Identification of a Second<i>Arcanobacterium pyogenes</i>Neuraminidase and Involvement of Neuraminidase Activity in Host Cell Adhesion

Jost, B. Helen; Songer, J. Glenn; Billington, Stephen J.

doi:10.1128/iai.70.3.1106-1112.2002

Cited by 47 publications

(29 citation statements)

References 33 publications

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“…CbpA is the second A. pyogenes protein involved in adhesion that is only encoded by a subset of isolates, as the NanP neuraminidase is present in only 64.2% of strains (15). This result highlights the possibility that A. pyogenes isolates involved in different diseases may be differentially equipped with adhesins.…”

Section: Discussionmentioning

confidence: 70%

The Arcanobacterium pyogenes Collagen-Binding Protein, CbpA, Promotes Adhesion to Host Cells

et al. 2003

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Arcanobacterium pyogenes is an opportunistic pathogen associated with suppurative diseases in economically important food animals such as cattle, pigs, and turkeys. A. pyogenes adheres to host epithelial cells, and adhesion is promoted by the action of neuraminidase, which is expressed by this organism. However, a neuraminidase-deficient mutant of A. pyogenes only had a reduced ability to adhere to host epithelial cells, indicating that other factors are involved in adhesion. Far Western blotting revealed the presence of an approximately 120-kDa A. pyogenes cell wall protein that binds collagen type I. The 3.5-kb gene that encodes the 124.7-kDa CbpA protein was cloned, and sequence analysis indicated that CbpA contains a typical MSCRAMM protein domain structure. Recombinant, six-His-tagged CbpA (HIS-CbpA) was capable of binding collagen types I, II, and IV but not fibronectin. In addition, CbpA was involved in the ability of A. pyogenes to adhere to HeLa and 3T6 cells, as a cbpA knockout strain had 38.2 and 57.0% of wild-type adhesion, respectively. This defect could be complemented by providing cbpA on a multicopy plasmid. Furthermore, HIS-CbpA blocked A. pyogenes adhesion to HeLa or 3T6 cells in a dose-dependent manner. cbpA was only present in 48% of the A. pyogenes strains tested (n ‫؍‬ 75), and introduction of plasmid-encoded cbpA into a naturally cbpA-deficient strain increased the ability of this strain to bind to HeLa and 3T6 cells 2.9-and 5.7-fold, respectively. These data indicate that CbpA, a collagen-binding protein of A. pyogenes, plays a role in the adhesion of this organism to host cells.

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Section: Discussionmentioning

confidence: 70%

The Arcanobacterium pyogenes Collagen-Binding Protein, CbpA, Promotes Adhesion to Host Cells

et al. 2003

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“…A. pyogenes isolates used in this study were obtained from veterinary diagnostic laboratories or personal culture collections in North America and include 20 tetracycline-resistant isolates (7 of bovine origin, 12 of porcine origin, and 1 from a macaw) and 10 tetracycline-susceptible isolates (6 of bovine origin and 4 of porcine origin). All of these are independent isolates and likely represent different strains based on U.S. state and animal host of isolation and the presence or absence of virulence genes such as cbpA (9) and nanP (15). A. pyogenes strains (Table 1) were grown on brain heart infusion (BHI) agar (Difco), supplemented with 5% citrated bovine blood, at 38°C and 5% CO 2 in a humidified incubator.…”

Section: Methodsmentioning

confidence: 99%

Multiple Genetic Elements Carry the Tetracycline Resistance Gene tet (W) in the Animal Pathogen Arcanobacterium pyogenes

