Symptom Attenuation by a Normally Virulent Satellite RNA of Turnip Crinkle Virus Is Associated with the Coat Protein Open Reading Frame

1995 ◽  
Vol 7 (10) ◽  
pp. 1625
Author(s):  
Qingzhong Kong ◽  
Jong-Won Oh ◽  
Anne E. Simon
Keyword(s):  
Coat Protein ◽  
Open Reading Frame ◽  
Turnip Crinkle Virus ◽  
Satellite Rna ◽  
Reading Frame

scholarly journals pIIICTX, a Predicted CTXφ Minor Coat Protein, Can Expand the Host Range of Coliphage fd To Include Vibrio cholerae

2003 ◽  
Vol 185 (3) ◽  
pp. 1037-1044 ◽  
Author(s):  
Andrew J. Heilpern ◽  
Matthew K. Waldor
Keyword(s):  
Coat Protein ◽  
Vibrio Cholerae ◽  
Protein Sequences ◽  
Open Reading Frame ◽  
Filamentous Phage ◽  
Host Bacterium ◽  
Reading Frame ◽  
New Evidence ◽  
Minor Coat Protein

ABSTRACT CTXφ is a filamentous bacteriophage that encodes cholera toxin. CTXφ infection of its host bacterium, Vibrio cholerae, requires the toxin-coregulated pilus (TCP) and the products of the V. cholerae tolQRA genes. Here, we have explored the role of OrfU, a predicted CTXφ minor coat protein, in CTXφ infection. Prior to the discovery that it was part of a prophage, orfU was initially described as an open reading frame of unknown function that lacked similarity to known protein sequences. Based on its size and position in the CTXφ genome, we hypothesized that OrfU may function in a manner similar to that of the coliphage fd protein pIII and mediate CTXφ infection as well as playing a role in CTXφ assembly and release. Deletion of orfU from CTXφ dramatically reduced the number of CTXφ virions detected in supernatants from CTXφ-bearing cells. This defect was complemented by expression of orfU in trans, thereby confirming a role for this gene in CTXφ assembly and/or release. To evaluate the requirement for OrfU in CTXφ infection, we introduced fragments of orfU into gIII in an fd derivative to create OrfU-pIII fusions. While fd is ordinarily unable to infect V. cholerae, an fd phage displaying the N-terminal 274 amino acids of OrfU could infect V. cholerae in a TCP- and TolA-dependent fashion. Since our findings indicate that OrfU functions as the CTXφ pIII, we propose to rename OrfU as pIIICTX. Our data also provide new evidence for a conserved pathway for filamentous phage infection.

scholarly journals Interaction between the Open Reading Frame III Product and the Coat Protein Is Required for Transmission of Cauliflower Mosaic Virus by Aphids

2001 ◽  
Vol 75 (1) ◽  
pp. 100-106 ◽  
Author(s):  
Véronique Leh ◽  
Emmanuel Jacquot ◽  
Angèle Geldreich ◽  
Muriel Haas ◽  
Stéphane Blanc ◽  
...  
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Direct Interaction ◽  
Cauliflower Mosaic Virus ◽  
Open Reading Frame ◽  
Nonstructural Proteins ◽  
Interaction Domain ◽  
Reading Frame ◽  
Virus Particles ◽  
Terminal Domain

ABSTRACT Transmission of cauliflower mosaic virus (CaMV) by aphids requires two viral nonstructural proteins, the open reading frame (ORF) II and ORF III products (P2 and P3). An interaction between a C-terminal domain of P2 and an N-terminal domain of P3 is essential for transmission. Purified particles of CaMV are efficiently transmitted only if aphids, previously fed a P2-containing solution, are allowed to acquire a preincubated mixture of P3 and virions in a second feed, thus suggesting a direct interaction between P3 and coat protein. Herein we demonstrate that P3 directly interacts with purified viral particles and unassembled coat protein without the need for any other factor and that P3 mediates the association of P2 with purified virus particles. The interaction domain of P3 is located in its C-terminal half, downstream of the P3-P2 interaction domain but overlapping a region which binds nucleic acids. Mutagenesis of P3 which interferes with the interaction between P3 and virions is correlated with the loss of transmission by aphids. Taken together, our results demonstrate that P3 plays a crucial role in the formation of the CaMV transmissible complex by serving as a bridge between P2 and virus particles.

scholarly journals Rice Tungro Bacilliform Virus Open Reading Frame 3 Encodes a Single 37-kDa Coat Protein

Virology ◽  
1999 ◽  
Vol 253 (2) ◽  
pp. 319-326 ◽  
Author(s):  
Philippe Marmey ◽  
Brian Bothner ◽  
Emmanuel Jacquot ◽  
Alexandre de Kochko ◽  
Ching Ang Ong ◽  
...  
Keyword(s):  
Coat Protein ◽  
Open Reading Frame ◽  
Rice Tungro Bacilliform Virus ◽  
Reading Frame

scholarly journals Coding-Complete Genome Sequence of a Partitivirus Isolated from Pine Processionary Moth Eggs

2021 ◽  
Vol 10 (8) ◽  
Author(s):  
Franck Dorkeld ◽  
Réjane Streiff ◽  
Carole Kerdelhué ◽  
Mylène Ogliastro
Keyword(s):  
Coat Protein ◽  
Complete Genome Sequence ◽  
Open Reading Frame ◽  
Thaumetopoea Pityocampa ◽  
Data Sets ◽  
Rna Dependent Rna Polymerase ◽  
Content Type ◽  
Reading Frame ◽  
Pine Processionary Moth ◽  
Transcriptomic Data

ABSTRACT Two coding-complete nucleotide sequences of a partitivirus (family Partitiviridae) were discovered in transcriptomic data sets obtained from eggs of the Lepidoptera Thaumetopoea pityocampa. Each segment encodes a single open reading frame, and these two segments are predicted to encode an RNA-dependent RNA polymerase and a coat protein, respectively.

Sign in / Sign up

Export Citation Format

Share Document