Dataset Information

Proteins of T7 phage pulled down with EfAvs5，LC-MSMS

ABSTRACT: We infected cells expressing a FLAG-tagged EfAvs5 with phage T7, and immunoprecipitated the tagged EfAvs5 together with proteins bound to it. Mass spectrometry analysis showed 17 proteins of phage T7 were pulled down together with EfAvs5. These proteins are potential activators of EfAvs5.The control group is not infected by phage.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli Bacteria

SUBMITTER: Yiqun Wang

LAB HEAD: Jianting Zheng

PROVIDER: PXD060416 | Pride | 2025-05-07

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20241101_YP202490650_SST_Slot2-2_1_4367.d.zip	Other
	20241101_YP202490650_SS_Slot2-1_1_4370.d.zip	Other
	20241115_183309_YP202490650.sne	Other
	checksum.txt	Txt

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Publications

Filamentation activates bacterial Avs5 antiviral protein.

Wang Yiqun Y Tian Yuqing Y Yang Xu X Yu Feng F Zheng Jianting J

Nature communications 20250311 1

Bacterial antiviral STANDs (Avs) are evolutionarily related to the nucleotide-binding oligomerization domain (NOD)-like receptors widely distributed in immune systems across animals and plants. EfAvs5, a type 5 Avs from Escherichia fergusonii, contains an N-terminal SIR2 effector domain, a NOD, and a C-terminal sensor domain, conferring protection against diverse phage invasions. Despite the established roles of SIR2 and STAND in prokaryotic and eukaryotic immunity, the mechanism underlying thei ...[more]

PMID: 40069208

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