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  • 1.
    Ekström, Jens-Ola
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Tolf, Conny
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Fahlgren, Camilla
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Johansson, Susanne
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Arbrandt, Gustav
    Apodemus, Stockholm.
    Niklasson, Bo
    Apodemus, Stockholm.
    Edman, Kjell
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lindberg, A. Michael
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Replication of Ljungan virus in cell culture: The genomic 5'-end, infectious cDNA clones and host cell response to viral infections2007In: Virus Research, ISSN 0168-1702, E-ISSN 1872-7492, Vol. 130, no December 2007, p. 129-139Article in journal (Refereed)
    Abstract [en]

    Ljungan virus (LV) is a picornavirus recently isolated from bank voles (Clethrionomys glareolus). The previously uncharacterised 5'-end sequence of the LV genome was determined. Infectious cDNA clones were constructed of the wild type LV prototype strain 87-012 and of the cytolytically replicating cell cultureadapted variant 87-012G. Virus generated from cDNA clones showed identical growth characteristics as uncloned virus stocks. Cell culture adapted LV, 87-012G, showed a clear cytopathic effect (CPE) at 3-4 days post-infection (p.i.). Virus titers, determined by plaque titration, increased however only within the first 18 h p.i. Replication of LV (+) strand RNA was determined by real-time PCR and corresponded in time with increasing titers. In contrast, the amounts of thereplication intermediate, the (-) strand, continued to increase until the cells showed CPE. This indicates separate controlling mechanisms for replication of LV (+) and (-) genome strands. Replication was also monitored by immunofluorescence (IF) staining. IF staining of both prototype 87-012 and the CPE causing 87-012G showed groups of 5-25 infected cells at 48 h p.i., suggesting a, for picornaviruses, not previously described direct cell-to-cell transmission.

  • 2.
    Israelsson, Stina
    et al.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Gullberg, Maria
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Jonsson, Nina
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Roivainen, Merja
    Edman, Kjell
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Lindberg, A. Michael
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Studies of Echovirus 5 interactions with the cell surface: Heparan sulfate mediates attachment to the host cell.2010In: Virus Research, ISSN 0168-1702, E-ISSN 1872-7492, Vol. 151, no 2, p. 170-176Article in journal (Refereed)
    Abstract [en]

    Infections caused by Echovirus 5 (E5), an enterovirus of the Picornaviridae family, have been associated with fever, rashes and sporadic cases of aseptic meningitis. To elucidate the receptor usage of this virus, the significance of a previously proposed integrin binding arginine-glycine-aspartic acid (RGD) motif found in the VP3 capsid protein was investigated, as well as the capacity of E5 to interact with heparan sulfate on the cell surface. Using the prototype strain E5 Noyce (E5N), an E5N mutant where the aspartic acid of the RGD motif has been substituted to a glutamic acid and clinical E5 isolates, the RGD motif of VP3 was found to be non-essential and hence not involved in integrin receptor binding. However, E5N and clinical E5 isolates interact with heparan sulfate at the cell surface, as demonstrated by virus replication inhibition assays using heparin and heparinase III, and studies of E5 interactions at the cell surface measured by real-time PCR analysis. In conclusion, E5 utilizes heparan sulfate as a cellular receptor, but the RGD motif of VP3 is not essential for E5 infectivity.

  • 3.
    Polacek, Charlotta
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ekström, Jens-Ola
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lundgren, Anneli
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lindberg, A Michael
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Cytolytic replication of coxsackievirus B2 in CAR-deficient rhabdomyosarcoma cells.2005In: Virus Research, ISSN 0168-1702, E-ISSN 1872-7492, Vol. 113, no 2, p. 107-15Article in journal (Refereed)
    Abstract [en]

    The six coxsackievirus B serotypes (CVB1-6) use the coxsackie- and adenovirus receptor (CAR) for host cell entry. Four of these serotypes, CVB1, 3, 5 and 6, have also shown the capacity to replicate and cause cytolysis in rhabdomyosarcoma (RD) cells, a CAR-deficient cell line. This extended tropism has been associated with an acquired ability to bind decay accelerating factor (DAF). In this study, we have adapted the CVB2 prototype strain Ohio-1 (CVB2/O) to replicate in RD cells. Two types of infection were identified: (I) an enterovirus-typical, lytic infection, and (II) a non-lytic infection. Both CVB2/O-RD variants retained the prototype-ability to cause cytopathic effect in HeLa cells using CAR as receptor. Phenotypic and genotypic changes in the CVB2/O-RD-variants were determined and compared to the prototype cultured in HeLa cells. Inhibition studies using antibodies against CAR and DAF revealed a maintained ability of the CVB2/O-RD-variants to bind CAR, but no binding to DAF was observed. In addition, neither the prototype nor the CVB2/O-RD-variants were able to cause hemagglutination in human red blood cells, an enterovirus feature associated with affinity for DAF. Sequence analysis of the CVB2/O-RD-variants showed acquired mutations in the capsid region, suggesting extended receptor usage towards an alternative, yet unidentified, receptor for CVB2.

  • 4.
    Truchado, Daniel A.
    et al.
    Univ Complutense Madrid, Spain.
    Williams, Richard A. J.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Biology and Environmental Science. Univ Complutense Madrid, Spain.
    Benitez, Laura
    Univ Complutense Madrid, Spain.
    Natural history of avian papillomaviruses2018In: Virus Research, ISSN 0168-1702, E-ISSN 1872-7492, Vol. 252, p. 58-67Article, review/survey (Refereed)
    Abstract [en]

    Papillomaviruses (Family: Papillomaviridae) are small non-enveloped viruses that cause skin and mucosa infections in diverse vertebrates. The vast majority have been detected in mammals. However, the number of papillomaviruses described in birds is growing, especially because of metagenomic studies. Seven complete genomes and one partial sequence have been described, corresponding to five papillomavirus genera. These have been detected from various sample types, including skin, internal epithelium, and faecal material, from seven highly diverse wild and captive avian species. This review summarizes the molecular epidemiology of avian papillomaviruses, their genomic organization, evolutionary history and diagnostic techniques used for detection. The most commonly detected avian papillomavirus lesions are cauliflower-shaped papillomas, or warts, found on the tarsus and digits of common chaffinch (Fringilla coelebs) and occasionally brambling (Fringilla montifringilla). Similar warty growths have been detected in African grey parrot (Psittacus erithacus) and northern fulmar (Fulmarus glacialis), on the head and the foot, respectively. Papillomavirus has also been detected in avian tissue with no apparent lesions, similar to findings in humans and other mammals. Papillomavirus involvement was initially suspected to cause other types of lesions, such as internal papillomatosis of parrots (IPP) and proliferative pododermatitis in waterfowl. However, determined efforts failed to demonstrate papillomavirus presence. We briefly describe avian papillomavirus genomic organization and viral gene diversity. Furthermore, we performed a detailed analysis of avian papillomavirus non-coding regions and a preliminary computational analysis of their E9 proteins.

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