scholarly journals Synthesis of Viral DNA and Late Capsid Protein L1 in Parabasal Spinous Cell Layers of Naturally Occurring Benign Warts Infected with Human Papillomavirus Type 1

Virology ◽  
2000 ◽  
Vol 268 (2) ◽  
pp. 281-293 ◽  
Author(s):  
Kiyofumi Egawa ◽  
Angelika Iftner ◽  
John Doorbar ◽  
Yumi Honda ◽  
Thomas Iftner
Keyword(s):  
Human Papillomavirus ◽  
Capsid Protein ◽  
Viral Dna ◽  
Naturally Occurring ◽  
Cell Layers

scholarly journals Identification of a Dynein Interacting Domain in the Papillomavirus Minor Capsid Protein L2

2006 ◽  
Vol 80 (13) ◽  
pp. 6691-6696 ◽  
Author(s):  
Luise Florin ◽  
Katrin A. Becker ◽  
Carsten Lambert ◽  
Thorsten Nowak ◽  
Cornelia Sapp ◽  
...  
Keyword(s):  
Amino Acids ◽  
Human Papillomavirus ◽  
Capsid Protein ◽  
Viral Genome ◽  
Promyelocytic Leukemia ◽  
Protein Bodies ◽  
Viral Dna ◽  
Microtubule Network ◽  
Promyelocytic Leukemia Protein ◽  
Minor Capsid Protein

ABSTRACT Papillomaviruses enter cells via endocytosis (H. C. Selinka et al., Virology 299:279-287, 2002). After egress from endosomes, the minor capsid protein L2 accompanies the viral DNA to the nucleus and subsequently to the subnuclear promyelocytic leukemia protein bodies (P. M. Day et al., Proc. Natl. Acad. Sci. USA 101:14252-14257, 2004), suggesting that this protein may be involved in the intracytoplasmic transport of the viral genome. We now demonstrate that the L2 protein is able to interact with the microtubule network via the motor protein dynein. L2 protein was found attached to microtubules after uncoating of incoming human papillomavirus pseudovirions. Based on immunofluorescence and coimmunoprecipitation analyses, the L2 region interacting with dynein is mapped to the C-terminal 40 amino acids. Mutations within this region abrogating the L2/dynein interaction strongly reduce the infectivity of pseudoviruses, indicating that this interaction mediates the minus-end-directed transport of the viral genome along microtubules towards the nucleus.

scholarly journals Monoclonal Antibodies to the Major Capsid Protein of Human Papillomavirus Type 1

1984 ◽  
Vol 65 (8) ◽  
pp. 1319-1324 ◽  
Author(s):  
A. Roseto ◽  
P. Pothier ◽  
M.-C. Guillemin ◽  
J. Peries ◽  
F. Breitburd ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Human Papillomavirus ◽  
Capsid Protein ◽  
Major Capsid Protein

scholarly journals Herpesvirus Capsid Association with the Nuclear Pore Complex and Viral DNA Release Involve the Nucleoporin CAN/Nup214 and the Capsid Protein pUL25

2009 ◽  
Vol 83 (13) ◽  
pp. 6610-6623 ◽  
Author(s):  
David Pasdeloup ◽  
Danielle Blondel ◽  
Anabela L. Isidro ◽  
Frazer J. Rixon
Keyword(s):  
Capsid Protein ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Cellular Interactions ◽  
Viral Dna ◽  
Microtubule Network ◽  
Infected Cells ◽  
Dna Release ◽  
Simplex Virus

ABSTRACT After penetrating the host cell, the herpesvirus capsid is transported to the nucleus along the microtubule network and docks to the nuclear pore complex before releasing the viral DNA into the nucleus. The viral and cellular interactions involved in the docking process are poorly characterized. However, the minor capsid protein pUL25 has recently been reported to be involved in viral DNA uncoating. Here we show that herpes simplex virus type 1 (HSV-1) capsids interact with the nucleoporin CAN/Nup214 in infected cells and that RNA silencing of CAN/Nup214 delays the onset of viral DNA replication in the nucleus. We also show that pUL25 interacts with CAN/Nup214 and another nucleoporin, hCG1, and binds to the pUL36 and pUL6 proteins, two other components of the herpesvirus particle that are known to be important for the initiation of infection and viral DNA release. These results identify CAN/Nup214 as being a nuclear receptor for the herpesvirus capsid and pUL25 as being an interface between incoming capsids and the nuclear pore complex and as being a triggering element for viral DNA release into the nucleus.

