Murine pneumotropic virus VP1 virus-like particles (VLPs) bind to several cell types independent of sialic acid residues and do not serologically cross react with murine polyomavirus VP1 VLPs.
The ability of murine pneumotropic virus (MPtV) major capsid protein VP1 to form virus-like particles (VLPs) was examined. MPtV-VLPs obtained were used to estimate the potential of MPtV to attach to different cells and to assess some characteristics of the MPtV cell receptor. Furthermore, to evaluate if MPtV-VLPs could potentially complement murine polyomavirus (MPyV) VP1 VLPs (MPyV-VLPs) as vectors for prime-boost gene therapy, the capability of MPtV-VLPs to serologically cross react with MPyV-VLPs and to transduce DNA into cells was examined. MPtV VP1 obtained in a recombinant baculovirus system formed MPtV-VLPs readily. MPtV-VLPs were shown by FACS analysis to bind to different cells, independent of MHC class I antigen expression. In addition, MPtV-VLPs did not cause haemagglutination of red blood cells and MPtV-VLP binding to cells was neuraminidase resistant but mostly trypsin and papain sensitive, indicating that the MPtV receptor lacks sialic acid components. When tested by ELISA and in vivo neutralization assays, MPtV-VLPs did not serologically cross react with MPyV-VLPs, suggesting that MPtV-VLPs and MPyV-VLPs could potentially be interchanged as carriers of DNA in repeated gene therapy. Finally, MPtV-VLPs were shown to transduce foreign DNA in vitro and in vivo. In conclusion, the data suggest that MPtV-VLPs, and possibly also MPtV, bind to several different cell types, that binding is neuraminidase resistant and that MPtV-VLPs should potentially be able to complement MPyV-VLPs for prime-boost gene transfer in vivo.
Tegerstedt
K
K
Department of Oncology-Pathology, Karolinska Institute, Cancer Center Karolinska R8 : 01, Karolinska Hospital, SE-171 76 Stockholm, Sweden.
Andreasson
K
K
Department of Oncology-Pathology, Karolinska Institute, Cancer Center Karolinska R8 : 01, Karolinska Hospital, SE-171 76 Stockholm, Sweden.
Vlastos
A
A
Department of Oncology-Pathology, Karolinska Institute, Cancer Center Karolinska R8 : 01, Karolinska Hospital, SE-171 76 Stockholm, Sweden.
Hedlund
K O
KO
Swedish Institute for Infectious Disease Control and Microbiology and Tumor Biology Center, Karolinska Institute, SE-171 82 Solna, Sweden.
Dalianis
T
T
Department of Oncology-Pathology, Karolinska Institute, Cancer Center Karolinska R8 : 01, Karolinska Hospital, SE-171 76 Stockholm, Sweden.
Ramqvist
T
T
Department of Oncology-Pathology, Karolinska Institute, Cancer Center Karolinska R8 : 01, Karolinska Hospital, SE-171 76 Stockholm, Sweden.
D000818:Animals; D000914:Antibodies, Viral / Q000276:immunology*; D036022:Capsid Proteins / Q000276:immunology / Q000378:metabolism*; D002460:Cell Line; D002522:Chlorocebus aethiops; D003429:Cross Reactions; D004268:DNA-Binding Proteins / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D006168:Guinea Pigs; D006384:Hemagglutination; D015395:Histocompatibility Antigens Class I / Q000378:metabolism; D006801:Humans; D051379:Mice; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000494:pharmacology; D009500:Neutralization Tests; D010206:Papain / Q000494:pharmacology; D010957:Plasmids; D011120:Polyomavirus / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D011991:Receptors, Virus / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology
D000914:Antibodies, Viral; D036022:Capsid Proteins; D004268:DNA-Binding Proteins; D015395:Histocompatibility Antigens Class I; D011991:Receptors, Virus; C062481:VP1 protein, polyomavirus; D009439:Neuraminidase; D014357:Trypsin; D010206:Papain; D019158:N-Acetylneuraminic Acid