Isolation and Characterization of Hyaluronidases from Streptococcus dysgalactiae, S. zooepidemicus and S. equi

Sting, Reinhard; Schaufuss, P.; Blobel, H.

doi:10.1016/s0934-8840(11)80028-9

Cited by 26 publications

(19 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Bacteroides fragilis, Bacteroides vulgatus, B. ovatus, B. melaninogenicus and Fusobacterium mortiferum are also reported to produce hyaluronidase. The pathogens Treponema pallidum and T. pertenue both produce surface associated HA lyases, whereas the non-pathogenic T. denticola and T. vencentii do not produce such an enzyme (Linhardt et al, 1986;Sting et al, 1990). Generally, HA lyases from gram positive and negative organisms are high molecular weight proteins compared to phage related hyaluronidases.…”

Section: Microbial Hyaluronidasesmentioning

confidence: 99%

The magic glue hyaluronan and its eraser hyaluronidase: A biological overview

2007

View full text Add to dashboard Cite

Section: Microbial Hyaluronidasesmentioning

confidence: 99%

The magic glue hyaluronan and its eraser hyaluronidase: A biological overview

2007

View full text Add to dashboard Cite

“…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).…”

mentioning

confidence: 99%

M-Like Proteins ofStreptococcus dysgalactiae

et al. 2000

View full text Add to dashboard Cite

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...

show abstract

“…Thus phage induction in vivo may itself represent an additional mechanism leading to host connective tissue damage. It has also been noted that in vitro secreted Hyl activity was absent from culture supernatants of four out of ten S. equi clinical isolates (Sting et al, 1990). Thus the extent to which S. equi is able to degrade host HA may vary from strain to strain.…”

Section: Discussionmentioning

confidence: 98%

The Streptococcus equi prophage-encoded protein SEQ2045 is a hyaluronan-specific hyaluronate lyase that is produced during equine infection

et al. 2009

View full text Add to dashboard Cite

Streptococcus equi causes equine ‘strangles’. Hyaluronate lyases, which degrade connective tissue hyaluronan and chondroitins, are thought to facilitate streptococcal invasion of the host. However, prophage-encoded hyaluronate lyases are hyaluronan-specific and are thought to be primarily involved in the degradation of the hyaluronan capsule of streptococci during bacteriophage infection. To understand the role of prophage-encoded hyaluronate lyases further, we have biochemically characterized such a hyaluronate lyase, SEQ2045 from S. equi, and have shown that it is produced during equine infection. Prophage-encoded hyaluronan-specific hyaluronate lyases may therefore play a more direct role in disease pathogenesis than previously thought.

show abstract

Isolation and Characterization of Hyaluronidases from Streptococcus dysgalactiae, S. zooepidemicus and S. equi

Cited by 26 publications

References 10 publications

The magic glue hyaluronan and its eraser hyaluronidase: A biological overview

The magic glue hyaluronan and its eraser hyaluronidase: A biological overview

M-Like Proteins ofStreptococcus dysgalactiae

The Streptococcus equi prophage-encoded protein SEQ2045 is a hyaluronan-specific hyaluronate lyase that is produced during equine infection

Contact Info

Product

Resources

About