کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2047578 1073994 2015 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A single amino acid of a Salmonella virulence protein contributes to pathogenicity by protecting from the FtsH-mediated proteolysis
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
A single amino acid of a Salmonella virulence protein contributes to pathogenicity by protecting from the FtsH-mediated proteolysis
چکیده انگلیسی


• Trp226 of the Salmonella MgtC protein is conserved only in intracellular pathogens.
• Trp226 to Ala substitution promotes MgtC degradation by the FtsH protease.
• Salmonella MgtC Trp226 protects from proteolysis, promoting virulence.
• The FtsH protease is inactive inside host, further increasing the MgtC protein.

FtsH is a membrane-bound ATP-dependent protease in bacteria that is critical for degrading membrane proteins. The MgtC virulence protein from Salmonella enterica is located at the inner membrane and required for survival inside macrophages. Here we report that a single substitution at tryptophan 226 of the MgtC protein to alanine promotes the FtsH-mediated proteolysis. The Trp residue is located at the very C-terminus of the cytoplasmic domain of the MgtC protein and conserved only in intracellular pathogens surviving within a macrophage phagosome, suggesting that Salmonella may acquire the tryptophan residue to prevent MgtC degradation by the FtsH protease. Moreover, the reduced proteolytic activity of the FtsH protease during infection further increases MgtC production, promoting Salmonella’s pathogenicity inside phagocytic cells.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 589, Issue 12, 22 May 2015, Pages 1346–1351
نویسندگان
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