Human Polyomavirus

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Bernhard Ehlers - One of the best experts on this subject based on the ideXlab platform.

  • novel Polyomaviruses in shrews soricidae with close similarity to Human Polyomavirus 12
    Journal of General Virology, 2017
    Co-Authors: Alma Gedvilaite, Sebastien Calvignacspencer, Ugo Moens, Morten Tryland, Rainer G Ulrich, Julia Schneider, Vaida Kurmauskaite, Hannah Preugschas, Bernhard Ehlers
    Abstract:

    Shrews (family Soricidae) have already been reported to host microorganisms pathogenic for Humans. In an effort to search for additional infectious agents with zoonotic potential, we detected Polyomaviruses (PyVs) in common shrew, crowned shrew, and pygmy shrew (Sorex araneus, S. coronatus and S. minutus). From these, 11 full circular genomes were determined. Phylogenetic analysis based on large T protein sequences showed that these novel PyVs form a separate clade within the genus AlphaPolyomavirus. Within this clade, the phylogenetic relationships suggest host-virus co-divergence. Surprisingly, one PyV from common shrew showed a genomic sequence nearly identical to that of the Human Polyomavirus 12 (HPyV12). This indicated that HPyV12 is a variant of a non-Human PyV that naturally infects shrews. Whether HPyV12 is a bona fide Human-tropic Polyomavirus arising from a recent shrew-to-Human transmission event or instead reflects a technical artefact, such as consumable contamination with shrew material, needs further investigation.

  • Crystallographic and Glycan Microarray Analysis of Human Polyomavirus 9 VP1 Identifies N-Glycolyl Neuraminic Acid as a Receptor Candidate
    Journal of virology, 2014
    Co-Authors: Zaigham Mahmood Khan, Bernhard Ehlers, Yan Liu, Ursula Neu, Michel Gilbert, Ten Feizi, Thilo Stehle
    Abstract:

    Human Polyomavirus 9 (HPyV9) is a closely related homologue of simian B-lymphotropic Polyomavirus (LPyV). In order to define the architecture and receptor binding properties of HPyV9, we solved high-resolution crystal structures of its major capsid protein, VP1, in complex with three putative oligosaccharide receptors identified by glycan microarray screening. Comparison of the properties of HPyV9 VP1 with the known structure and glycan-binding properties of LPyV VP1 revealed that both viruses engage short sialylated oligosaccharides, but small yet important differences in specificity were detected. Surprisingly, HPyV9 VP1 preferentially binds sialyllactosamine compounds terminating in 5-N-glycolyl neuraminic acid (Neu5Gc) over those terminating in 5-N-acetyl neuraminic acid (Neu5Ac), whereas LPyV does not exhibit such a preference. The structural analysis demonstrated that HPyV9 makes specific contacts, via hydrogen bonds, with the extra hydroxyl group present in Neu5Gc. An equivalent hydrogen bond cannot be formed by LPyV VP1. IMPORTANCE The most common sialic acid in Humans is 5-N-acetyl neuraminic acid (Neu5Ac), but various modifications give rise to more than 50 different sialic acid variants that decorate the cell surface. Unlike most mammals, Humans cannot synthesize the sialic acid variant 5-N-glycolyl neuraminic acid (Neu5Gc) due to a gene defect. Humans can, however, still acquire this compound from dietary sources. The role of Neu5Gc in receptor engagement and in defining viral tropism is only beginning to emerge, and structural analyses defining the differences in specificity for Neu5Ac and Neu5Gc are still rare. Using glycan microarray screening and high-resolution protein crystallography, we have examined the receptor specificity of a recently discovered Human Polyomavirus, HPyV9, and compared it to that of the closely related simian Polyomavirus LPyV. Our study highlights critical differences in the specificities of both viruses, contributing to an enhanced understanding of the principles that underlie pathogen selectivity for modified sialic acids.

