α-enolase, a plasmin(ogen) binding and cell wall associating protein from a fish pathogenic Streptococcus iniae strain

• Published in: Aquaculture 2007-05, Vol.265 (1), p.55-60
• Main Authors: Kim, Min Sun, Choi, Seung Hyuk, Lee, Eun Hye, Nam, Yoon Kwon, Kim, Sung Koo, Kim, Ki Hong
• Format: Article
• Language: English
• Subjects: Agnatha. Pisces; alpha-enolase; amino acid sequences; Animal aquaculture; animal pathogenic bacteria; Animal productions; bacterial infections; bacterial proteins; Biological and medical sciences; Cell wall association; cell walls; fish culture; fish diseases; Fundamental and applied biological sciences. Psychology; General aspects; Gram-positive bacteria; hydro-lyases; molecular sequence data; nucleotide sequences; Paralichthys olivaceus; Pisces; Plasmin(ogen); plasminogen; recombinant fusion proteins; streptococcosis; Streptococcus iniae; Streptococcus pneumoniae; Streptococcus pyogenes; Vertebrates: general zoology, morphology, phylogeny, systematics, cytogenetics, geographical distribution; α-enolase
• ISSN: 0044-8486; 1873-5622
• DOI: 10.1016/j.aquaculture.2007.01.034

The plasmin(ogen) binding property of pathogenic bacteria is suggested to be one of the characteristics that may contribute to tissue invasion. Recently, the presence of a surface-localized α-enolase that binds both plasmin and plasminogen has been reported from Streptococcus pyogenes and from S. pneumoniae. To investigate whether α-enolase of S. iniae has similar characteristics to that of the above streptococci, in the present study, we have produced α-enolase as a recombinant protein from a fish pathogenic S. iniae strain, and demonstrated for the first time its plasmin(ogen)-binding ability and cell wall-association using immunoblot method. These results suggest that α-enolase of S. iniae may be responsible in part for the ability of S. iniae to cross tissue barriers through plasminogen activation.