S-nitrosylation of peroxiredoxin 1 contributes to viability of lung epithelial cells during Bacillus anthracis infection

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• 作者：Myung-Chul Chung^a ; Farhang Alem^a ; Sarah G. Hamer^a ; Aarthi Narayanan^a ; Konstantin Shatalin^b ; Charles Bailey^a ; Evgeny Nudler^b ; Ramin M. Hakami^a ; ^{rhakami@gmu.edu}
• 关键词：NO ; nitric oxide ; NOS ; nitric oxide synthase ; bNOS ; bacterial nitric oxide synthase ; Prx ; peroxiredoxin ; HSAECs ; human small airway epithelial cells ; MOI ; multiplicity of infection ; BST ; Biotin-Switch technique ; L-NAME ; L-Nω-nitroarginine methyl ester ; DAF-2DA ; 4 ; 5-diaminofluorescein diacetate ; SNOC ; S-nitrosocysteine
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1861
• 期：1
• 页码：3019-3029
• 全文大小：975 K
• 卷排序：1861

文摘

bNOS causes S-nitrsoylation of specific host proteins during anthrax infection. Prx1 is a major host target that becomes S-nitrosylated during anthrax infection. S-nitrosylated Prx1 has lower peroxidase activity and increased chaperone function. S-nitrosylated Prx1 contributes to the viability of infected host cell.