GLORIA

GEOMAR Library Ocean Research Information Access

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Online Resource
    Online Resource
    Microbiology Society ; 2013
    In:  Journal of General Virology Vol. 94, No. 5 ( 2013-05-01), p. 1039-1050
    In: Journal of General Virology, Microbiology Society, Vol. 94, No. 5 ( 2013-05-01), p. 1039-1050
    Abstract: Piscine reovirus (PRV) is a tentative new member of the family Reoviridae and has been linked to heart and skeletal muscle inflammation in farmed Atlantic salmon ( Salmo salar L.). Recent sequence-based evidence suggests that PRV is about equally related to members of the genera Orthoreovirus and Aquareovirus . Sequence similarities have also suggested that PRV might encode a fusion-associated small transmembrane (FAST) protein, which in turn suggests that PRV might be the prototype of a new genus with syncytium-inducing potential. In previous support of this designation has been the absence of identifiable PRV-encoded homologues of either the virion outer-clamp protein of ortho- and aquareoviruses or the virion outer-fibre protein of most orthoreoviruses. In the current report, we have provided experimental evidence that the putative p13 FAST protein of PRV lacks the defining feature of the FAST protein family – the ability to induce syncytium formation. Instead, p13 is the first example of a cytosolic, integral membrane protein encoded by ortho- or aquareoviruses, and induces cytotoxicity in the absence of cell–cell fusion. Sequence analysis also identified signature motifs of the outer-clamp and outer-fibre proteins of other reoviruses in two of the predicted PRV gene products. Based on these findings, we conclude that PRV does not encode a FAST protein and is therefore unlikely to be a new fusogenic reovirus. The presence of a novel integral membrane protein and two previously unrecognized, essential outer-capsid proteins has important implications for the biology, evolution and taxonomic classification of this virus.
    Type of Medium: Online Resource
    ISSN: 0022-1317 , 1465-2099
    RVK:
    RVK:
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2013
    detail.hit.zdb_id: 2007065-2
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 2
    Online Resource
    Online Resource
    Microbiology Society ; 2018
    In:  Journal of General Virology Vol. 99, No. 1 ( 2018-01-01), p. 17-18
    In: Journal of General Virology, Microbiology Society, Vol. 99, No. 1 ( 2018-01-01), p. 17-18
    Type of Medium: Online Resource
    ISSN: 0022-1317 , 1465-2099
    RVK:
    RVK:
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2018
    detail.hit.zdb_id: 2007065-2
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 3
    In: Journal of Virology, American Society for Microbiology, Vol. 89, No. 2 ( 2015-01-15), p. 1182-1194
    Abstract: Giardia lamblia virus (GLV) is a small, nonenveloped, nonsegmented double-stranded RNA (dsRNA) virus infecting Giardia lamblia , the most common protozoan pathogen of the human intestine and a major agent of waterborne diarrheal disease worldwide. GLV (genus Giardiavirus ) is a member of family Totiviridae , along with several other groups of protozoal or fungal viruses, including Leishmania RNA viruses and Trichomonas vaginalis viruses. Interestingly, GLV is more closely related than other Totiviridae members to a group of recently discovered metazoan viruses that includes penaeid shrimp infectious myonecrosis virus (IMNV). Moreover, GLV is the only known protozoal dsRNA virus that can transmit efficiently by extracellular means, also like IMNV. In this study, we used transmission electron cryomicroscopy and icosahedral image reconstruction to examine the GLV virion at an estimated resolution of 6.0 Å. Its outermost diameter is 485 Å, making it the largest totivirus capsid analyzed to date. Structural comparisons of GLV and other totiviruses highlighted a related “T=2” capsid organization and a conserved helix-rich fold in the capsid subunits. In agreement with its unique capacity as a protozoal dsRNA virus to survive and transmit through extracellular environments, GLV was found to be more thermoresistant than Trichomonas vaginalis virus 1, but no specific protein machinery to mediate cell entry, such as the fiber complexes in IMNV, could be localized. These and other structural and biochemical findings provide a basis for future work to dissect the cell entry mechanism of GLV into a “primitive” (early-branching) eukaryotic host and an important enteric pathogen of humans. IMPORTANCE Numerous pathogenic bacteria, including Corynebacterium diphtheriae , Salmonella enterica , and Vibrio cholerae , are infected with lysogenic bacteriophages that contribute significantly to bacterial virulence. In line with this phenomenon, several pathogenic protozoa, including Giardia lamblia , Leishmania species, and Trichomonas vaginalis are persistently infected with dsRNA viruses, and growing evidence indicates that at least some of these protozoal viruses can likewise enhance the pathogenicity of their hosts. Understanding of these protozoal viruses, however, lags far behind that of many bacteriophages. Here, we investigated the dsRNA virus that infects the widespread enteric parasite Giardia lamblia . Using electron cryomicroscopy and icosahedral image reconstruction, we determined the virion structure of Giardia lamblia virus, obtaining new information relating to its assembly, stability, functions in cell entry and transcription, and similarities and differences with other dsRNA viruses. The results of our study set the stage for further mechanistic work on the roles of these viruses in protozoal virulence.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2015
