking part in conjugation (26). Due to their itntnunogenicity sotne OMP may be possible candidates for itnmunotherapy (3,14). Although sotne attention has been paid to OMP of some strains of A. aeiinomyeeiemeomiians and H. aphrophiltis (8), mostly protein profiles of whole bacterial cell extracts have been studied (29).…”

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confidence: 99%

Outer membrane proteins of Actinobacillus actinomycetemcomitans and Haemophilus aphrophilus studied by SDS‐PAGE and immunoblotting

Bolstad¹,

Kristoffersen²,

Olsen³

et al. 1990

Oral Microbiology and Immunology

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This investigation characterized and compared outer membrane proteins (OMP) of the closely related Actinobacillus actinomycetemcomitans and Haemophilus aphrophilus by means of SDS-PAGE patterns and reactions on immunoblots with rabbit antiserum against A. actinomycetemcomitans FDC Y4. Reactions with serum from a patient with Papillon Lefévre syndrome (PLS), from whom periodontal wild strains of A. actinomycetemcomitans had been isolated, were also studied. OMP were purified with selective solubilization from lyophilized cells of 10 wild and 4 reference strains of A. actinomycetemcomitans and 4 reference strains of H. aphrophilus. OMP profiles from wild and reference strains of A. actinomycetemcomitans were similar while those from A. actinomycetemcomitans and H. aphrophilus differed. The most prominent difference was absence of a heat modifiable protein in H. aphrophilus strains. Immunoblotting revealed strong common antigens in most strains, including a heat modifiable protein with mol wt 34 kDa, as well as a 29 kDa and a 16.5 kDa protein. Treatment with pronase and sodium periodate confirmed the protein nature of the major OMP antigens.

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“…The 40-kDa protein of F. nucleatum shares sequences with the OmpA protein of Escherichia coli [5]. Brucella abortus strains share antigens among OMPs of porin nature that appear to be species wide [30] and in Haernophilus influenzae an OMP antigen has been shown to be antigenically preserved among strains [31].…”

Section: -6-mentioning

confidence: 99%

Outer membrane proteins as major antigens of Fusobacterium nucleatum

Bakken

Aarø

Hofstad

et al. 1989

FEMS Microbiology Letters

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The immunochemical reactions of rabbit polyclonal antibodies directed to different preparations of Fusobacterium nucleatum i.e, whole cells, peptidoglycan associated proteins, a peptidoglycan‐protein complex and a purified 40 kiloDalton (kDa) protein, were investigated on outer membrane preparations of Fusobacterium species and a restricted number of Leptotrichia buccalis after their separation on sodium dodecyl sulphate polyacrylamide gels and electrotransfer to nitrocellulose. All F. nucleatum strains had identical reaction patterns with the immune sera tested. Surface exposed parts of a restricted number of proteins with apparent molecular weights at 70 kDa (a doublet band), 60 kDa, 55 kDa and 40 kDa seemed to be major immunogens. Antigenic related proteins either of identical or slightly deviating electrophoretic mobilities to the 40‐kDa protein were observed with the other members of Bacteroidaceae tested. The characteristic 70‐kDa protein doublet seemed to be restricted to F. nucleatum although single protein bands of near identical molecular weights belonging to the other species tested also reacted. The data also indicate that the 60‐kDa and 55‐kDa polypeptides might be present in other species of Fusobacterium.

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Antigenic characterization of the P6 protein of nontypable Haemophilus influenzae

Cited by 89 publications

References 19 publications

Comparative studies of the outer membranes of Bacteroides gingivalis, strains ATCC 33277, W50, W83,381

Comparative studies of the outer membranes of Bacteroides gingivalis, strains ATCC 33277, W50, W83,381

Outer membrane proteins of Actinobacillus actinomycetemcomitans and Haemophilus aphrophilus studied by SDS‐PAGE and immunoblotting

Outer membrane proteins as major antigens of Fusobacterium nucleatum

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