Binding of fibronectin, fibrinogen and type II collagen to streptococci isolated from bovine mastitis

Mamo, Wubshet; Fröman, Gunnar; Sundås, Annika; Wadström, Torkel

doi:10.1016/0882-4010(87)90048-9

Cited by 34 publications

(25 citation statements)

References 21 publications

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“…Streptococcus dysgalactiae, a group C streptococcus, is like S. aureus, frequently associated with bovine mastitis (Watts, 1988). Most strains of S. dysgalactiae bind Fn and a dissociation constant of 26 nM was determined for binding of the 29-kDa NH,-terminal fragment of Fn to strain S2 (Mamo et al, 1987). We previously reported (Lindgren et al, 1992) the cloning of two different genes encoding Fn-binding proteins from S. dysgalactiae S2.…”

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Two different genes coding for fibronectin‐binding proteins from Streptococcus dysgalactiae

Lindgren

McGavin

Signäs

et al. 1993

European Journal of Biochemistry

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The binding of Streptococcus dysgalactiae to fibronectin involves fibronetcin-binding protein(s) present on the bacterial surface. Previously, we reported the cloning of two different genes coding for cell-wall-associated fibronectin-binding proteins from S. dysgalactiae strain S2 [Lindgren, P.-E., Speziale, P., McGavin, M. J., Monstein, H.-J., Hook, M., Visai, L., Kostiainen, T., Bozzini, S. & Lindberg, M. (1992) J. Biol. Chem. 267, 1924-19311. The two genes, fibA and fnbB, have now been sequenced and the primary amino acid sequences of the two fibronectin-binding proteins, FnBA and FnBB, have been deduced. The two proteins have predicted molecular masses of 117 kDa and 122 kDa, respectively, and are organized in a similar way. The fibronectin-binding activities are localized in repeated motifs, 32-37 amino acids long, in the COOH-terminal regions of the proteins. The two fibronectin-binding proteins have heterologous amino acid sequences, except for the COOH-terminal ends which include the fibronectin-binding repeats. The fibronectin-binding regions of the genes have been fused to IgG-binding domains of protein A, utilizing the IgG-binding capacity of the resulting fusion proteins, to facilitate isolation of the fibronectin-binding domains.Fibronectin (Fn) is a large dimeric glycoprotein (molecular mass 430-470 kDa) which is found in plasma and other body fluids in a soluble form, and is incorporated as microfibrils into the extracellular matrix of most tissues as an insoluble form. The main function of Fn is presumably related to its ability to mediate the substrate adhesion of eucaryotic cells, which involves the binding of specific cell-surface receptors of the integrin family to certain domains in the Fn molecule. The first characterized binding site in Fn for eucaryotic cells contains the amino acid sequence RGD and is located in the central region of the protein (Pierschbacher and Ruoslahti, 1984). Recently, additional recognition sites have been identified (Komoriya et al., 1991). Fn also interacts with other matrix components ; binding sites for collagen, fibrin and sulfated glycosaminoglycans are located in discrete domains of the protein. The present knowledge of the structure and function of Fn has recently been summarized by Hynes (1990).

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Two different genes coding for fibronectin‐binding proteins from Streptococcus dysgalactiae

Lindgren

McGavin

Signäs

et al. 1993

European Journal of Biochemistry

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“…dysgalactiae (GCS) is a pathogen frequently associated with clinical and subclinical bovine mastitis, a disease that causes major economic losses in the dairy industry (51,67). Virulence determinants have been identified for this pathogen, such as surface proteins which specifically interact with plasma or extracellular matrix proteins of the host, such as alpha-2-macroglobulin, plasminogen, albumin, fibrinogen, fibronectin, vitronectin, and collagen (30,35,46,64), and genes coding for proteins assumed to play a role in mastitis, such as the alpha-2-macroglobulin-, immunoglobulin G-, or immunoglobulin Abinding protein Mig (25,55); the alpha 2-macroglobulin-or immunoglobulin G-binding protein Mag (24); and a fibrinogen-binding M-like protein (65).…”

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Virulence Gene Pool Detected in Bovine Group C Streptococcus dysgalactiae subsp. dysgalactiae Isolates by Use of a Group A S. pyogenes Virulence Microarray