    detail.hit.zdb_id: 1495529-5
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 4
    Online Resource
    Online Resource
    American Society for Microbiology ; 2003
    In:  Journal of Virology Vol. 77, No. 24 ( 2003-12-15), p. 13361-13375
    In: Journal of Virology, American Society for Microbiology, Vol. 77, No. 24 ( 2003-12-15), p. 13361-13375
    Abstract: Cell entry by reoviruses requires a large, transcriptionally active subvirion particle to gain access to the cytoplasm. The features of this particle have been the subject of debate, but three pri mary candidates—the infectious subvirion particle (ISVP), ISVP*, and core particle forms—that differ in whether putative membrane penetration protein μ1 and adhesin σ1 remain particle bound have been identified. Experiments with antibody reagents in this study yielded new information about the steps in particle disassembly during cell entry. Monoclonal antibodies specific for the δ region of μ1 provided evidence for a conformational change inμ 1 and for release of the δ proteolytic fragment from entering particles. Antiserum raised against cores provided evidence for entry-related changes in particle structure and identified entering particles that largely lack the δ fragment inside cells. Antibodies specific for σ1 showed that it is also largely shed from entering particles. Limited coimmunostaining with markers for late endosomes and lysosomes indicated the particles lacking δ andσ 1 did not localize to those subcellular compartments, and other observations suggested that both the particles and free δ were released into the cytoplasm. Essentially equivalent findings were obtained with native ISVPs and highly infectious recoated particles containing wild-type proteins. Poorly infectious recoated particles containing a hyperstable mutant form of μ1, however, showed no evidence for the in vitro and intracellular changes in particle structure normally detected by antibodies, and these particles instead accumulated in late endosomes or lysosomes. Recoated particles with hyperstable μ1 were also ineffective at mediating erythrocyte lysis in vitro and promoting α-sarcin coentry and intoxication of cells in cultures. Based on these and other findings, we propose that ISVP* is a transient intermediate in cell entry which mediates membrane penetration and is then further uncoated in the cytoplasm to yield particles, resembling cores, that largely lack the δ fragment ofμ 1.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2003
    detail.hit.zdb_id: 1495529-5
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 5
    Online Resource
    Online Resource
    American Society for Microbiology ; 2004
    In:  Journal of Virology Vol. 78, No. 19 ( 2004-10), p. 10695-10705
    In: Journal of Virology, American Society for Microbiology, Vol. 78, No. 19 ( 2004-10), p. 10695-10705
    Abstract: Nonfusogenic mammalian orthoreovirus (reovirus) is an enteric pathogen of mice and a useful model for studies of how an enteric virus crosses the mucosal barrier of its host and is subject to control by the mucosal immune system. We recently generated and characterized a new murine immunoglobulin A (IgA)-class monoclonal antibody (MAb), 1E1, that binds to the adhesin fiber, σ1, of reovirus type 1 Lang (T1L) and thereby neutralizes the infectivity of that strain in cell culture. 1E1 is produced in hybridoma cultures as a mixture of monomers, dimers, and higher polymers and is protective against peroral challenges with T1L either when the MAb is passively administered or when it is secreted into the intestines of mice bearing subcutaneous hybridoma tumors. In the present study, selection and analysis of mutants resistant to neutralization by 1E1 identified the region of T1L σ1 to which the MAb binds. The region bound by a previously characterized type 1 σ1-specific neutralizing IgG MAb, 5C6, was identified in the same way. Each of the 15 mutants isolated and analyzed was found to be much less sensitive to neutralization by either 1E1 or 5C6, suggesting the two MAbs bind to largely overlapping regions of σ1. The tested mutants retained the capacity to recognize specific glycoconjugate receptors on rabbit M cells and cultured epithelial cells, even though viral binding to epithelial