scholarly journals Novel Polyomavirus Detected in the Feces of a Chimpanzee by Nested Broad-Spectrum PCR

2005 ◽  
Vol 79 (6) ◽  
pp. 3883-3887 ◽  
Author(s):  
Reimar Johne ◽  
Dirk Enderlein ◽  
Hermann Nieper ◽  
Hermann Müller
Keyword(s):  
Pan Troglodytes ◽  
Broad Spectrum ◽  
Animal Species ◽  
Major Capsid Protein ◽  
Human Polyomavirus ◽  
Jc Polyomavirus ◽  
Distinct Virus ◽  
Field Samples ◽  
Polyomavirus Jc ◽  
Capsid Protein Vp1

ABSTRACT In order to screen for new polyomaviruses in samples derived from various animal species, degenerated PCR primer pairs were constructed. By using a nested PCR protocol, the sensitive detection of nine different polyomavirus genomes was demonstrated. The screening of field samples revealed the presence of a new polyomavirus, tentatively designated chimpanzee polyomavirus (ChPyV), in the feces of a juvenile chimpanzee (Pan troglodytes). Analysis of the region encoding the major capsid protein VP1 revealed a unique insertion in the EF loop of the protein and showed that ChPyV is a distinct virus related to the monkey polyomavirus B-lymphotropic polyomavirus and the human polyomavirus JC polyomavirus.

scholarly journals Analysis of Capsid Formation of Human Polyomavirus JC (Tokyo-1 Strain) by a Eukaryotic Expression System: Splicing of Late RNAs, Translation and Nuclear Transport of Major Capsid Protein VP1, and Capsid Assembly

2000 ◽  
Vol 74 (4) ◽  
pp. 1840-1853 ◽  
Author(s):  
Yukiko Shishido-Hara ◽  
Yoshinobu Hara ◽  
Theresa Larson ◽  
Kotaro Yasui ◽  
Kazuo Nagashima ◽  
...  
Keyword(s):  
Nuclear Transport ◽  
Expression System ◽  
Eukaryotic Expression ◽  
Capsid Proteins ◽  
Human Polyomavirus ◽  
Reading Frame ◽  
Eukaryotic Expression System ◽  
Capsid Formation ◽  
Polyomavirus Jc ◽  
Capsid Protein Vp1

ABSTRACT Human polyomavirus JC (JCV) can encode the three capsid proteins VP1, VP2, and VP3, downstream of the agnoprotein in the late region. JCV virions are identified in the nucleus of infected cells. In this study, we have elucidated unique features of JCV capsid formation by using a eukaryotic expression system. Structures of JCV polycistronic late RNAs (M1 to M4 and possibly M5 and M6) generated by alternative splicing were determined. VP1 would be synthesized from M2 RNA, and VP2 and VP3 would be synthesized from M1 RNA. The presence of the open reading frame of the agnoprotein or the leader sequence (nucleotides 275 to 409) can decrease the expression level of VP1. VP1 was efficiently transported to the nucleus in the presence of VP2 and VP3 but distributed both in the cytoplasm and in the nucleus in their absence. Mutation analysis indicated that inefficiency in nuclear transport of VP1 is due to the unique structure in the N-terminal sequence, KRKGERK. Within the nucleus, VP1 was localized discretely and identified as speckles in the presence of VP2 and VP3 but distributed diffusely in their absence. These results suggest that VP1 was efficiently transported to the nucleus and localized in the discrete subnuclear regions, possibly with VP2 and VP3. By electron microscopy, recombinant virus particles were identified in the nucleus, and their intranuclear distribution was consistent with distribution of speckles. This system provides a useful model with which to understand JCV capsid formation and the structures and functions of the JCV capsid proteins.

scholarly journals New sequence polymorphisms in the outer loops of the JC polyomavirus major capsid protein (VP1) possibly associated with progressive multifocal leukoencephalopathy

2005 ◽  
Vol 86 (7) ◽  
pp. 2035-2045 ◽  
Author(s):  
Huai-Ying Zheng ◽  
Tomokazu Takasaka ◽  
Kazuyuki Noda ◽  
Akira Kanazawa ◽  
Hideo Mori ◽  
...  
Keyword(s):  
Amino Acid ◽  
Progressive Multifocal Leukoencephalopathy ◽  
Capsid Protein ◽  
Major Capsid Protein ◽  
Biological Significance ◽  
Jc Polyomavirus ◽  
Nucleotide Substitutions ◽  
Coding Sequences ◽  
Capsid Protein Vp1 ◽  
Surface Loops