scholarly journals Naturally occurring capsid protein variants L1 of human papillomavirus genotype 16 in Morocco

2017 ◽  
Vol 13 (08) ◽  
pp. 241-248 ◽  
Author(s):  
Aissam El-Aliani ◽  
◽  
My Abdelaziz El Alaoui ◽  
Imane Chaoui ◽  
My Mustapha Ennaji ◽  
...  
Keyword(s):  
Human Papillomavirus ◽  
Capsid Protein ◽  
Naturally Occurring ◽  
Protein Variants

scholarly journals Comprehensive Assessment of the Antigenic Impact of Human Papillomavirus Lineage Variation on Recognition by Neutralizing Monoclonal Antibodies Raised against Lineage A Major Capsid Proteins of Vaccine-Related Genotypes

2020 ◽  
Vol 94 (24) ◽  
Author(s):  
Anna Godi ◽  
Dolcibella Boampong ◽  
Busayo Elegunde ◽  
Kavita Panwar ◽  
Maxime Fleury ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Human Papillomavirus ◽  
Capsid Protein ◽  
Capsid Proteins ◽  
Antigenic Determinants ◽  
Epithelial Cancers ◽  
Naturally Occurring ◽  
Hpv Genotypes ◽  
The Impact ◽  
Oncogenic Hpv

ABSTRACT Human papillomavirus (HPV) is the causative agent of cervical and other epithelial cancers. Naturally occurring variants of HPV have been classified into lineages and sublineages based on their whole-genome sequences, but little is known about the impact of this diversity on the structure and function of viral gene products. The HPV capsid is an icosahedral lattice comprising 72 pentamers of the major capsid protein (L1) and the associated minor capsid protein (L2). We investigated the potential impact of this genome variation on the capsid antigenicity of lineage and sublineage variants of seven vaccine-relevant, oncogenic HPV genotypes by using a large panel of monoclonal antibodies (MAbs) raised against the L1 proteins of lineage A antigens. Each genotype had at least one variant that displayed a ≥4-fold reduced neutralizing antibody sensitivity against at least one MAb, demonstrating that naturally occurring variation can affect one or more functional antigenic determinants on the HPV capsid. For HPV16, HPV18, HPV31, and HPV45, the overall impact was of a low magnitude. For HPV33 (sublineages A2 and A3 and lineages B and C), HPV52 (lineage D), and HPV58 (lineage C), however, variant residues in the indicated lineages and sublineages reduced their sensitivity to neutralization by all MAbs by up to 1,000-fold, suggesting the presence of key antigenic determinants on the surface of these capsids. These determinants were resolved further by site-directed mutagenesis. These data improve our understanding of the impact of naturally occurring variation on the antigenicity of the HPV capsid of vaccine-relevant oncogenic HPV genotypes. IMPORTANCE Human papillomavirus (HPV) is the causative agent of cervical and some other epithelial cancers. HPV vaccines generate functional (neutralizing) antibodies that target the virus particles (or capsids) of the most common HPV cancer-causing genotypes. Each genotype comprises variant forms that have arisen over millennia and which include changes within the capsid proteins. In this study, we explored the potential for these naturally occurring variant capsids to impact recognition by neutralizing monoclonal antibodies. All genotypes included at least one variant form that exhibited reduced recognition by at least one antibody, with some genotypes affected more than others. These data highlight the impact of naturally occurring variation on the structure of the HPV capsid proteins of vaccine-relevant oncogenic HPV genotypes.

scholarly journals Low-Level Secretion of Human Hepatitis B Virus Virions Caused by Two Independent, Naturally Occurring Mutations (P5T and L60V) in the Capsid Protein

2000 ◽  
Vol 74 (19) ◽  
pp. 9099-9105 ◽  
Author(s):  
Sophie Le Pogam ◽  
Thomas Ta-Tung Yuan ◽  
Gautam Kumar Sahu ◽  
Soma Chatterjee ◽  
Chiaho Shih
Keyword(s):  
Amino Acid ◽  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Capsid Protein ◽  
Core Protein ◽  
Wild Type Virus ◽  
Viral Dna ◽  
Naturally Occurring ◽  
Human Hepatitis ◽  
B Virus