cells was inhibited by both MAbs. S1 sequence determinations for 12 of the mutants identified σ1 mutations at four positions between residues 415 and 447, which contribute to forming the receptor-binding head domain. When aligned with the σ1 sequence of reovirus type 3 Dearing (T3D) and mapped onto the previously reported crystal structure of the T3D σ1 trimer, the four positions cluster on the side of the σ1 head, across the interface between two subunits. Three such interface-spanning epitopes are thus present per σ1 trimer and require the intact quaternary structure of the head domain for MAb binding. Identification of these intersubunit epitopes on σ1 opens the way for further studies of the mechanisms of antibody-based neutralization and protection with type 1 reoviruses.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2004
    detail.hit.zdb_id: 1495529-5
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 6
    Online Resource
    Online Resource
    American Society for Microbiology ; 2002
    In:  Journal of Virology Vol. 76, No. 19 ( 2002-10), p. 9920-9933
    In: Journal of Virology, American Society for Microbiology, Vol. 76, No. 19 ( 2002-10), p. 9920-9933
    Abstract: The mechanisms employed by nonenveloped animal viruses to penetrate the membranes of their host cells remain enigmatic. Membrane penetration by the nonenveloped mammalian reoviruses is believed to deliver a partially uncoated, but still large (∼70-nm), particle with active transcriptases for viral mRNA synthesis directly into the cytoplasm. This process is likely initiated by a particle form that resembles infectious subvirion particles (ISVPs), disassembly intermediates produced from virions by proteolytic uncoating. Consistent with that idea, ISVPs, but not virions, can induce disruption of membranes in vitro. Both activities ascribed to ISVP-like particles, membrane disruption in vitro and membrane penetration within cells, are linked to N-myristoylated outer-capsid protein μ1, present in 600 copies at the surfaces of ISVPs. To understand how μ1 fulfills its role as the reovirus penetration protein, we monitored changes in ISVPs during the permeabilization of red blood cells induced by these particles. Hemolysis was preceded by a major structural transition in ISVPs, characterized by conformational change in μ1 and elution of fibrous attachment protein σ1. The altered conformer of μ1 was required for hemolysis and was markedly hydrophobic. The structural transition in ISVPs was further accompanied by derepression of genome-dependent mRNA synthesis by the particle-associated transcriptases. We propose a model for reovirus entry in which (i) primed and triggered conformational changes, analogous to those in enveloped-virus fusion proteins, generate a hydrophobic μ1 conformer capable of inserting into and disrupting cell membranes and (ii) activation of the viral particles for membrane interaction and mRNA synthesis are concurrent events. Reoviruses provide an opportune system for defining the molecular details of membrane penetration by a large nonenveloped animal virus.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2002
    detail.hit.zdb_id: 1495529-5
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 7
    In: The EMBO Journal, Wiley, Vol. 27, No. 8 ( 2008-4-23), p. 1289-1298
    Type of Medium: Online Resource
    ISSN: 0261-4189 , 1460-2075
    RVK:
    Language: Unknown
    Publisher: Wiley
    Publication Date: 2008
    detail.hit.zdb_id: 1467419-1
    detail.hit.zdb_id: 586044-1
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 8
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 2000
    In:  Nature Vol. 404, No. 6781 ( 2000-04-27), p. 960-967
    In: Nature, Springer Science and Business Media LLC, Vol. 404, No. 6781 ( 2000-04-27), p. 960-967
    Type of Medium: Online Resource
    ISSN: 0028-0836 , 1476-4687
    RVK:
    RVK:
    RVK:
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2000
    detail.hit.zdb_id: 120714-3
    detail.hit.zdb_id: 1413423-8
    SSG: 11
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 9
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 2009
    In:  Archives of Virology Vol. 154, No. 2 ( 2009-02), p. 373-379
    In: Archives of Virology, Springer Science and Business Media LLC, Vol. 154, No. 2 ( 2009-02), p. 373-379
    Type of Medium: Online Resource
    ISSN: 0304-8608 , 1432-8798
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2009
    detail.hit.zdb_id: 1458460-8
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 10
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 2009
    In:  Archives of Virology Vol. 154, No. 12 ( 2009-12), p. 1959-1965
    In: Archives of Virology, Springer Science and Business Media LLC, Vol. 154, No. 12 ( 2009-12), p. 1959-1965
    Type of Medium: Online Resource
    ISSN: 0304-8608 , 1432-8798
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2009
    detail.hit.zdb_id: 1458460-8
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...