JC polyomavirus (JCPyV) causes progressive multifocal leukoencephalopathy (PML) in patients with decreased immune competence. To elucidate genetic changes in JCPyV associated with the pathogenesis of PML, multiple complete JCPyV DNA clones originating from the brains of three PML cases were established and sequenced. Although unique rearranged control regions occurred in all clones, a low level of nucleotide variation was also found in the coding region. In each case, a parental coding sequence was identified, from which variant coding sequences with nucleotide substitutions would have been generated. A comparison between the parental and variant coding sequences demonstrated that all 12 detected nucleotide substitutions gave rise to amino acid changes. Interestingly, seven of these changes were located in the surface loops of the major capsid protein (VP1). Finally, 16 reported VP1 sequences of PML-type JCPyV (i.e. derived from the brain or cerebrospinal fluid of PML patients) were compared with their genotypic prototypes, generated as consensus sequences of representative archetypal isolates belonging to the same genotypes; 13 VP1 proteins had amino acid changes in the surface loops. In contrast, VP1 proteins from isolates from the urine of immunocompetent and immunosuppressed patients rarely underwent mutations in the VP1 loops. The present findings suggest that PML-type JCPyV frequently undergoes amino acid substitutions in the VP1 loops. These polymorphisms should serve as a new marker for the identification of JCPyV isolates associated with PML. The biological significance of these mutations, however, remains unclear.

Human polyomavirus JC variants in Papua New Guinea and Guam reflect ancient population settlement and viral evolution

2000 ◽  
Vol 2 (9) ◽  
pp. 987-996 ◽  
Author(s):  
Caroline F Ryschkewitsch ◽  
Jonathan S Friedlaender ◽  
Charles S Mgone ◽  
David V Jobes ◽  
Hansjürgen T Agostini ◽  
...  
Keyword(s):  
Papua New Guinea ◽  
Viral Evolution ◽  
New Guinea ◽  
Human Polyomavirus ◽  
Ancient Population ◽  
Polyomavirus Jc

T-antigen of the human polyomavirus JC attenuates faithful DNA repair by forcing nuclear interaction between IRS-1 and Rad51

2005 ◽  
Vol 206 (1) ◽  
pp. 35-46 ◽  
Author(s):  
Joanna Trojanek ◽  
Sidney Croul ◽  
Thu Ho ◽  
Jin Ying Wang ◽  
Armine Darbinyan ◽  
...  
Keyword(s):  
Dna Repair ◽  
Nuclear Interaction ◽  
T Antigen ◽  
Human Polyomavirus ◽  
Polyomavirus Jc

scholarly journals Early Events during BK Virus Entry and Disassembly

2008 ◽  
Vol 83 (3) ◽  
pp. 1350-1358 ◽  
Author(s):  
Mengxi Jiang ◽  
Johanna R. Abend ◽  
Billy Tsai ◽  
Michael J. Imperiale
Keyword(s):  
Bk Virus ◽  
Dominant Negative ◽  
Host Cells ◽  
Human Polyomavirus ◽  
Microtubule Network ◽  
Early Entry ◽  
Dominant Negative Form ◽  
Immunosuppressed Patients ◽  
Capsid Protein Vp1 ◽  
Cellular Components

ABSTRACT BK virus (BKV) is a nonenveloped, ubiquitous human polyomavirus that establishes a persistent infection in healthy individuals. It can be reactivated, however, in immunosuppressed patients and cause severe diseases, including polyomavirus nephropathy. The entry and disassembly mechanisms of BKV are not well defined. In this report, we characterized several early events during BKV infection in primary human renal proximal tubule epithelial (RPTE) cells, which are natural host cells for BKV. Our results demonstrate that BKV infection in RPTE cells involves an acidic environment relatively early during entry, followed by transport along the microtubule network to reach the endoplasmic reticulum (ER). A distinct disulfide bond isomerization and cleavage pattern of the major capsid protein VP1 was observed, which was also influenced by alterations in pH and disruption of trafficking to the ER. A dominant negative form of Derlin-1, an ER protein required for retro-translocation of certain misfolded proteins, inhibited BKV infection. Consistent with this, we detected an interaction between Derlin-1 and VP1. Finally, we show that proteasome function is also linked to BKV infection and capsid rearrangement. These results indicate that BKV early entry and disassembly are highly regulated processes involving multiple cellular components.