  • identification of a novel Human Polyomavirus in organs of the gastrointestinal tract
    PLOS ONE, 2013
    Co-Authors: Sarah Korup, Janita Rietscher, R Schmuck, Igor M. Sauer, Franziska Trusch, Sebastien Calvignacspencer, Sebastian Voigt, Ugo Moens, Jörg Hofmann, Bernhard Ehlers
    Abstract:

    Polyomaviruses are small, non-enveloped viruses with a circular double-stranded DNA genome. Using a generic Polyomavirus PCR targeting the VP1 major structural protein gene, a novel Polyomavirus was initially identified in resected Human liver tissue and provisionally named Human Polyomavirus 12 (HPyV12). Its 5033 bp genome is predicted to encode large and small T antigens and the 3 structural proteins VP1, VP2 and VP3. Phylogenetic analyses did not reveal a close relationship to any known Human or animal Polyomavirus. Investigation of organs, body fluids and excretions of diseased individuals and healthy subjects with both HPyV12-specific nested PCR and quantitative real-time PCR revealed additional virus-positive samples of resected liver, cecum and rectum tissues and a positive fecal sample. A capsomer-based IgG ELISA was established using the major capsid protein VP1 of HPyV12. Seroprevalences of 23% and 17%, respectively, were determined in sera from healthy adults and adolescents and a pediatric group of children. These data indicate that the virus naturally infects Humans and that primary infection may already occur in childhood.

  • Seroprevalence of Human Polyomavirus 9 and cross-reactivity to African green monkey-derived lymphotropic Polyomavirus
    Journal of General Virology, 2012
    Co-Authors: Franziska Trusch, Joachim E Kuhn, Jörg Hofmann, Marcus Klein, Tim Finsterbusch, Bernhard Ehlers
    Abstract:

    Human Polyomavirus 9 (HPyV9) was discovered recently in immunocompromised patients and shown to be genetically closely related to B-lymphotropic Polyomavirus (LPyV). No serological data are available for HPyV9, but Human antibodies against LPyV have been reported previously. To investigate the seroepidemiology of HPyV9 and the sero-cross-reactivity between HPyV9 and LPyV, a capsomer-based IgG ELISA was established using the major capsid protein VP1 of HPyV9 and LPyV. VP1 of an avian Polyomavirus was used as control. For HPyV9, a seroprevalence of 47 % was determined in healthy adults and adolescents (n = 328) and 20 % in a group of children (n = 101). In both groups, the seroreactivities for LPyV were less frequent and the ELISA titres of LPyV were lower. Of the HPyV9-reactive sera, 47 % reacted also with LPyV, and the titres for both PyVs correlated. Sera from African green monkeys, the natural hosts of LPyV, reacted also with both HPyV9 and LPyV, but here the HPyV9 titres were lower. This potential sero-cross-reactivity between HPyV9 and LPyV was confirmed by competition assays, and it was hypothesized that the reactivity of Human sera against LPyV may generally be due to cross-reactivity between HPyV9 and LPyV. The HPyV9 seroprevalence of liver transplant recipients and patients with neurological dysfunctions did not differ from that of age-matched controls, but a significantly higher seroprevalence was determined in renal and haematopoietic stem-cell transplant recipients, indicating that certain immunocompromised patient groups may be at a higher risk for primary infection with or for reactivation of HPyV9.

  • a novel Human Polyomavirus closely related to the african green monkey derived lymphotropic Polyomavirus
    Journal of Virology, 2011
    Co-Authors: Nelly Scuda, Peter Liman, Joachim E Kuhn, Hartmut Hengel, Sebastien Calvignacspencer, Klemens Ruprecht, Jörg Hofmann, Bernhard Ehlers
    Abstract:

    We identified a novel Human Polyomavirus from a kidney transplant patient under immunosuppressive treatment, by use of a generic PCR. The genome of the virus was completely amplified and sequenced. In phylogenetic analyses, it appeared as the closest relative to the African green monkey-derived lymphotropic Polyomavirus (LPV). Further investigation of clinical samples from immunocompromised patients with specific nested PCR revealed additional positive samples, indicating that the virus naturally infects Humans. The virus was tentatively named Human Polyomavirus 9 (HPyV9). The previously observed seroreactivity to LPV in Human populations might find a partial explanation in the circulation of HPyV9.

Gerald L. Stoner - One of the best experts on this subject based on the ideXlab platform.

  • 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
    Journal of Virology, 2000
    Co-Authors: Yukiko Shishidohara, Kazuo Nagashima, Yoshinobu Hara, Theresa A Larson, Kotaro Yasui, Gerald L. Stoner
    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.