et al. 2011

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A custom-designed microarray containing 220 virulence genes of Streptococcus pyogenes (group A Streptococcus [GAS]) was used to test group C Streptococcus dysgalactiae subsp. dysgalactiae (GCS) field strains causing bovine mastitis and group C or group G Streptococcus dysgalactiae subsp. equisimilis (GCS/GGS) isolates from human infections, with the latter being used for comparative purposes, for the presence of virulence genes. All bovine and all human isolates carried a fraction of the 220 genes (23% and 39%, respectively). The virulence genes encoding streptolysin S, glyceraldehyde-3-phosphate dehydrogenase, the plasminogen-binding M-like protein PAM, and the collagen-like protein SclB were detected in the majority of both bovine and human isolates (94 to 100%). Virulence factors, usually carried by human beta-hemolytic streptococcal pathogens, such as streptokinase, laminin-binding protein, and the C5a peptidase precursor, were detected in all human isolates but not in bovine isolates. Additionally, GAS bacteriophage-associated virulence genes encoding superantigens, DNase, and/or streptodornase were detected in bovine isolates (72%) but not in the human isolates. Determinants located in non-bacteriophage-related mobile elements, such as the gene encoding R28, were detected in all bovine and human isolates. Several virulence genes, including genes of bacteriophage origin, were shown to be expressed by reverse transcriptase PCR (RT-PCR). Phylogenetic analysis of superantigen gene sequences revealed a high level (>98%) of identity among genes of bovine GCS, of the horse pathogen Streptococcus equi subsp. equi, and of the human pathogen GAS. Our findings indicate that alphahemolytic bovine GCS, an important mastitis pathogen and considered to be a nonhuman pathogen, carries important virulence factors responsible for virulence and pathogenesis in humans.

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“…The bacterium expresses various extracellular and cell surface bound proteins which specifically interact with plasma or connective tissue proteins of the host (21,26,35,39) and are assumed to play an important role for the colonization and persistence of the pathogen in the host. Genes of various S. dysgalactiae isolates coding for proteins binding ␣ 2 -macroglobulin (␣ 2 M), albumin, immunoglobulin G (IgG), and fibronectin have been cloned and characterized (15-17, 22, 43).…”

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“…Since fibrinogen (Fg) binding is common among mastitis isolates of S. dysgalactiae (26,35) and is also a feature expressed by M or M-like proteins, the library was affinity selected against this protein. Phagemid clones binding to Fg were isolated, and the inserts of chromosomal DNA in the corresponding phagemid vectors were sequenced.…”

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M-Like Proteins ofStreptococcus dysgalactiae

et al. 2000

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Streptococcus dysgalactiae is one of the most important bacterial species isolated from bovine mastitis. To identify potential virulence factors of this species we prepared chromosomal DNA from strain 8215 and constructed a phage display library. By affinity selection of the library against fibrinogen (Fg), we isolated and characterized a gene, called demA, encoding a protein with the molecular mass of ϳ58 kDa, called DemA, displaying both plasma protein binding properties and sequence similarities with the M and M-like proteins of other streptococcal species. Purified recombinant DemA protein was found to completely inhibit Fg-binding to cells of S. dysgalactiae. A continued sequence analysis revealed that the demA gene was preceded by an open reading frame (dmgA) coding for a putative protein, called DmgA, with high similarities to the Mga proteins of Streptococcus pyogenes. By additional cloning, the corresponding dmgA and demA genes from another strain, called Epi9, were isolated and analyzed. These genes, called dmgB and demB, respectively, revealed a high degree of similarity to the corresponding genes in strain 8215. Increased binding of Fg by cells of strain Epi9, grown in an atmosphere with 10% CO 2 , was correlated to an enhanced transcription of the demB gene as shown in a Northern blot. Strain 8215 did not respond to CO 2 , which could be explained by a nonfunctional dmgA gene due to insertion of an insertion sequence element. Based on sequence similarities of the described proteins to Mga, M, and M-like proteins and the response to elevated level of CO 2 , we suggest that the dmg and dem genes are members of a regulon similar to the described mga regulon in S. pyogenes, which encodes several virulence factors in this species.Streptococcus dysgalactiae, a Lancefield group C ␣-hemolytic streptococcus species, is a common pathogen in subclinical and clinical mastitis causing substantial economic losses in dairy herds (6, 41). The bacterium expresses various extracellular and cell surface bound proteins which specifically interact with plasma or connective tissue proteins of the host (21,26,35,39) and are assumed to play an important role for the colonization and persistence of the pathogen in the host. Genes of various S. dysgalactiae isolates coding for proteins binding ␣ 2 -macroglobulin (␣ 2 M), albumin, immunoglobulin G (IgG), and fibronectin have been cloned and characterized (15-17, 22, 43). The interaction between the ␣ 2 M-protease complex and cells of streptococci reduces the phagocytosis of the bacteria by polymorphonuclear leukocytes (42). Binding of IgG from various animal species in a nonimmune fashion via the constant region of the molecule is considered to interfere in various ways with the recognition of the streptococcal cells by the host immune system (3, 9, 34). Recent publications on colonization and invasion of host epithelial cells by group A streptococci revealed the importance of the fibronectin-binding property and the M1 protein in this process (10, 31). The invasion of epithe...

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Binding of fibronectin, fibrinogen and type II collagen to streptococci isolated from bovine mastitis

Cited by 34 publications

References 21 publications

Two different genes coding for fibronectin‐binding proteins from Streptococcus dysgalactiae

Two different genes coding for fibronectin‐binding proteins from Streptococcus dysgalactiae

Virulence Gene Pool Detected in Bovine Group C Streptococcus dysgalactiae subsp. dysgalactiae Isolates by Use of a Group A S. pyogenes Virulence Microarray

M-Like Proteins ofStreptococcus dysgalactiae

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