Identification of a functional ITAM-like sequence within G1 cytoplasmic tail of Hantaan virus.
- Author:
Dan-Lei MOU
1
;
Ying-Peng WANG
;
Hong JIANG
;
Shu-Yuan XIAO
;
Xu YU
;
Guang-Yu LI
;
Ping-Zhong WANG
;
Yong-Tao SUN
;
Qing-He NIE
;
Chang-Xing HUANG
;
Xue-Fan BAI
Author Information
1. Center of Infectious Diseases, Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, China. moudanle@yahoo.com.cn
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Cells, Cultured;
Hantaan virus;
chemistry;
physiology;
Humans;
Intracellular Signaling Peptides and Proteins;
physiology;
Molecular Sequence Data;
Phosphorylation;
Protein-Tyrosine Kinases;
physiology;
Proto-Oncogene Proteins c-fyn;
physiology;
Signal Transduction;
Syk Kinase;
Viral Envelope Proteins;
chemistry;
physiology
- From:
Chinese Journal of Virology
2007;23(6):424-428
- CountryChina
- Language:Chinese
-
Abstract:
The G1 cytoplasmic tail of Hantaan virus (HTNV) harbors a highly conserved region, which is homologous to immunoreceptor tyrosine-based activation motifs (ITAM) and is termed the ITAM-like sequence. To demonstrate the potential signal-transducing activity of G1 ITAM-like sequence resembling the canonical ITAM within immune and endothelial cells, a series of experiments were performed to define its interaction with cellular kinases. The synthesized G1 ITAM-like peptide was shown to coprecipitate with cellular phosphoprotein complexes by an immune-complex kinase assay. Mutational analyses showed that this ITAM-like sequence was a substrate for the Src family kinase Fyn, and two conserved tyrosine residues were required for coprecipitating Lyn, Syk, and ZAP-70 kinases. These findings demonstrated that HTNV envelope glycoprotein G1 contains a functional ITAM-like sequence in its cytoplasmic tail, which can bind critical cellular kinases that regulate immune and endothelial cell functions.
