THE PHOSPHORYLATION OF THE INTEGRAL MEMBRANE (M1) PROTEIN OF INFLUENZA-VIRUS

被引：21

作者：

GREGORIADES, A ^{[1
]}

GUZMAN, GG ^{[1
]}

PAOLETTI, E ^{[1
]}

机构：

[1] NEW YORK STATE DEPT HLTH,WADSWORTH LABS & RES,ALBANY,NY 12201

来源：

VIRUS RESEARCH | 1990年 / 16卷 / 01期

关键词：

Influenza virus; Phosphorylation;

D O I：

10.1016/0168-1702(90)90041-9

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The phosphorylation of the internal and integral membrane (M1) protein of influenza virus was studied. Four points can be made based on the data: (1) The M1 contains at least two moles of phosphate per mole of M1. (2) Phosphorylation of M1 is conserved between influenza A, B and C viruses. Other characteristics of the M1 are also conserved, such as solubility in organic solvent, heterogeneity and ability to partition into lipid vesicles. (3) M1 is phosphorylated in cells infected with a vaccinia recombinant (vP273) containing only the gene of M1, either as a result of a vaccinia virus associated kinase or a cellular one. (4) The phosphate is located within or in close proximity to the major stretch of neutral and hydrophobic amino acids found in M1, as determined by analyzing cyanogen bromide fragments. © 1990.

引用

页码：27 / 42

页数：16

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