Virus Name | Sindbis virus |
Virus Short Name | SINV |
Order | Unassigned |
Virus Family | Togaviridae |
Virus Subfamily | N.A. |
Genus | Alphavirus |
Species | Sindbis virus |
Host | Human, mammals,mosquitoes and birds |
Cell Tropism | N.A. |
Associated Disease | Sindbis fever |
Mode of Transmission | By infected mosquito |
VIPR DB link | https://www.viprbrc.org/brc/vipr_allSpecies_search.spg?method=SubmitForm&decorator=toga |
ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/positive-sense-rna-viruses-2011/w/posrna_viruses/275/togaviridae |
Virus Host DB link | N.A. |
Paper Title | Natural Resistance-associated macrophage protein (NRAMP) is a cellular receptor for sindbis virus in both insect and mammalian hosts |
Author's Name | Patrick P. Rose, Sheri L. Hanna, Anna Spiridigliozzi, Nattha Wannissorn, Daniel P. Beiting, Susan R. Ross, Richard W. Hardy, Shelly A. Bambina, Mark T. Heise, and Sara Cherry |
Journal Name | Cell Host & Microbe |
Pubmed ID | 21843867 |
Abstract | Alphaviruses, including several emerging human pathogens, are a large family of mosquito-borne viruses with Sindbis virus being a prototypical member of the genus. The host factor requirements and receptors for entry of this class of viruses remain obscure. Using a Drosophila system, we identified the divalent metal ion transporter natural resistance-associated macrophage protein (NRAMP) as a host cell surface molecule required for Sindbis virus binding and entry into Drosophila cells. Consequently, flies mutant for dNRAMP were protected from virus infection. NRAMP2, the ubiquitously expressed vertebrate homolog, mediated binding and infection of Sindbis virus into mammalian cells, and murine cells deficient for NRAMP2 were nonpermissive to infection. Alphavirus glycoprotein chimeras demonstrated that the requirement for NRAMP2 is at the level of Sindbis virus entry. Given the conserved structure of alphavirus glycoproteins, and the widespread use of transporters for viral entry, other alphaviruses may use conserved multipass membrane proteins for infection. |
Used Model | Kc167 |
DOI | 10.1016/j.chom.2011.06.009 |