Mammalian Reservoirs of Arenaviruses

Salazar‐Bravo, Jorge; Ruedas, Luis A.; Yates, Terry L.

doi:10.1007/978-3-642-56029-3_2

Cited by 80 publications

(90 citation statements)

References 128 publications

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“…Also, the GTOV GP did not mediate entry into cells expressing either ccTfR1 or cmTfR1 ( Fig. 1 C and E) (5). However, it did mediate efficient entry into cells expressing the TfR1 of the GTOV host species Z. brevicauda, as did MACV and JUNV GP molecules (Fig.…”

Section: Utilization Of Tfr1mentioning

confidence: 88%

Receptor determinants of zoonotic transmission of New World hemorrhagic fever arenaviruses

Radoshitzky

Kuhn

Spiropoulou

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

124

199

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Transferrin receptor 1 (TfR1) is a cellular receptor for the New World hemorrhagic fever arenaviruses Machupo (MACV), Junín (JUNV), and Guanarito (GTOV). Each of these viruses is specifically adapted to a distinct rodent host species, but all cause human disease. Here we compare the ability of these viruses to use various mammalian transferrin receptor 1 (TfR1) orthologs, including those of the South American rodents that serve as reservoirs for MACV, JUNV, and GTOV (Calomys callosus, Calomys musculinus, and Zygodontomys brevicauda, respectively). Retroviruses pseudotyped with MACV and JUNV but not GTOV glycoproteins (GPs) efficiently used C. callosus TfR1, whereas only JUNV GP could use C. musculinus TfR1. All three viruses efficiently used Z. brevicauda TfR1. TfR1 orthologs from related rodents, including house mouse (Mus musculus) and rat (Rattus norvegicus), did not support entry of these viruses. In contrast, these viruses efficiently used human and domestic cat TfR1 orthologs. We further show that a local region of the human TfR1 apical domain, including tyrosine 211, determined the efficiency with which MACV, JUNV, and GTOV used various TfR1 orthologs. Our data show that these New World arenaviruses are specifically adapted to the TfR1 orthologs of their respective rodent hosts and identify key commonalities between these orthologs and human TfR1 necessary for efficient transmission of these viruses to humans.Calomys ͉ Junín virus ͉ Machupo virus ͉ transferrin receptor 1

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Section: Utilization Of Tfr1mentioning

confidence: 88%

Receptor determinants of zoonotic transmission of New World hemorrhagic fever arenaviruses

Radoshitzky

Kuhn

Spiropoulou

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

124

199

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“…Up to 300,000 infections by Lassa fever virus occur annually in Africa (44), and cases of Argentine, Bolivian, and Venezuelan hemorrhagic fevers are regularly reported in South America (49). Genetic diversification and worldwide dissemination of arenaviruses with their rodent hosts (51) provide opportunities for the continued emergence of new pathogenic strains (10). Vaccines to prevent arenavirus infection are not available, and treatment options for arenaviral hemorrhagic fevers are extremely limited.…”

mentioning

confidence: 99%

A Novel Zinc-Binding Domain Is Essential for Formation of the Functional Junín Virus Envelope Glycoprotein Complex

York

Nunberg

2007

J Virol

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The envelope glycoprotein of the Junín arenavirus (GP-C) mediates entry into target cells through a pHdependent membrane fusion mechanism. Unlike other class I viral fusion proteins, the mature GP-C complex retains a cleaved, 58-amino-acid signal peptide (SSP) as an essential subunit, required both for trafficking of GP-C to the cell surface and for the activation of membrane fusion. SSP has been shown to associate noncovalently in GP-C via the cytoplasmic domain (CTD) of the transmembrane fusion subunit G2. In this report we investigate the molecular basis for this intersubunit interaction. We identify an invariant series of six cysteine and histidine residues in the CTD of G2 that is essential for incorporation of SSP in the GP-C complex. Moreover, we show that a CTD peptide fragment containing His-447, His-449, and Cys-455 specifically binds Zn 2؉ at subnanomolar concentrations. Together, these results suggest a zinc finger-like domain structure in the CTD of G2. We propose that the remaining residues in the series (His-459, Cys-467, and Cys-469) form an intersubunit zinc-binding center that incorporates Cys-57 of SSP. This unusual motif may act to retain SSP in the GP-C complex and position the ectodomain loop of SSP for its role in modulating membrane fusion activity. The unique tripartite organization of GP-C could provide novel molecular targets for therapeutic intervention in arenaviral disease.