Billington

Jost

2006

Antimicrob Agents Chemother

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The tet(W) gene is associated with tetracycline resistance in a wide range of bacterial species, including obligately anaerobic rumen bacteria and isolates from the human gut and oral mucosa. However, little is known about how this gene is disseminated and the types of genetic elements it is carried on. We examined tetracycline-resistant isolates of the animal commensal and opportunistic pathogen Arcanobacterium pyogenes, all of which carried tet(W), and identified three genetic elements designated ATE-1, ATE-2, and ATE-3. These elements were found in 25%, 35%, and 60% of tetracycline-resistant isolates, respectively, with some strains carrying both ATE-2 and ATE-3. ATE-1 shows characteristics of a mobilizable transposon, and the tet(W) genes from strains carrying this element can be transferred at low frequencies between A. pyogenes strains. ATE-2 has characteristics of a simple transposon, carrying only the resistance gene and a transposase, while in ATE-3, the tet(W) gene is associated with a streptomycin resistance gene that is 100% identical at the DNA level with the aadE gene from the Campylobacter jejuni plasmid pCG8245. Both ATE-2 and ATE-3 show evidence of being carried on larger genetic elements, but conjugation to other strains was not observed under the conditions tested. ATE-1 was preferentially associated with A. pyogenes strains of bovine origin, while ATE-2 and ATE-3 elements were primarily found in porcine isolates, suggesting that these elements may circulate in different environments. In addition, four alleles of the tet(W) gene, primarily associated with different elements, were detected among A. pyogenes isolates.

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“…Economically significant disease includes liver abscessation in beef cattle, and pneumonia and arthritis in swine (Jost & Billington, 2005). A. pyogenes is armed with several factors that contribute to its pathogenesis, including a cholesterol-dependent cytolysin, pyolysin (Billington et al, 1997), several proteases (Schaufuss et al, 1989) and a number of adhesive mechanisms, including two cell-surface neuraminidases (Jost et al, 2002) and a collagen-binding protein, CbpA (Esmay et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Functional and structural properties of CbpA, a collagen-binding protein from Arcanobacterium pyogenes

et al. 2007

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Arcanobacterium pyogenes, an opportunistic pathogen of economically important food animals, is the causative agent of liver abscesses in feedlot cattle, osteomyelitis in turkeys, and pneumonia and arthritis in pigs. Previous studies identified the first A. pyogenes adhesin, CbpA, a protein located on the bacterial surface which has the ability to bind collagen and promotes adhesion to the host cells. The protein has an N-terminal ligand-binding region (region A) and a C-terminal repetitive domain (region B). In this study we found that CbpA bound to almost all the collagen types tested but not to other proteins, and it displayed a propensity to interact with several collagenous peptides derived by CNBr cleavage of type I and II collagens. The K D values of CbpA for type I and II collagens and collagen peptides determined by solid-phase binding assay and intrinsic tryptophan fluorescence were in the range of 1-15 nM. It was also found that CbpA and its A region bound fibronectin, and that collagen and fibronectin interacted with distinct subsites. Anti-CbpA antibodies were effective at inhibiting both binding of isolated CbpA and bacterial adhesion to immobilized collagen, suggesting that CbpA is a functional collagen-binding adhesin. Analysis of the immunological cross-reactivity of CbpA with antibodies against other bacterial collagen-binding proteins indicated that CbpA is immunologically related to ACE from Enterococcus faecalis but not to CNA from Staphylococcus aureus or Acm from Enterococcus faecium. Far-UV and near-UV circular dichroism spectra showed that full-length CbpA and its region A are mainly composed of b-sheet with only a minor a-helical component and that both the proteins have a well-defined tertiary structure.

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Identification of a SecondArcanobacterium pyogenesNeuraminidase and Involvement of Neuraminidase Activity in Host Cell Adhesion

Cited by 47 publications

References 33 publications

The Arcanobacterium pyogenes Collagen-Binding Protein, CbpA, Promotes Adhesion to Host Cells

The Arcanobacterium pyogenes Collagen-Binding Protein, CbpA, Promotes Adhesion to Host Cells

Multiple Genetic Elements Carry the Tetracycline Resistance Gene tet (W) in the Animal Pathogen Arcanobacterium pyogenes

Functional and structural properties of CbpA, a collagen-binding protein from Arcanobacterium pyogenes

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