ABSTRACT The functional significance of naturally occurring variants of human hepatitis B virus (HBV) remains largely unknown. Previously, we reported an immature secretion phenotype caused by a highly frequent mutation at amino acid 97 of the HBV core (capsid) protein (HBcAg). This phenotype is characterized by a nonselective and excessive secretion of virions containing an immature genome of single-stranded viral DNA. To extend our study of virion secretion to other naturally occurring variants, we have characterized mutations at HBcAg codons 5, 38, and 60 via site-directed mutagenesis. Although the phenotype of the mutation at codon 38 is nearly identical to that for the wild-type virus, our study reveals that a single mutation at codon 5 or 60 exhibits a new extracellular phenotype with significantly reduced virion secretion yet maintains normal intracellular viral DNA replication. A complementation study indicates that the mutant core protein alone is sufficient for the “low-secretion” phenotype. Furthermore, the low-secretion phenotype of the codon 5 mutant appears to be induced by the loss of a parental proline residue, rather than by the gain of a new amino acid. Our study underscores the core protein as another crucial determinant in virion secretion, in addition to the known envelope proteins. Our present results suggest that a very precise structure of both α-helical and nonhelical loop regions of the entire HBcAg molecule is important for virion secretion. The low-secretion variants may contribute to the phenomenon of gradually decreasing viremia in chronic carriers during the late phase of persistent infection.

scholarly journals Human Papillomavirus Major Capsid Protein L1 Remains Associated with the Incoming Viral Genome throughout the Entry Process

2017 ◽  
Vol 91 (16) ◽  
Author(s):  
Stephen DiGiuseppe ◽  
Malgorzata Bienkowska-Haba ◽  
Lucile G. M. Guion ◽  
Timothy R. Keiffer ◽  
Martin Sapp
Keyword(s):  
Human Papillomavirus ◽  
Capsid Protein ◽  
Conformational Changes ◽  
Viral Genome ◽  
Neutralizing Antibodies ◽  
Major Capsid Protein ◽  
Mitotic Chromosomes ◽  
Viral Dna ◽  
Minor Capsid Protein ◽  
L1 Protein

ABSTRACT During infectious entry, acidification within the endosome triggers uncoating of the human papillomavirus (HPV) capsid, whereupon host cyclophilins facilitate the release of most of the major capsid protein, L1, from the minor capsid protein L2 and the viral genome. The L2/DNA complex traffics to the trans-Golgi network (TGN). After the onset of mitosis, HPV-harboring transport vesicles bud from the TGN, followed by association with mitotic chromosomes. During this time, the HPV genome remains in a vesicular compartment until the nucleus has completely reformed. Recent data suggest that while most of L1 protein dissociates and is degraded in the endosome, some L1 protein remains associated with the viral genome. The L1 protein has DNA binding activity, and the L2 protein has multiple domains capable of interacting with L1 capsomeres. In this study, we report that some L1 protein traffics with L2 and viral genome to the nucleus. The accompanying L1 protein is mostly full length and retains conformation-dependent epitopes, which are recognized by neutralizing antibodies. Since more than one L1 molecule contributes to these epitopes and requires assembly into capsomeres, we propose that L1 protein is present in the form of pentamers. Furthermore, we provide evidence that the L1 protein interacts directly with viral DNA within the capsid. Based on our findings, we propose that the L1 protein, likely arranged as capsomeres, stabilizes the viral genome within the subviral complex during intracellular trafficking. IMPORTANCE After internalization, the nonenveloped human papillomavirus virion uncoats in the endosome, whereupon conformational changes result in a dissociation of a subset of the major capsid protein L1 from the minor capsid protein L2, which remains in complex with the viral DNA. Recent data suggest that some L1 protein may accompany the viral genome beyond the endosomal compartment. We demonstrate that conformationally intact L1 protein, likely still arranged as capsomeres, remains associated with the incoming viral genome throughout mitosis and transiently resides in the nucleus until after the viral DNA is released from the transport vesicle.

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