Phosphorylation of LukS by Protein Kinase A is Crucial for the LukS-Specific Function of the Staphylococcal Leukocidin on Human Polymorphonuclear Leukocytes

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概要

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• Staphylococcal leukocidin (Luk) consists of two protein components, LukF and LukS, which cooperatively lyse human and rabbit polymorphonuclear leukocytes. Here, we demonstrate that the phosphorylation of LukS by protein kinase A is crucial for the LukS-specific leukocytolytic function of Luk on HPMNLs by using N-[2(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), which is a potent and selective inhibitor of protein kinase A. At 0.5μM H-89 completely prevented the Luk-induced cell lysis accompanied by blocking of the incorporation of exogenous ^<32>P-H_3PO_4 into LukS on HPMNLs. However, with LukS and LukF together, 0.5μM H-89 did not inhibit the cell swelling which takes place before the cell lysis. HPMNLs also became swollen upon treating with both LukF and LukS mutants which could not be phosphorylated.

• 社団法人日本農芸化学会の論文
• 1998-09-23

著者

• NARIYA Hirofumi

  Department of Applied Microbiology, Graduate School of Agricultural Science, Tohoku University

• KAMIO Yoshiyuki

  Department of Applied Microbiology, Graduate School of Agricultural Science, Tohoku University

• Nariya Hirofumi

  Department Of Applied Microbiology Graduate School Of Agricultural Science Tohoku University

• Nariya Hirofumi

  Department Of Applied Biological Chemistry Faculty Of Agriculture Tohoku University

• NISHIYAMA Akihito

  Department of Physics, Tokyo Metropolitan University

• Kamio Yoshiyuki

  Department Of Agricultural Chemistry Tohoku University

• Kamio Yoshiyuki

  Department Of Applied Microbiology Graduate School Of Agricultural Science Tohoku University

• Nishiyama Akihito

  Laboratory Of Applied Microbiology Department Of Microbial Biotechnology Graduate School Of Agricult

• Nishiyama Akihito

  Department Of Physics Tokyo Metropolitan University

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