Cell lines having genetically modified glycosylation pathways that allow them to carry out a sequence of enzymatic reactions, which mimic the processing of glycoproteins in humans, have been developed. Recombinant proteins expressed in these engineered hosts yield glycoproteins more similar, if not substantially identical, to their human counterparts. The lower eukaryotes, which ordinarily produce high-mannose containing N-glycans, including unicellular and multicellular fungi are modified to produce N-glycans such as Man 5 GlcNAc 2 or other structures along human glycosylation pathways. This is achieved using a combination of engineering and/or selection of strains which: do not express certain enzymes which create the undesirable complex structures characteristic of the fungal glycoproteins, which express exogenous enzymes selected either to have optimal activity under the conditions present in the fungi where activity is desired, or which are targeted to an organelle where optimal activity is achieved, and combinations thereof wherein the genetically engineered eukaryote expresses multiple exogenous enzymes required to produce “human-like” glycoproteins.

Methods for producing modified glycoproteins

Antibodies from phage antibody libraries.

The tropism of organ involvement in primary systemic amyloidosis: contributions of Ig V(L) germ line gene use and clonal plasma cell burden.

Anti-inflammatory and antinociceptive activity assessment of plants used as remedy in Turkish folk medicine

Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain–associated amyloidosis (AL)

Amino acid sequence based PCR primers for amplification of rearranged human heavy and light chain immunoglobulin variable region genes.

Recent reports have pointed out the difficulties in generating recombinant adenoviral vectors expressing FasL using eukaryotic cells. In the present study we cloned the murine FasL (mFasL) gene into the pCA14 or pShuttle vectors and recombined them with the adeno-5 virus backbone pBHG10 or pAdEasy-1 in eukaryotic (911 cells) or prokaryotic (E. coli) cells, respectively. Recombination of pCA14-mFasL with pBHG10 in Fas-carrying 911 cells leads to rapid expression of mFasL and cell death by apoptosis before virus replication is initiated. The same effect is observed when 911 cells are transfected with the pCA14-mFasL shuttle vector only. If recombination (pShuttle-mFasL with pAdEasy-1) is performed first in bacteria and 911 cells are transfected thereafter with recombined AdEasy-mFasL, virus production starts immediately and the cells survive longer. The resulting AdEasy-mFasL viruses are able to infect other eukaryotic cells and induce expression of functional mFasL. This study describes a method for efficient generation of recombinant FasL adeno-5 viruses in eukaryotic cells. The method may be generally suitable for producing viruses carrying deleterious genes.

Fas ligand gene-carrying adeno-5 AdEasy viruses can be efficiently propagated in apoptosis-sensitive human embryonic retinoblast 911 cells.

Suppression of T-cell alloreactivity by gene-therapeutic modulation of human dendritic stimulator cells with TGF-β adenoviral vectors

Functional characterization of HP12: a novel immunosuppressant purified from Helleborus species.

CONTRARY TO EARLY expectations, Fas Ligand (FasL) expression in organ allografts compromised the transplanted tissue and did not prolong graft survival. It is known that antigen-presenting cells (APCs) strongly stimulate allogenic T cells. Recent data in a mouse model revealed that the T cell response to adenovirus could be suppressed by treating the recipient with APCs that previously were infected with recombinant FasL-adenovirus and consequently expressed FasL. It was thought that adenoviral antigens are presented by APCs to T cells and that concomitant expression of FasL induces apoptosis of specific T cells. Based on this finding, we speculated that FasL-expressing APCs would induce apoptosis of allogenic T cells and thus suppress the subsequent response to alloantigen. In vivo one could possibly inject donor APCs expressing FasL into an allogenic recipient and thereby suppress the T cell response to a subsequent graft. In the present experiment we tested this hypothesis by infecting allogenic rat macrophages with FasL-adenovirus and using the infected cells for stimulation of allogenic T cells in cell culture experiments. MATERIALS AND METHODS Construction of Ad-mFasL Recombinant adenoviruses carrying the murine FasL (mFasL) gene were generated as previously described. Briefly, the mFasL gene was cloned into a shuttle vector and recombined with an adeno-5 vector in bacteria. Adeno-mFasL viruses were propagated in 911 cells. The correct mFasL insert of the recombinant construct was proven by sequence analysis. Transcription of the mFasL gene in infected cells was verified by RT-PCR.

Generation of FASL-expressing antigen-presenting cells for suppression of alloreactive T cells in the rat.

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