  • phylogenetic analysis of 22 complete genomes of the Human Polyomavirus jc virus
    Journal of General Virology, 1998
    Co-Authors: David V Jobes, Caroline F. Ryschkewitsch, Sylvester C Chima, Gerald L. Stoner
    Abstract:

    The Polyomavirus JC (JCV) establishes a persistent infection in the kidneys, and is the virus agent that causes the demyelinating disease progressive multifocal leukoencephalopathy. PCR and DNA sequence analyses of partial JCV genomes have shown that there are at least four main JCV types, each associated with a specific geographical region. Type 1 is of European origin, Type 2 is Asian, Type 3 is found in individuals of African decent and Type 4 is a potential recombinant of Types 1 and 3, and is widely distributed throughout the population of the United States. A comprehensive phylogenetic analysis of 22 complete JCV genomes excluding part of the regulatory region was accomplished using neighbour-joining, UPGMA and maximum parsimony methods. The resulting UPGMA and parsimony phylogenies suggest that the European Type 1 strains diverged from the other types during the evolution of JCV and that each of the other genotypes (and subtypes) falls into well-supported clades. This is the first whole genome approach to phylogeny reconstruction for JCV and represents a significant improvement over earlier studies that were limited to partial JCV sequences and the neighbour-joining method.

  • Genotype profile of Human Polyomavirus JC excreted in urine of immunocompetent individuals.
    Journal of clinical microbiology, 1996
    Co-Authors: H T Agostini, Caroline F. Ryschkewitsch, Gerald L. Stoner
    Abstract:

    The Human Polyomavirus JC (JCV) causes the central demyelinating disease progressive multifocal leukoencephalopathy in about 5% of AIDS patients. To characterize the type profile of JCV in a control population in the United States, 54 females (10 to 79 years of age; average age, 43.4 years) and 51 males (18 to 94 years of age; average age, 47.9 years) were examined for the excretion of different genotypes of JCV in their urine by PCR followed by direct cycle sequencing. The group consisted of 89 patients of a general medical clinic in addition to 16 healthy volunteers. The overall incidence of JC viruria was 43 of 105 (40.9%) subjects, with a marked increase for those subjects above the age of 30 years. Two men were found to excrete two different types of JCV at the same time, indicating double infections. Of the three different genotypes of JCV identified to date, type 1 strains (European) were the most common in this cohort (64% of total strains) followed by type 2 (East Asian) (18%). No type 3 (East African) strains were detected. Indirect evidence for the existence of JCV type 3 was found in seven individuals (16%) in the form of a type 1/3 recombinant (also called type 4). In addition, a single example of JCV which differs from types 1, 2, and 3 and may represent a phylogenetically older type (type 5) was found in a 59-year-old African-American. Delineation of sequence variations between JCV types is essential for the design of primers for sensitive PCR with clinical samples.

  • Human Polyomavirus jc promoter enhancer rearrangement patterns from progressive multifocal leukoencephalopathy brain are unique derivatives of a single archetypal structure
    Journal of General Virology, 1993
    Co-Authors: Grace S Ault, Gerald L. Stoner
    Abstract:

    We have compared the promoter/enhancer structure of Human Polyomavirus JC (JCV) isolates from 11 progressive multifocal leukoencephalopathy brains. The duplications and deletions of the regulatory region were different in each patient, and usually only one sequence was found in each. The sites of strand breakage in the promoter were not random; four or five preferred sites or areas exist. Alignment of the JCV prototype Mad-1 regulatory region with the unduplicated archetypal structure defines six blocks of sequence, A to F. The preferred sites of strand breaks delineate these regions, although Mad-1 is an unusual promoter containing a break site not observed in other isolates, and an additional site is targeted in several promoters. Region A, containing the TATA box, and the first half of region C, containing several enhancer elements, and region E are consistently retained. Region B, the 23 bp insertion in the archetypal structure (relative to Mad-1) was also retained in all 11 isolates. Region D, the 66 bp insertion, was retained in isolates from three patients. Regions A and D were never duplicated, whereas regions C and E usually were duplicated or triplicated. Variation in the exact point of breakage within the preferred sites, alternative use of the sites in individual promoters and occasional short deletions at other sites result in sequences that are unique in each case. At the same time, the limited choice of break sites and the characteristic fates of the regions themselves result in three broad patterns of repeat sequences. The patterns do not correspond to the viral genotypes 1 and 2 defined by coding region base changes, and do not appear to be a stable feature of the virus. Rather, rearrangements appear to be generated in the host from a basic archetypal sequence.

Kamel Khalili - One of the best experts on this subject based on the ideXlab platform.

