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Review
. 2021 May 13;13(5):907.
doi: 10.3390/v13050907.

Hamster Polyomavirus Research: Past, Present, and Future

Burkhard Jandrig  1 , Hans Krause  2 , Wolfgang Zimmermann  3 , Emilija Vasiliunaite  4 , Alma Gedvilaite  4 , Rainer G Ulrich  5   6
Affiliations
Review

Hamster Polyomavirus Research: Past, Present, and Future

Burkhard Jandrig et al. Viruses. .

Abstract

Hamster polyomavirus (Mesocricetus auratus polyomavirus 1, HaPyV) was discovered as one of the first rodent polyomaviruses at the end of the 1960s in a colony of Syrian hamsters (Mesocricetus auratus) affected by skin tumors. Natural HaPyV infections have been recorded in Syrian hamster colonies due to the occurrence of skin tumors and lymphomas. HaPyV infections of Syrian hamsters represent an important and pioneering tumor model. Experimental infections of Syrian hamsters of different colonies are still serving as model systems (e.g., mesothelioma). The observed phylogenetic relationship of HaPyV to murine polyomaviruses within the genus Alphapolyomavirus, and the exclusive detection of other cricetid polyomaviruses, i.e., common vole (Microtus arvalis polyomavirus 1) and bank vole (Myodes glareolus polyomavirus 1) polyomaviruses, in the genus Betapolyomavirus, must be considered with caution, as knowledge of rodent-associated polyomaviruses is still limited. The genome of HaPyV shows the typical organization of polyomaviruses with an early and a late transcriptional region. The early region encodes three tumor (T) antigens including a middle T antigen; the late region encodes three capsid proteins. The major capsid protein VP1 of HaPyV was established as a carrier for the generation of autologous, chimeric, and mosaic virus-like particles (VLPs) with a broad range of applications, e.g., for the production of epitope-specific antibodies. Autologous VLPs have been applied for entry and maturation studies of dendritic cells. The generation of chimeric and mosaic VLPs indicated the high flexibility of the VP1 carrier protein for the insertion of foreign sequences. The generation of pseudotype VLPs of original VP1 and VP2-foreign protein fusion can further enhance the applicability of this system. Future investigations should evaluate the evolutionary origin of HaPyV, monitor its occurrence in wildlife and Syrian hamster breeding, and prove its value for the generation of potential vaccine candidates and as a gene therapy vehicle.

Keywords: Syrian hamster; genome organization; major capsid protein; middle T antigen; rodent polyomaviruses; tumor model; virus discovery; virus-like particles.

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Conflict of interest statement

The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.

Figures

Figure 1
Figure 1
Genome organization of hamster polyomavirus. The double-stranded DNA genome of 5372 base pairs contains a noncoding control region (NCCR), an early transcriptional region encoding three T antigens and a late transcriptional region encoding capsid proteins VP1, VP2, and VP3. The coding regions are depicted as shaded green, blue, light blue, and violet arrows. As for all polyomaviruses, the proximal N-terminal region of all three T antigens is identical. The VP2 represents an N-terminally prolonged VP3; i.e., the VP3 region is identical to the C-terminal part of VP2.
Figure 2
Figure 2
The nucleotide sequences of HaPyV strains from different Syrian hamster colonies available in GenBank were assembled and the contig formed with the phred-basecalling and the phrap-assembly tool available in the suite CodonCode Aligner v.9 (CodonCode Corp., Centerville, MA, USA). CodonCode Aligner also supported building neighbor-joining trees for the contig. The branch lengths of the neighbor-joining tree represent the distance between the samples. Part of the contig is shown on the right representing the area between nucleotides 3337 and 3404 of the Hamster polyomavirus isolate Berlin (GenBank JX036360). This area is located within the VP1 gene.
Figure 3
Figure 3
Phylogenetic trees of 174 representatives of the Polyomaviridae family obtained using LT (a) and VP1 (b) amino acid sequence alignments. Polyomaviruses are named following the recommendations of the International Committee on Taxonomy of Viruses (ICTV), accession numbers of sequences are provided. Virus genera are indicated by a colored stripe on the right side of each tree and the orders of the viral hosts are given. Rodent polyomaviruses are depicted in bold font with an orange background, hamster polyomavirus is emphasized with a bright yellow background. Trees were generated using a maximum likelihood analysis, Transfer Bootstrap Expectation support for bold black branches is >0.85. The number of leaves in condensed nodes are given in parenthesis. Detailed information on condensed nodes and tree generation and quoted references are given in Supplementary Table S1 [51,52,53,54,55,56,57,58,59].
Figure 4
Figure 4
Strategies for the production of autologous, chimeric, mosaic, and pseudotype VLPs. For the generation of chimeric VLPs, four potential insertion sites were used that are located on flexible and variable regions of VP1. Mosaic VLPs are generated by the simultaneous expression of non-modified VP1 with a VP1-foreign sequence fusion protein. Pseudotype VLPs can be generated by the co-expression of VP1 and a VP2-foreign sequence fusion protein.
Figure 5
Figure 5
Electron-microscopical images of autologous VP1-derived virus-like particles (a), chimeric VP1-derived virus-like particles with hepatitis B virus preS1 peptide (b) or lymphocytic choriomeningitis virus gp30 peptide in insertion site #1 (c), HBV preS1 peptide, Puumala orthohantavirus nucleocapsid protein (N) amino acids 1–45 or 1–120 at insertion site #4 (d–f), mosaic virus-like particles with enhanced green fluorescent protein (eGFP) in site #4 (g) and pseudotype virus-like particles with a VP2 fusion of eGFP or single chain variable fragment with human Fc IgG domain (h,i), all produced in yeast Saccharomyces cerevisiae. The bar represents 100 nm.
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