Characterization of thePasteurella haemolyticatransferrin receptor genes and the recombinant receptor proteins

Ogunnariwo, J.; Woo, Tricia; Lo, Reggie Y.C.; Gonzalez, Guido C.; Schryvers, Anthony B.

doi:10.1006/mpat.1997.0156

Cited by 42 publications

(37 citation statements)

References 33 publications

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“…Our prior experience with isolating receptor proteins from M. haemolytica demonstrated that the conditions could affect whether one or two receptor proteins were identified (22,24). Thus, we attempted to isolate receptor proteins from the receptor-positive strains of P. multocida using different condi- tions for growth and affinity isolation, including an alternate affinity isolation procedure which entailed prebinding biotinylated bTf and isolating the receptor ligand complex with immobilized streptavidin (31).…”

Section: Resultsmentioning

confidence: 99%

“…N-terminal amino acid analysis was performed as previously described (24). Essentially, samples of affinity-purified Tbp from P. multocida strain h48 were subjected to SDS-PAGE in duplicate.…”

Section: Methodsmentioning

confidence: 99%

“…The genes encoding TbpA and TbpB (tbpA and tbpB) are in an operonic arrangement, with tbpB preceding tbpA and putative regulatory and promoter sequences upstream of the tbpB gene (13,14,24). TbpB is a largely surface-exposed lipoprotein, capable of independently binding Tf and participating in the iron acquisition process, but it is not absolutely essential for iron acquisition in vitro (14).…”

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confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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

Ogunnariwo

Schryvers

2001

J Bacteriol

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“…96 Several of these proteins are iron-regulated outer membrane proteins, such as Tbp 1 and Tbp 2, and are physiologically and pathologically relevant because they are in involved in iron acquisition. 93 Because M haemolytica does not produce siderophores, expression of these iron-regulated outer membrane proteins is the main mechanism of iron acquisition. 62,93 Furthermore, Iovane et al 57 demonstrated that outer membrane proteins are chemotactic agents for neutrophils and inhibit their phagocytic and subsequent bacterial-killing mechanisms, thus favoring bacterial pulmonary colonization.…”

Section: Capsulementioning

confidence: 99%

Mannheimia haemolytica

2010

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Mannheimia haemolytica serotype S1 is considered the predominant cause of bovine pneumonic pasteurellosis, or shipping fever. Various virulence factors allow M haemolytica to colonize the lungs and establish infection. These virulence factors include leukotoxin (LKT), lipopolysaccharide, adhesins, capsule, outer membrane proteins, and various proteases. The effects of LKT are species specific for ruminants, which stem from its unique interaction with the bovine b2 integrin receptor present on leukocytes. At low concentration, LKT can activate bovine leukocytes to undergo respiratory burst and degranulation and stimulate cytokine release from macrophages and histamine release from mast cells. At higher concentration, LKT induces formation of transmembrane pores and subsequent oncotic cell necrosis. The interaction of LKT with leukocytes is followed by activation of these leukocytes to undergo oxidative burst and release proinflammatory cytokines such as interleukins 1, 6, and 8 and tumor necrosis factor a. Tumor necrosis factor a and other proinflammatory cytokines contribute to the accumulation of leukocytes in the lung. Formation of transmembrane pores and subsequent cytolysis of activated leukocytes possibly cause leakage of products of respiratory burst and other inflammatory mediators into the surrounding pulmonary parenchyma and so give rise to fibrinous and necrotizing lobar pneumonia. The effects of LKT are enhanced by lipopolysaccharide, which is associated with the release of proinflammatory cytokines from the leukocytes, activation of complement and coagulation cascade, and cell cytolysis. Similarly, adhesins, capsule, outer membrane proteins, and proteases assist in pulmonary colonization, evasion of immune response, and establishment of the infection. This review focuses on the roles of these virulence factors in the pathogenesis of shipping fever.

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“…They are subunits of the species-specific transferrin receptor. Genes for these proteins have been cloned, sequenced, and expressed in E. coli cells (Ogunnariwo et al 1997). The role of TbpA and TbpB in inducing protection of calves against experimental M. haemolytica infection has been documented by Potter et al (1999).…”

Section: Discussionmentioning

confidence: 99%

An electrophoretic characterization of iron-transporting proteins in Mannheimia haemolytica A1

Puchalski¹,

Urban‐Chmiel²,

Dec³

et al. 2013

Polish Journal of Veterinary Sciences

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Iron-regulated outer membrane proteins (IROMPs) in Mannheimia haemolytica A1, which function as a receptor for complexes containing iron ions, are induced by iron deficiency in the growth environment of the bacteria. Densitometric analysis of SDS-PAGE separation showed expression of IROMPs of 71, 77, and 100 kDa in the case of bacteria grown in a medium with 2,2-dipyridyl. The electrophoregrams obtained in 2-DE separations confirmed the presence of protein fractions with these molecular weights and isoelectric points ranging from 5.4 to 6.4. The results of the study also confirmed the ability of M. haemolytica A1 proteins involved in iron uptake to induce a protective immune response. In Western blot with serum from convalescent calves naturally infected with M. haemolytica A1, distinct reactions were obtained for IROMPs of 71, 77, and 100 kDa.

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Characterization of thePasteurella haemolyticatransferrin receptor genes and the recombinant receptor proteins

Cited by 42 publications

References 33 publications

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

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

Mannheimia haemolytica

An electrophoretic characterization of iron-transporting proteins in Mannheimia haemolytica A1

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