  • Detection of Human Polyomavirus Proteins, T-Antigen and Agnoprotein, in Human Tumor Tissue Arrays
    Journal of medical virology, 2010
    Co-Authors: Luís J. Del Valle, Kamel Khalili
    Abstract:

    Expression of the Human Polyomavirus JCV genome in several experimental animals induces a variety of neural origin tumors. The viral proteins, T-antigen and Agnoprotein, contribute to the oncogenesis of JCV by associating with several tumor suppressor proteins and dysregulating signaling pathways, which results in uncontrolled cell proliferation. In addition, T-antigen and Agnoprotein have been associated with DNA damage and interfering with DNA repair mechanisms. In this study, we have utilized commercially available tissue arrays of Human tumors of various origins and demonstrated the expression of both T-antigen and Agnoprotein in some, but not all, tumors of neural and non-neural origin. Most notably, more than 40% of Human glioblastomas and greater than 30% of colon adenocarcinomas express viral proteins. The detection of viral transforming proteins, T-antigen and Agnoprotein in the absence of viral capsid proteins suggests a role for JCV in the development and/or progression of Human tumors. These results invite further large-scale investigation on the role of Polyomaviruses, particularly JCV in the pathogenesis of Human cancer.

  • association of Human Polyomavirus jcv with colon cancer evidence for interaction of viral t antigen and β catenin
    Cancer Research, 2002
    Co-Authors: Sahnila Enam, Luís J. Del Valle, Cesar Lara, Carlos Ortizhidalgo, Daidi Gan, Juan P Palazzo, Kamel Khalili
    Abstract:

    Infection of the gastrointestinal tract by the Human Polyomavirus, JCV, which has been frequently detected in raw urban sewage, can occur via intake of contaminated water and food. In light of earlier reports on the tumorigenecity of JCV, we investigated the presence of the JCV genome and the expression of viral proteins in a collection of 27 well-characterized epithelial malignant tumors of the large intestine. Results from gene amplification revealed the presence of the viral early genome in 22 of 27 samples. Expression of the viral oncogenic early protein, T-antigen, and the late auxiliary protein, Agnoprotein, was observed in >50% of the samples. The absence of the viral capsid protein in the tumor cells excludes productive replication of the virus in neoplastic cells. Laser capture microdissection confirmed the presence of the JCV genome and expression of T-antigen in precancerous villous adenomas and regions of invasive adenocarcinoma. The ability of JCV T-antigen to interact with β-catenin and the nuclear detection of β-catenin in T-antigen-positive cells suggests dysregulation of the Wnt pathway in the tumor cells. The coproduction of T-antigen and β-catenin in colon cancer cells enhanced transcription of the c-myc promoter, the downstream target of β-catenin. These observations provide evidence for a possible association of JCV with colon cancer and suggest a novel regulatory role for T-antigen in the deregulation of the Wnt signaling pathway through β-catenin in tumors of the gastrointestinal tract.

  • association of Human Polyomavirus jcv with colon cancer evidence for interaction of viral t antigen and beta catenin
    Cancer Research, 2002
    Co-Authors: Sahnila Enam, Luís J. Del Valle, Cesar Lara, Carlos Ortizhidalgo, Daidi Gan, Juan P Palazzo, Kamel Khalili
    Abstract:

    Infection of the gastrointestinal tract by the Human Polyomavirus, JCV, which has been frequently detected in raw urban sewage, can occur via intake of contaminated water and food. In light of earlier reports on the tumorigenecity of JCV, we investigated the presence of the JCV genome and the expression of viral proteins in a collection of 27 well-characterized epithelial malignant tumors of the large intestine. Results from gene amplification revealed the presence of the viral early genome in 22 of 27 samples. Expression of the viral oncogenic early protein, T-antigen, and the late auxiliary protein, Agnoprotein, was observed in >50% of the samples. The absence of the viral capsid protein in the tumor cells excludes productive replication of the virus in neoplastic cells. Laser capture microdissection confirmed the presence of the JCV genome and expression of T-antigen in precancerous villous adenomas and regions of invasive adenocarcinoma. The ability of JCV T-antigen to interact with β-catenin and the nuclear detection of β-catenin in T-antigen-positive cells suggests dysregulation of the Wnt pathway in the tumor cells. The coproduction of T-antigen and β-catenin in colon cancer cells enhanced transcription of the c-myc promoter, the downstream target of β-catenin. These observations provide evidence for a possible association of JCV with colon cancer and suggest a novel regulatory role for T-antigen in the deregulation of the Wnt signaling pathway through β-catenin in tumors of the gastrointestinal tract.

