1995
DOI: 10.1128/iai.63.8.3015-3020.1995
|View full text |Cite
|
Sign up to set email alerts
|

Analysis of a second bacteriophage hyaluronidase gene from Streptococcus pyogenes: evidence for a third hyaluronidase involved in extracellular enzymatic activity

Abstract: The hyaluronidase gene (hylP2) from a second group A streptococcal bacteriophage was isolated from ATCC T-type-22 hyaluronidase-producing strain 10403, a strain known to produce increased amounts of extracellular hyaluronidase. Sequence analysis of hylP2 and alignment with the previously described bacteriophage hyaluronidase gene (hylP) showed a high degree of similarity; however, hylP2 had deletions of regions specifying 34 amino acids. Twenty-eight of the deleted amino acids were in a region of HylP containi… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
39
0

Year Published

1997
1997
2015
2015

Publication Types

Select...
8
1

Relationship

0
9

Authors

Journals

citations
Cited by 77 publications
(39 citation statements)
references
References 32 publications
0
39
0
Order By: Relevance
“…Comparison of the deduced amino acid sequence of the S. pyogenes hyaluronidase with that of other hyaluronidases indicates a high degree of similarity to deduced se-quences from Streptococcus pneumoniae [6], Staphylococcus aureus [4] and Streptococcus agalactiae [5] with 49, 44 and 40% similarities, respectively, over the entire gene. Similarities with other Gram-positive organism hyaluronate lyases are weaker (21^31% similarities), with little or no homology to the streptococcal bacteriophage hyaluronidases [11,23].…”
Section: Resultsmentioning
confidence: 99%
“…Comparison of the deduced amino acid sequence of the S. pyogenes hyaluronidase with that of other hyaluronidases indicates a high degree of similarity to deduced se-quences from Streptococcus pneumoniae [6], Staphylococcus aureus [4] and Streptococcus agalactiae [5] with 49, 44 and 40% similarities, respectively, over the entire gene. Similarities with other Gram-positive organism hyaluronate lyases are weaker (21^31% similarities), with little or no homology to the streptococcal bacteriophage hyaluronidases [11,23].…”
Section: Resultsmentioning
confidence: 99%
“…A hyaluronic acid capsule can surround the host cells of both of these phages; hence the bacteriophage may require hyaluronidase for penetration of this capsular material. No hyaluronidase activity was detected in the extracellular milieu of either S. pyogenes or S. equi infected with the temperate bacteriophages [18,19], suggesting the enzymes may be part of the bacteriophage particle.…”
Section: Organisms Producing Hyaluronidasementioning
confidence: 99%
“…The bacterial hyaluronidases, along with their accession number, are from S. aureus (U21221) [20], Streptococcus agalactiae (Y15903) [21], S. pneumoniae (L20670) [7], S. griseus (AB028210), S. coelicolor (AL031124), P. acnes (U15927) [22], C. perfringens (P26831) [12], Proteus vulgaris (1095454) [23], along with a partial sequence of the lyase from Bacteroides thetaiotaomicron (L42367) [24]. Two sequenced bacteriophage hyaluronidases are both derived from temperate phages that infect group A streptococci (M19348 and U28144) [18]. Sequence analysis of the hyaluronidase genes provides important information on the hyaluronidases.…”
Section: Sequence Informationmentioning
confidence: 99%
“…The bound hyaluronidase produced by the bacteriophage is not secreted from the cell and is a part of the bacteriophage particle. Its main function is to assist the phage in the penetration of the HA capsule that surrounds the host cells of this phage and hence gain access to the cell surface of the host Streptococcus [4]. Apart from this, an indirect role of the bacteriophage-encoded hyaluronidase in streptococcal disease has also been indicated where it transforms the nonvirulent streptococcal strains into virulent strains.…”
mentioning
confidence: 99%