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Mesoniviruses are mosquito-specific viruses with extensive geographic distribution and host range

Nikos Vasilakis123*, Hilda Guzman1, Cadhla Firth4, Naomi L Forrester123, Steven G Widen5, Thomas G Wood5, Shannan L Rossi1, Elodie Ghedin67, Vsevolov Popov1, Kim R Blasdell4, Peter J Walker4 and Robert B Tesh123

Author Affiliations

1 Department of Pathology and Center for Biodefense and Emerging Infectious Diseases, University of Texas Medical Branch, Galveston, TX 77555-0609, USA

2 Center for Tropical Diseases, University of Texas Medical Branch, Galveston, TX 77555-0609, USA

3 Institute for Human Infection and Immunity, University of Texas Medical Branch, Galveston, TX 77555-0610, USA

4 CSIRO Animal, Food and Health Sciences, Australian Animal Health Laboratory, Geelong, VIC 3220, Australia

5 Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX 77555-1079, USA

6 Department of Computational Biology and Center for Vaccine Research, University of Pittsburgh, Pittsburgh, PA 15214, USA

7 Current Address: NYU-Biology, Center for Genomics and Systems Biology, New York University, New York, NY 10032, USA

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Virology Journal 2014, 11:97  doi:10.1186/1743-422X-11-97

Published: 20 May 2014

Additional files

Additional file 1: Figure S1:

Sliding window analysis of the pairwise amino acid distances within and between the seven putatively designated mesonivirus species for ORF1ab (replicase proteins), ORF2a (S) and ORF2b (N).

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Additional file 2: Figure S2:

A Clustal X multiple sequence alignment of mesonivirus pp1ab polyproteins illustrating region containing the block insertions (yellow shading) and various imperfectly repeated sequences that occur at the boundary and within the blocks of inserted sequence.

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Additional file 3: Figure S3:

A Clustal X multiple sequence alignment of the polypeptides encoded in ORF2a (S proteins) of the mesoniviruses. A predicted signal peptide in MenoV and predicted transmembrane domains in all mesoniviruses are shaded in aqua, predicted N-glycosylation sites are shaded in green, cysteine residues are shaded in yellow and the sites of proteolytic cleavage to generate glycoproteins S1 and S2 and the unidentified N-terminal fragment are shaded in purple.

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Additional file 4: Figure S4:

A Clustal X multiple alignment of the sequences of putative polypeptides encoded on ORF4 which occurs in the 3’-terminal regions of all mesoniviruses except MenoV. To emphasize the alignment, the KSaV ORF4 protein has been shown to commence at the next available methionine residue located 34 amino acids downstream of the predicted initiation codon.

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Additional file 5: Figure S5:

A Clustal X multiple sequence alignment of region immediately downstream of the ORF1a/ORF1b RFS that has been predicted previously to adopt a stem-loop structure in NDiV. The alignment illustrates sequence variations in nucleotides predicted in NDiV to be involved in base pairs that sustain the structure.

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