  • physical and functional interaction between the y box binding protein yb 1 and Human Polyomavirus jc virus large t antigen
    Journal of Virology, 1999
    Co-Authors: Mahmut Safak, Kamel Khalili, Gary L Gallia, Sameer A Ansari
    Abstract:

    Y-box binding protein YB-1 is a member of a family of DNA and RNA binding proteins which have been shown to affect gene expression at both the transcriptional and translational levels. We have previously shown that YB-1 modulates transcription from the promoters of the ubiquitous Human Polyomavirus JC virus (JCV). Here we investigate the physical and functional interplay between YB-1 and the viral regulatory protein large T antigen (T-antigen), using JCV as a model system. Results of mobility band shift assays demonstrated that the efficiency of binding of YB-1 to a 23-bp single-stranded viral target sequence was significantly increased when T-antigen was included in the binding reaction mixture. Affinity chromatography and coimmunoprecipitation assays demonstrated that YB-1 and T-antigen physically interact with each other. Additionally, results of transcription studies demonstrated that these two proteins interact functionally on the JCV early and late gene promoters. Whereas ectopic expression of YB-1 and T-antigen results in synergistic transactivation of the viral late promoter, YB-1 alleviates T-antigen-mediated transcriptional suppression of the viral early promoter activity. Furthermore, we have localized, through the use of a series of deletion mutants, the sequences of these proteins which are important for their interaction. The T-antigen-interacting region of YB-1 is located in the cold shock domain of YB-1 and its immediate flanking sequences, and the YB-1-interacting domain of T-antigen maps to the carboxy-terminal half of T-antigen. Results of transient transfection assays with various YB-1 mutants and T-antigen expression constructs confirm the specificity of the functional interaction between YB-1 and T-antigen. Taken together, these data demonstrate that the cellular factor YB-1 and the viral regulatory protein T-antigen interact both physically and functionally and that this interaction modulates transcription from the JCV promoters.

Jörg Hofmann - One of the best experts on this subject based on the ideXlab platform.

  • identification of a novel Human Polyomavirus in organs of the gastrointestinal tract
    PLOS ONE, 2013
    Co-Authors: Sarah Korup, Janita Rietscher, R Schmuck, Igor M. Sauer, Franziska Trusch, Sebastien Calvignacspencer, Sebastian Voigt, Ugo Moens, Jörg Hofmann, Bernhard Ehlers
    Abstract:

    Polyomaviruses are small, non-enveloped viruses with a circular double-stranded DNA genome. Using a generic Polyomavirus PCR targeting the VP1 major structural protein gene, a novel Polyomavirus was initially identified in resected Human liver tissue and provisionally named Human Polyomavirus 12 (HPyV12). Its 5033 bp genome is predicted to encode large and small T antigens and the 3 structural proteins VP1, VP2 and VP3. Phylogenetic analyses did not reveal a close relationship to any known Human or animal Polyomavirus. Investigation of organs, body fluids and excretions of diseased individuals and healthy subjects with both HPyV12-specific nested PCR and quantitative real-time PCR revealed additional virus-positive samples of resected liver, cecum and rectum tissues and a positive fecal sample. A capsomer-based IgG ELISA was established using the major capsid protein VP1 of HPyV12. Seroprevalences of 23% and 17%, respectively, were determined in sera from healthy adults and adolescents and a pediatric group of children. These data indicate that the virus naturally infects Humans and that primary infection may already occur in childhood.

  • Seroprevalence of Human Polyomavirus 9 and cross-reactivity to African green monkey-derived lymphotropic Polyomavirus
    Journal of General Virology, 2012
    Co-Authors: Franziska Trusch, Joachim E Kuhn, Jörg Hofmann, Marcus Klein, Tim Finsterbusch, Bernhard Ehlers
    Abstract:

    Human Polyomavirus 9 (HPyV9) was discovered recently in immunocompromised patients and shown to be genetically closely related to B-lymphotropic Polyomavirus (LPyV). No serological data are available for HPyV9, but Human antibodies against LPyV have been reported previously. To investigate the seroepidemiology of HPyV9 and the sero-cross-reactivity between HPyV9 and LPyV, a capsomer-based IgG ELISA was established using the major capsid protein VP1 of HPyV9 and LPyV. VP1 of an avian Polyomavirus was used as control. For HPyV9, a seroprevalence of 47 % was determined in healthy adults and adolescents (n = 328) and 20 % in a group of children (n = 101). In both groups, the seroreactivities for LPyV were less frequent and the ELISA titres of LPyV were lower. Of the HPyV9-reactive sera, 47 % reacted also with LPyV, and the titres for both PyVs correlated. Sera from African green monkeys, the natural hosts of LPyV, reacted also with both HPyV9 and LPyV, but here the HPyV9 titres were lower. This potential sero-cross-reactivity between HPyV9 and LPyV was confirmed by competition assays, and it was hypothesized that the reactivity of Human sera against LPyV may generally be due to cross-reactivity between HPyV9 and LPyV. The HPyV9 seroprevalence of liver transplant recipients and patients with neurological dysfunctions did not differ from that of age-matched controls, but a significantly higher seroprevalence was determined in renal and haematopoietic stem-cell transplant recipients, indicating that certain immunocompromised patient groups may be at a higher risk for primary infection with or for reactivation of HPyV9.

