A novel member of the thermolysin family, cloning and biochemical characterization of metalloprotease from Staphylococcus pseudintermedius

• Autorzy: Wladyka B. , Bista M. , Sabat A.J. , Bonar E. , Grzeszczuk S. , Hryniewicz W. , Dubin A.
• Języki publikacji: EN

Abstrakty

EN

Thermolysins constitute a family of secreted bacterial metalloproteases expressed, among others, by several pathogens. Strains of Staphylococcus pseudintermedius isolated from diseased dogs and judged as protease-positive, by skim milk agar plate culture, were investigated for protease content. No proteolytic activity was detected when the bacteria were grown in regular liquid media. Unexpectedly, supplementation of the medium with calcium ions resulted in expression of a metalloprotease and profound changes in the profile of extracellular proteins. On the basis of homology to other staphylococcal metalloproteases, the nucleotide sequence of the gene encoding this protease (Pst) and its flanking regions was determined. The full-length pstcodes for a protein with an open reading frame of 505 amino acids. The internal region contains the HEXXH catalytic domain that is conserved in members of the thermolysin family. Regardless of the presence of calcium in the medium, the expression of the protease gene was of the same intensity. This suggests that regulation of the metalloprotease production by calcium ions is at a post-transcriptional level. Isolates of S. pseudintermediusexhibit a proteolytic phenotype due to the metalloprotease expression, however only in presence of calcium ions, which most probably stabilize the structure of the protease.

Słowa kluczowe

PL

thermolysin family; cloning; biochemical characteristics; metalloprotease; Staphylococcus pseudintermedius; pathogen; calcium; animal pathogen; protease structure

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2008
• Tom: 55
• Numer: 3
• Opis fizyczny: p.525-536,fig.,ref.

Twórcy

autor

Wladyka B.

• Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland

autor

Bista M.

autor

Sabat A.J.

autor

Bonar E.

autor

Grzeszczuk S.

autor

Hryniewicz W.

autor

Dubin A.

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