Initial Events Associated with Virus PBCV-1 Infection of Chlorella NC64A

Thiel, Gerhard; Moroni, Anna; Dunigan, David D.; Etten, James L. Van

doi:10.1007/978-3-642-02167-1_7

Cited by 37 publications

(58 citation statements)

References 53 publications

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“…These data are essential for understanding the immediate-early events of infection, such as binding, the entrisome, macromolecular synthetic shutoff, DNA degradation, and viral transcription (47). PBCV-1 is representative of the giant viruses in that they are large, complex, and highly diverse (11).…”

Section: Pbcv-1 Virion Proteomementioning

confidence: 99%

Paramecium bursaria Chlorella Virus 1 Proteome Reveals Novel Architectural and Regulatory Features of a Giant Virus

Dunigan

Cerny

Bauman³

et al. 2012

J Virol

104

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The 331-kbp chlorovirusParamecium bursariachlorella virus 1 (PBCV-1) genome was resequenced and annotated to correct errors in the original 15-year-old sequence; 40 codons was considered the minimum protein size of an open reading frame. PBCV-1 has 416 predicted protein-encoding sequences and 11 tRNAs. A proteome analysis was also conducted on highly purified PBCV-1 virions using two mass spectrometry-based protocols. The mass spectrometry-derived data were compared to PBCV-1 and its hostChlorella variabilisNC64A predicted proteomes. Combined, these analyses revealed 148 unique virus-encoded proteins associated with the virion (about 35% of the coding capacity of the virus) and 1 host protein. Some of these proteins appear to be structural/architectural, whereas others have enzymatic, chromatin modification, and signal transduction functions. Most (106) of the proteins have no known function or homologs in the existing gene databases except as orthologs with proteins of other chloroviruses, phycodnaviruses, and nuclear-cytoplasmic large DNA viruses. The genes encoding these proteins are dispersed throughout the virus genome, and most are transcribed late or early-late in the infection cycle, which is consistent with virion morphogenesis.

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Section: Pbcv-1 Virion Proteomementioning

confidence: 99%

Paramecium bursaria Chlorella Virus 1 Proteome Reveals Novel Architectural and Regulatory Features of a Giant Virus

Dunigan

Cerny

Bauman³

et al. 2012

J Virol

104

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“…The initial recognition and attachment process is probably complete in less than 1 min after mixing virus and algae (20). PBCV-1 protein Vp130 (A140/145R) is required for virus attachment (21).…”

mentioning

confidence: 99%

Three-dimensional structure and function of the Paramecium bursaria chlorella virus capsid

Zhang

Xiang

Dunigan

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

126

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A cryoelectron microscopy 8.5 Å resolution map of the 1,900 Å diameter, icosahedral, internally enveloped Paramecium bursaria chlorella virus was used to interpret structures of the virus at initial stages of cell infection. A fivefold averaged map demonstrated that two minor capsid proteins involved in stabilizing the capsid are missing in the vicinity of the unique vertex. Reconstruction of the virus in the presence of host chlorella cell walls established that the spike at the unique vertex initiates binding to the cell wall, which results in the enveloped nucleocapsid moving closer to the cell. This process is concurrent with the release of the internal viral membrane that was linked to the capsid by many copies of a viral membrane protein in the mature infectous virus. Simultaneously, part of the trisymmetrons around the unique vertex disassemble, probably in part because two minor capsid proteins are absent, causing Paramecium bursaria chlorella virus and the cellular contents to merge, possibly as a result of enzyme(s) within the spike assembly. This may be one of only a few recordings of successive stages of a virus while infecting a eukaryotic host in pseudoatomic detail in three dimensions.3D structure | cell entry | conformation changes | minor proteins | PBCV-1

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“…These hydrolytic enzymes rapidly digest a hole into the cell wall. These holes were observable after only 1 min post-infection (Thiel et al 2010). Plugge and collaborators (2000) discovered that PBCV-1 encodes small potassium ion channel protein or viroporin that form a functional tetrameric transmembrane channel.…”

Section: Pore-forming Enzymesmentioning

confidence: 94%

“…27 allows the entry of viral DNA easier (Thiel et al 2010). These kinds of ion channels are widely present in Chlorella viruses (Kang et al 2004).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Algicidal microorganisms and secreted algicides: New tools to induce microalgal cell disruption

Demuez

González‐Fernández

Ballesteros

2015

Biotechnology Advances

126

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Initial Events Associated with Virus PBCV-1 Infection of Chlorella NC64A

Cited by 37 publications

References 53 publications

Paramecium bursaria Chlorella Virus 1 Proteome Reveals Novel Architectural and Regulatory Features of a Giant Virus

Paramecium bursaria Chlorella Virus 1 Proteome Reveals Novel Architectural and Regulatory Features of a Giant Virus

Three-dimensional structure and function of the Paramecium bursaria chlorella virus capsid

Algicidal microorganisms and secreted algicides: New tools to induce microalgal cell disruption

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