The Paramyxovirus SV5 V Protein Binds Two Atoms of Zinc and Is a Structural Component of Virions

Reay G. Paterson; George P. Leser; Margaret A. Shaughnessy; Robert A. Lamb

doi:10.1006/viro.1995.1135

The Paramyxovirus SV5 V Protein Binds Two Atoms of Zinc and Is a Structural Component of Virions

Reay G. Paterson^*, George P. Leser, Margaret A. Shaughnessy, Robert A. Lamb

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

129 Scopus citations

Abstract

The paramyxovirus simian virus 5 (SVS) cysteine-rich V protein has been shown to be a virus structural protein by analysis of the polypeptides of purified SV5 virions. In addition, the V protein has been identified as a component of the virus nucleocapsid core both by the analysis of the polypeptides present in radioactively labeled preparations of purified nucleocapsids and by immunoelectron microscopy. Quantitative autoradiography was used to determine that there are ∼350 molecules of the V protein in virions. The V protein has been purified from V recombinant baculovirus-infected insect cells and by using inductively coupled argon plasma atomic emission spectroscopy it was found that each molecule of V binds two zinc atoms.

Original language	English (US)
Article number	71135
Pages (from-to)	121-131
Number of pages	11
Journal	Virology
Volume	208
Issue number	1
DOIs	https://doi.org/10.1006/viro.1995.1135
State	Published - Apr 1 1995

ASJC Scopus subject areas

Virology

Access to Document

10.1006/viro.1995.1135

Cite this

@article{2073ed82dec44ac5b9bb7c2fc1c98774,

title = "The Paramyxovirus SV5 V Protein Binds Two Atoms of Zinc and Is a Structural Component of Virions",

abstract = "The paramyxovirus simian virus 5 (SVS) cysteine-rich V protein has been shown to be a virus structural protein by analysis of the polypeptides of purified SV5 virions. In addition, the V protein has been identified as a component of the virus nucleocapsid core both by the analysis of the polypeptides present in radioactively labeled preparations of purified nucleocapsids and by immunoelectron microscopy. Quantitative autoradiography was used to determine that there are ∼350 molecules of the V protein in virions. The V protein has been purified from V recombinant baculovirus-infected insect cells and by using inductively coupled argon plasma atomic emission spectroscopy it was found that each molecule of V binds two zinc atoms.",

author = "Paterson, {Reay G.} and Leser, {George P.} and Shaughnessy, {Margaret A.} and Lamb, {Robert A.}",

year = "1995",

month = apr,

day = "1",

doi = "10.1006/viro.1995.1135",

language = "English (US)",

volume = "208",

pages = "121--131",

journal = "Virology",

issn = "0042-6822",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - The Paramyxovirus SV5 V Protein Binds Two Atoms of Zinc and Is a Structural Component of Virions

AU - Paterson, Reay G.

AU - Leser, George P.

AU - Shaughnessy, Margaret A.

AU - Lamb, Robert A.

PY - 1995/4/1

Y1 - 1995/4/1

N2 - The paramyxovirus simian virus 5 (SVS) cysteine-rich V protein has been shown to be a virus structural protein by analysis of the polypeptides of purified SV5 virions. In addition, the V protein has been identified as a component of the virus nucleocapsid core both by the analysis of the polypeptides present in radioactively labeled preparations of purified nucleocapsids and by immunoelectron microscopy. Quantitative autoradiography was used to determine that there are ∼350 molecules of the V protein in virions. The V protein has been purified from V recombinant baculovirus-infected insect cells and by using inductively coupled argon plasma atomic emission spectroscopy it was found that each molecule of V binds two zinc atoms.

AB - The paramyxovirus simian virus 5 (SVS) cysteine-rich V protein has been shown to be a virus structural protein by analysis of the polypeptides of purified SV5 virions. In addition, the V protein has been identified as a component of the virus nucleocapsid core both by the analysis of the polypeptides present in radioactively labeled preparations of purified nucleocapsids and by immunoelectron microscopy. Quantitative autoradiography was used to determine that there are ∼350 molecules of the V protein in virions. The V protein has been purified from V recombinant baculovirus-infected insect cells and by using inductively coupled argon plasma atomic emission spectroscopy it was found that each molecule of V binds two zinc atoms.

UR - http://www.scopus.com/inward/record.url?scp=0028964081&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028964081&partnerID=8YFLogxK

U2 - 10.1006/viro.1995.1135

DO - 10.1006/viro.1995.1135

M3 - Article

C2 - 11831692

AN - SCOPUS:0028964081

SN - 0042-6822

VL - 208

SP - 121

EP - 131

JO - Virology

JF - Virology

IS - 1

M1 - 71135

ER -

The Paramyxovirus SV5 V Protein Binds Two Atoms of Zinc and Is a Structural Component of Virions

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this