Monoclonal antibodies to the matrix protein of vesicular stomatitis virus (New Jersey serotype) and their effects on viral transcription

Ye, Zhiping; Pal, Ranajit; Ogden, John R.; Snyder, Ruth M.; Wagner, Robert R.

doi:10.1016/0042-6822(85)90408-8

Cited by 9 publications

(6 citation statements)

References 15 publications

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“…The findings presented in this study confirm the conclusions of earlier reports that assigned a vRNA transcription inhibition function to the influenza virus Mr protein (8,9), and that provided a partial epitope map of the site(s) critical for such a function (8).…”

Section: Discussionsupporting

confidence: 81%

“…Recently, reports have appeared that indicate the involvement of influenza virus MI protein in regulation of viral RNA transcription (8,9). This protein had previously been thought to function solely as a structural template for attachment of the surface glycoproteins during virus encapsidation (3,lO).…”

Section: Introductionmentioning

confidence: 99%

“…Although the transcription inhibition function of M, is well supported by experimental evidence, the region(s) of the polypeptide tertiary structure necessary for exerting this effect have not yet been identified. Ye et al reported that the carboxy-terminal two thirds of MI is critical for interaction with RNP (8), but analyses were conducted only in one dimension.…”

Section: Introductionmentioning

confidence: 99%

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Monoclonal antibody analysis of influenza virus matrix protein epitopes involved in transcription inhibition

Hankins¹,

Nagata

Bucher

et al. 1989

Virus Genes

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Influenza virus M1 protein has been shown to inhibit viral RNA transcription, and in this study the epitopes on M1 critical for this function were localized. When a battery of 15 monoclonal anti-M1 antibodies were reacted with chemically cleaved fragments of M1 on a western blot, five distinct banding patterns were observed. A representative antibody was selected from each banding group, and its ability to reverse M1-effected transcription inhibition was measured. From these data, the sites on M1 critical for transcription inhibition were deduced. It appears now that the regions on M1 in the vicinity of amino acid residues #70 and #140 are critical for inhibition. Furthermore, by taking into account the hydropathicity and secondary structure, it is hypothesized that amino acids #70 and #140 are physically close together in the final three-dimensional conformation of M1 protein and that the residues in between form a loop and are thus removed from the functional site.

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Section: Discussionsupporting

confidence: 81%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Monoclonal antibody analysis of influenza virus matrix protein epitopes involved in transcription inhibition

Hankins¹,

Nagata

Bucher

et al. 1989

Virus Genes

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“…Recently, Wagner and his co-workers (155,156,246) have raised monoclonal antibodies against the M protein to study the role of M protein in viral transcription in vitro. Monoclonal antibodies to three distinct antigenic determinants affected in vitro transcription by wild-type RNP/M cores (RNP with M protein attached) in widely divergent ways.…”

Section: Regulation Of Rna Synthesis: Role Of M Proteinmentioning

confidence: 99%

Transcription and replication of rhabdoviruses.

Banerjee¹

1987

Microbiological Reviews

187

110

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“…Group III temperaturesensitive mutants with a lesion in the M protein did not exhibit this transcription-inhibitory activity (12,14,25). Reconstitution of purified wild-type M protein with RNP cores has been shown to inhibit in vitro viral transcription reactions at the level of RNA chain elongation (13,15,17,39,42,55,56).These studies collectively suggest that M protein must have at least two sites of interaction: one with the envelope and one with the RNP of the virion. In this study we present data to show that M protein can mediate the binding of RNP structures to acidic phospholipid bilayers.…”

mentioning

confidence: 99%

Mapping regions of the matrix protein of vesicular stomatitis virus which bind to ribonucleocapsids, liposomes, and monoclonal antibodies

Ogden¹,

Pal²,

Wagner³

1986

J Virol

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The matrix (M) protein of vesicular stomatitis virus (VSV) appears to function as a bridge between the ribonucleocapsid (RNP) core and the envelope in assembly of the virion. Two such properties would necessitate at least one site for interaction with the nucleocapsid and one with the envelope. In this study M protein was found to mediate the in vitro binding to RNP cores of phospholipid vesicles, representing membrane structures. The M protein could bind initially to either the vesicles or the RNP cores to promote RNP-vesicle association. A trypsin-resistant fragment (MT) of M protein, missing the initial 43 amino acids from its amino terminus, reconstituted with acidic phospholipid vesicles with the same binding efficiency as did whole M protein, suggesting that the carboxy-terminal 81% retained those regions of the M protein which interact with a lipid bilayer. The MT protein, however, was considerably less efficient than intact M protein as an inhibitor of in vitro virus transcription; almost 2.5-fold more MT protein than intact M protein was required for 50% inhibition of VSV transcription, indicating that a site for interaction with the RNP core may have been lost. A monoclonal antibody which is able to reverse the in vitro inhibition of transcription by M protein did not react by immunoblotting with MT protein. Partial tryptic digests of the M protein probed with this monoclonal antibody indicated that epitope 1 lies between amino acid residues 18 and 43. This region appears to be a site that promotes interaction of the M protein with the RNP core of VSV. Monoclonal antibodies to epitopes 2 and 3, which exhibit some overlap in binding to M protein but do not reverse transcription inhibition, were mapped by cleavage with N-chlorosuccinimide at regions in a carboxy direction from epitope 1. * Corresponding author. t Present address: Biotherapeutics Incorporated, Franklin, TN 37064.G, and M) take independent paths to the site of virus assembly at the plasma membrane of the infected cell (1,2,6,16,22,23,34); synthesis of M protein is the rate-limiting step in this maturation process (53). Removal of M protein from the RNP core yields a relaxed, highly extended nucleocapsid structure, while condensation of the RNP into a tightly coiled skeleton is mediated through the association of M protein with the nucleocapsid (20,37,38). Appearance of M protein at the cell membrane causes decreased mobility of the already-inserted G protein (46). Protein cross-linking studies with intact virions revealed the formation of G-M and M-N but not G-N heterodimers (18). These studies suggest that M protein functions as a bridge between the cytoplasmic RNP structures and those regions of the cellular membrane into which the G protein has been inserted.The strong interaction between M protein and the RNP core enables M protein to act as an endogenous inhibitor of viral transcription. Transcription reactions with detergentdisrupted whole virions demonstrate a virus-concentrationdependent regulatory effect which was attributed to an ...

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Monoclonal antibodies to the matrix protein of vesicular stomatitis virus (New Jersey serotype) and their effects on viral transcription

Cited by 9 publications

References 15 publications

Monoclonal antibody analysis of influenza virus matrix protein epitopes involved in transcription inhibition

Monoclonal antibody analysis of influenza virus matrix protein epitopes involved in transcription inhibition

Transcription and replication of rhabdoviruses.

Mapping regions of the matrix protein of vesicular stomatitis virus which bind to ribonucleocapsids, liposomes, and monoclonal antibodies

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