  • a novel Human Polyomavirus closely related to the african green monkey derived lymphotropic Polyomavirus
    Journal of Virology, 2011
    Co-Authors: Nelly Scuda, Peter Liman, Joachim E Kuhn, Hartmut Hengel, Sebastien Calvignacspencer, Klemens Ruprecht, Jörg Hofmann, Bernhard Ehlers
    Abstract:

    We identified a novel Human Polyomavirus from a kidney transplant patient under immunosuppressive treatment, by use of a generic PCR. The genome of the virus was completely amplified and sequenced. In phylogenetic analyses, it appeared as the closest relative to the African green monkey-derived lymphotropic Polyomavirus (LPV). Further investigation of clinical samples from immunocompromised patients with specific nested PCR revealed additional positive samples, indicating that the virus naturally infects Humans. The virus was tentatively named Human Polyomavirus 9 (HPyV9). The previously observed seroreactivity to LPV in Human populations might find a partial explanation in the circulation of HPyV9.

Joachim E Kuhn - One of the best experts on this subject based on the ideXlab platform.

  • Seroprevalence of Human Polyomavirus 9 and cross-reactivity to African green monkey-derived lymphotropic Polyomavirus
    Journal of General Virology, 2012
    Co-Authors: Franziska Trusch, Joachim E Kuhn, Jörg Hofmann, Marcus Klein, Tim Finsterbusch, Bernhard Ehlers
    Abstract:

    Human Polyomavirus 9 (HPyV9) was discovered recently in immunocompromised patients and shown to be genetically closely related to B-lymphotropic Polyomavirus (LPyV). No serological data are available for HPyV9, but Human antibodies against LPyV have been reported previously. To investigate the seroepidemiology of HPyV9 and the sero-cross-reactivity between HPyV9 and LPyV, a capsomer-based IgG ELISA was established using the major capsid protein VP1 of HPyV9 and LPyV. VP1 of an avian Polyomavirus was used as control. For HPyV9, a seroprevalence of 47 % was determined in healthy adults and adolescents (n = 328) and 20 % in a group of children (n = 101). In both groups, the seroreactivities for LPyV were less frequent and the ELISA titres of LPyV were lower. Of the HPyV9-reactive sera, 47 % reacted also with LPyV, and the titres for both PyVs correlated. Sera from African green monkeys, the natural hosts of LPyV, reacted also with both HPyV9 and LPyV, but here the HPyV9 titres were lower. This potential sero-cross-reactivity between HPyV9 and LPyV was confirmed by competition assays, and it was hypothesized that the reactivity of Human sera against LPyV may generally be due to cross-reactivity between HPyV9 and LPyV. The HPyV9 seroprevalence of liver transplant recipients and patients with neurological dysfunctions did not differ from that of age-matched controls, but a significantly higher seroprevalence was determined in renal and haematopoietic stem-cell transplant recipients, indicating that certain immunocompromised patient groups may be at a higher risk for primary infection with or for reactivation of HPyV9.

  • a novel Human Polyomavirus closely related to the african green monkey derived lymphotropic Polyomavirus
    Journal of Virology, 2011
    Co-Authors: Nelly Scuda, Peter Liman, Joachim E Kuhn, Hartmut Hengel, Sebastien Calvignacspencer, Klemens Ruprecht, Jörg Hofmann, Bernhard Ehlers
    Abstract:

    We identified a novel Human Polyomavirus from a kidney transplant patient under immunosuppressive treatment, by use of a generic PCR. The genome of the virus was completely amplified and sequenced. In phylogenetic analyses, it appeared as the closest relative to the African green monkey-derived lymphotropic Polyomavirus (LPV). Further investigation of clinical samples from immunocompromised patients with specific nested PCR revealed additional positive samples, indicating that the virus naturally infects Humans. The virus was tentatively named Human Polyomavirus 9 (HPyV9). The previously observed seroreactivity to LPV in Human populations might find a partial explanation in the circulation of HPyV9.