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“…Newly developed "next-generation" sequencing (NGS) technologies allow the rapid and costeffective acquisition of thousands to millions of short sequence reads from a single sample and provide unprecedented possibilities for the large-scale sequencing of virus genomes [50,68,89,95]. These technological [119] e Previously also abbreviated GUAV [27] f Members of Calomys cf. callosus have been reported to be the actual reservoir of MACV [119].…”

Section: Current Challenges In Arenavirus Taxonomymentioning

confidence: 99%

“…These technological [119] e Previously also abbreviated GUAV [27] f Members of Calomys cf. callosus have been reported to be the actual reservoir of MACV [119]. These lauchas are morphologically indistinguishable from members of Calomys callosus (s.s.) but may comprise a separate species g Previously also abbreviated TACV [27] h The proper species name for this reservoir rodent is Calomys callosus (s.s.) [119] i Members of Necromys benefactus Waterhouse, 1837 were previously thought to be the hosts [119] advances promise an even richer haul of genomic data for arenaviruses in the near future, mainly due to their generally small genomes.…”

Section: Current Challenges In Arenavirus Taxonomymentioning

confidence: 99%

Past, present, and future of arenavirus taxonomy

et al. 2015

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Until recently, members of the monogeneric family Arenaviridae (arenaviruses) have been known to infect only muroid rodents and, in one case, possibly phyllostomid bats. The paradigm of arenaviruses exclusively infecting small mammals shifted dramatically when several groups independently published the detection and isolation of a divergent group of arenaviruses in captive alethinophidian snakes. Preliminary phylogenetic analyses suggest that these reptilian arenaviruses constitute a sister clade to mammalian arenaviruses. Here, the members of the International Committee on Taxonomy of Viruses (ICTV) Arenaviridae Study Group, together with other experts, outline the taxonomic reorganization of the family Arenaviridae to accommodate reptilian arenaviruses and other recently discovered mammalian arenaviruses and to improve compliance with the Rules of the International Code of Virus Classification and Nomenclature (ICVCN). PAirwise Sequence Comparison (PASC) of arenavirus genomes and NP amino acid pairwise distances support the modification of the present classification. As a result, the current genus Arenavirus is replaced by two genera, Mammarenavirus and Reptarenavirus, which are established to accommodate mammalian and reptilian arenaviruses, respectively, in the same family. The current species landscape among mammalian arenaviruses is upheld, with two new species added for Lunk and Merino Walk viruses and minor corrections to the spelling of some names. The published snake arenaviruses are distributed among three new separate reptarenavirus species. Finally, a non-Latinized binomial species name scheme is adopted for all arenavirus species. In addition, the current virus abbreviations have been evaluated, and some changes are 123Arch Virol (2015) 160:1851-1874 DOI 10.1007/s00705-015-2418 introduced to unequivocally identify each virus in electronic databases, manuscripts, and oral proceedings.

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Mammalian Reservoirs of Arenaviruses

Cited by 80 publications

References 128 publications

Receptor determinants of zoonotic transmission of New World hemorrhagic fever arenaviruses

Receptor determinants of zoonotic transmission of New World hemorrhagic fever arenaviruses

A Novel Zinc-Binding Domain Is Essential for Formation of the Functional Junín Virus Envelope Glycoprotein Complex

Past, present, and future of arenavirus taxonomy

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