scholarly journals Genetic Analysis of the Major Capsid Protein of the Archaeal Fusellovirus SSV1: Mutational Flexibility and Conformational Change

2017 ◽  
Author(s):  
Eric A. Iverson ◽  
David A. Goodman ◽  
Madeline E. Gorchels ◽  
Kenneth M. Stedman
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Point Mutations ◽  
Site Directed Mutagenesis ◽  
Vp1 Gene ◽  
Capsid Protein Gene ◽  
Vp1 Protein ◽  
Transposon Insertion ◽  
N Terminus ◽  
Capsid Protein Vp1

Viruses with spindle or lemon-shaped virions are rare in the world of viruses, but are common in viruses of archaeal extremophiles, possibly due to the extreme conditions in which they thrive. However, the structural and genetic basis for the unique spindle shape is unknown. The best-studied spindle-shaped virus, SSV1, is composed mostly of the major capsid protein VP1. Similar to many other viruses, proteolytic cleavage of VP1 is thought to be critical for virion formation. Unlike half of the genes in SSV1, including the minor capsid protein gene vp3, the vp1 gene does not tolerate deletion or transposon insertion. In order determine the role of the vp1 gene and its proteolysis for virus function, we developed techniques for site-directed mutagenesis of the SSV1 genome and complemented deletion mutants with vp1 genes from other SSVs. By analyzing these mutants we demonstrate that the N-terminus of the VP1 protein is required, but the N-terminus, or entire SSV1 VP1 protein, can be exchanged with VP1s from other SSVs. However, the conserved glutamate at the cleavage site is not essential for infectivity. Interestingly, viruses containing point mutations at this position generate mostly abnormal virions.

scholarly journals Genetic Analysis of the Major Capsid Protein of the Archaeal Fusellovirus SSV1: Mutational Flexibility and Conformational Change

2017 ◽  
Author(s):  
Eric A. Iverson ◽  
David A. Goodman ◽  
Madeline E. Gorchels ◽  
Kenneth M. STEDMAN
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Point Mutations ◽  
Site Directed Mutagenesis ◽  
Vp1 Gene ◽  
Vp1 Protein ◽  
Transposon Insertion ◽  
N Terminus ◽  
Capsid Protein Vp1 ◽  
Virion Formation

Viruses with spindle or lemon-shaped virions are rare in the world of viruses, but are common in viruses of archaeal extremophiles, possibly due to the extreme conditions in which they thrive. However, the structural and genetic basis for the unique spindle shape is unknown. The best-studied spindle-shaped virus, SSV1, is composed mostly of the major capsid protein VP1. Similar to many other viruses, proteolytic cleavage of VP1 is thought to be critical for virion formation. Unlike half of the genes in SSV1, including the minor capsid protein VP3, the vp1 gene does not tolerate deletion or transposon insertion. In order determine the role of the vp1 gene and its proteolysis for virus function, we developed techniques for site-directed mutagenesis of the SSV1 genome and complemented deletion mutants with vp1 genes from other SSVs. By analyzing these mutants we demonstrate that the N-terminus of the VP1 protein is required, but the N-terminus, or entire SSV1 VP1 protein, can be exchanged with VP1s from other SSVs. However, the conserved glutamate at the cleavage site is not essential. Interestingly, viruses containing point mutations at this position generate mostly abnormal virions.

scholarly journals Virion assembly defect of polyomavirus hr-t mutants: underphosphorylation of major capsid protein VP1 before viral DNA encapsidation.

1985 ◽  
Vol 54 (2) ◽  
pp. 311-316 ◽  
Author(s):  
R L Garcea ◽  
K Ballmer-Hofer ◽  
T L Benjamin
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Viral Dna ◽  
Virion Assembly ◽  
Capsid Protein Vp1 ◽  
Assembly Defect
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