Immunization of pigs against Actinobacillus pleuropneumoniae with two recombinant protein preparations

Rossi-Campos, A.; Anderson, Carol; Gerlach, Gerald-F.; Klashinsky, S; Potter, Andrew; Willson, Philip

doi:10.1016/0264-410x(92)90349-o

Cited by 107 publications

(79 citation statements)

References 25 publications

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“…The primary sequence of both gonococcal and meningococcal (22) (38). Much remains to be done to assess the localization and surface accessibility of Thp2.…”

Section: Discussionmentioning

confidence: 99%

Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization

1994

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“…The primary sequence of both gonococcal and meningococcal (22) (38). Much remains to be done to assess the localization and surface accessibility of Thp2.…”

Section: Discussionmentioning

confidence: 99%

Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization

1994

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“…Indeed, for N. meningitidis, H. infwqae and A . pleuropnezmoniae, several groups have shown that vaccination with Tbpl, Tbp2, or both, can protect experimental animals from infection following challenge with the live homologous organism (Danve e t al., 1993;Gorringe et al, 1995 ;Lissolo et al, 1995 ;Loosmore e t al., 1996;Rossi Campos et al, 1992). Further progress in this field will undoubtedly rely on a more detailed understanding of the antigenic domains within these ironregulated outer-membrane proteins.…”

Section: Discussionmentioning

confidence: 99%

Conservation and antigenic cross-reactivity of the transferrin-binding proteins of Haemophilus influenzae, Actinobacillus pleuropneumoniae and Neisseria meningitidis

et al. 1996

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Haemophilus influenzae acquires iron from the iron-transporting glycoprotein transferrin via a receptor-mediated process. This involves two outer-membrane transferrin-binding proteins (Tbps) termed T b p l and Tbp2 which show considerable preference for the human form of transferrin. Since the Tbps are attracting considerable attention as potential vaccine components, we used transferrin affinity chromatography to examine their conservation amongst 28 H. influenzae type b strains belonging to different outer-membrane-protein subtypes as well as six non-typable strains. Whole cells of all type b and nontypable strains examined bound human transferrin; whilst most strains possessed a T b p l of approximately 105 kDa, the molecular mass of Tbp2 varied from 79 to 94 kDa. Antisera raised against affinity-purified native H. influenzae TbpllTbp2 receptor complex cross-reacted on Western blots with the respective Tbps of all the Haemophilus strains examined. When used to probe Neisseria meningitidis Tbps, sera from each of four mice immunized with the Haemophilus TbplR complex recognized the 68 kDa Tbp2 of N. meningitidis strain B16B6 but not the 78 kDa Tbp2 of N. meningitidis strain 70942. Serum from one mouse also reacted weakly with T b p l of strain B16B6. Apart from a weak reaction with the Tbp2 of a serotype 5 strain, this mouse antiserum failed to recognize the Tbps of the porcine pathogen A. pleuropneumoniae. However, a monospecif ic polyclonal antiserum raised against the denatured Tbp2 of Neisseria meningitidis B16B6 recognized the Tbps of all Haemophilus and Actinobacillus strains examined. Since H. influenzae forms part of the natural flora of the upper respiratory tract, human sera were screened for the presence of antibodies to the Tbps. Sera from healthy adults contained antibodies which recognized both T b p l and Tbp2 from H. influenzae but not N. meningitidis. Convalescent sera from meningococcal meningitis patients contained antibodies which, on Western blots, recognized the Tbps2s of both pathogens. These data demonstrate the existence of shared epitopes on the Tbps of H. influenre, N. meningitidis and A. pleuropneumoniae despite their transferrin species specificity.

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“…One vaccine strategy that has been adopted in several other bacterial species in the Pasteurellaceae is to target the surface proteins involved in acquisition of iron in the host as vaccine antigens (20,26,30). The rationale for targeting these antigens is that they are essential for overcoming the iron restriction imposed by the host iron binding protein transferrin (Tf) and are accessible at the cell surface.…”

mentioning

confidence: 99%

“…This protein ranges in size from 60 to 90 kDa in different strains and species (15). Experimental studies support the use of TbpBs as a vaccine antigen (20,26,30). TbpA is an integral, TonB-dependent OMP proposed to mediate transport of iron across the outer membrane (32).…”

mentioning

confidence: 99%

Characterization of a Novel Transferrin Receptor in Bovine Strains of Pasteurella multocida

Ogunnariwo

Schryvers

2001

J Bacteriol

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Analysis of bovine respiratory isolates of Pasteurella multocida demonstrated that six of nine strains tested were capable of growth dependent upon bovine transferrin and of specifically binding ruminant transferrins. A single 82-kDa protein was affinity isolated from the P. multocida strains with immobilized bovine transferrin.In contrast to what has been observed in other species, binding of this protein to immobilized transferrin was specifically blocked by the N-lobe subfragment of bovine transferrin. A single gene encoding the 82-kDa protein was flanked by a leucyl-tRNA synthetase gene and an IS1060 element, in contrast to other species where genes encoding the two receptor proteins (TbpB and TbpA) are found in an operonic arrangement. A similar gene arrangement was observed in all of the receptor-positive strains, in spite of the observation that they belonged to different genomic groups. Analysis of the deduced amino acid sequence of the receptor protein indicated that it is a member of the TonB-dependent outer membrane receptor family, and although it is related to transferrin and lactoferrin receptor proteins (TbpAs and LbpAs) from other species, it differs substantially from other members of this group. Amino acid alignments suggest that the reduced size (20 kDa smaller) of the P. multocida TbpA is primarily due to the absence of larger predicted external loops. Collectively these results suggest that P. multocida has a single, novel receptor protein (TbpA) that is capable of efficiently mediating iron acquisition from bovine transferrin without the involvement of a second receptor protein (TbpB).

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Immunization of pigs against Actinobacillus pleuropneumoniae with two recombinant protein preparations

Cited by 107 publications

References 25 publications

Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization

Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization

Conservation and antigenic cross-reactivity of the transferrin-binding proteins of Haemophilus influenzae, Actinobacillus pleuropneumoniae and Neisseria meningitidis

Characterization of a Novel Transferrin Receptor in Bovine Strains of Pasteurella multocida

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