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• W2001518910 abstract "A 120-kilodalton protein (p120) was identified in the duck liver that binds to several truncated versions of duck hepatitis B virus (DHBV) pre-S envelope protein, suggesting p120 may serve as a DHBV co-receptor. The amino acid sequences of tryptic peptides from purified p120 were found to be the duck p protein of the glycine decarboxylase complex (DGD). DGD cDNA cloning revealed extensive protein conservation with the chicken homologue except for several insertions in the N-terminal leader sequence. The DGD cDNA contained no in-frame AUG codon at the predicted initiation site of the open reading frame, and site-directed mutagenesis experiments established an AUU codon as the translational initiator. The DGD protein expressed in rabbit reticulocyte lysates bound truncated DHBV pre-S protein identical to that of p120 derived from duck liver confirming DGD as p120. Moreover, transfection studies in liver- and kidney-derived cells revealed both cell surface and cytoplasmic expression of the protein. Cloning of the glycine decarboxylase cDNA will permit a direct test of whether it functions as a cell surface co-receptor or as a co-factor in the DHBV replication cycles. A 120-kilodalton protein (p120) was identified in the duck liver that binds to several truncated versions of duck hepatitis B virus (DHBV) pre-S envelope protein, suggesting p120 may serve as a DHBV co-receptor. The amino acid sequences of tryptic peptides from purified p120 were found to be the duck p protein of the glycine decarboxylase complex (DGD). DGD cDNA cloning revealed extensive protein conservation with the chicken homologue except for several insertions in the N-terminal leader sequence. The DGD cDNA contained no in-frame AUG codon at the predicted initiation site of the open reading frame, and site-directed mutagenesis experiments established an AUU codon as the translational initiator. The DGD protein expressed in rabbit reticulocyte lysates bound truncated DHBV pre-S protein identical to that of p120 derived from duck liver confirming DGD as p120. Moreover, transfection studies in liver- and kidney-derived cells revealed both cell surface and cytoplasmic expression of the protein. Cloning of the glycine decarboxylase cDNA will permit a direct test of whether it functions as a cell surface co-receptor or as a co-factor in the DHBV replication cycles. duck hepatitis B virus glutathione S-transferase primary duck hepatocyte duck glycine decarboxylase chicken glycine decarboxylase polyacrylamide gel electrophoresis high pressure liquid chromatography kilobase(s) polymerase chain reaction nucleotide(s) The human hepatitis B virus and related animal viruses form hepatotropic DNA viruses or hepadnaviruses (1Ganem D. Fields B.N. Knipe D.M. Howley P.M. Fields Virology. Lippincott-Raven Publishers, Philadelphia1996Google Scholar); because the early events of hepatocyte infection are unclear, studies were initiated via the duck hepatitis B virus (DHBV)1 model in a multifold approach to identify candidate cell surface receptor proteins. Interactive proteins for the pre-S domain of DHBV large envelope protein (the assumed ligand to viral receptor) were identified and cDNAs cloned to verify their potential role as DHBV receptor/co-receptor in nonsusceptible cell lines.Two pre-S interacting proteins, p170 (2Tong S. Li J. Wands J.R. J. Virol. 1995; 69: 7106-7112Crossref PubMed Google Scholar) and p120 (3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar), were classified using DHBV pre-S domain fused to glutathione S-transferase (GST); p170 was analogous to the gp180 DHBV-binding protein characterized by Kuroki et al. (4Kuroki K. Cheung R. Marion P.L. Ganem D. J. Virol. 1994; 68: 2091-2096Crossref PubMed Google Scholar) and, based on its similarity to carboxypeptidases (5Kuroki K. Eng F. Ishikawa T. Turck C. Harada F. Ganem D. J. Biol. Chem. 1995; 270: 15022-15028Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar), was renamed duck carboxypeptidase D. Transfection of duck carboxypeptidase D cDNA into liver- and kidney-derived cell lines, conferred efficient DHBV binding and entry 2S. Tong, J. Li, and J. R. Wands, submitted for publication. 2S. Tong, J. Li, and J. R. Wands, submitted for publication., indicating p170 (duck carboxypeptidase D) pre-S-binding protein served as a primary DHBV receptor.Optimal p170 binding requires an entire pre-S domain (residues 1–161) (2Tong S. Li J. Wands J.R. J. Virol. 1995; 69: 7106-7112Crossref PubMed Google Scholar). Although p120 interacts with this pre-S peptide, it also binds with high affinity to several cleaved pre-S polypeptides (92–161, 98–161, 1–102) (3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar); of these, 1–102 may be generated in vivo by cleavage of the large envelope protein present on virion particles by a dibasic endopeptidase. The sequence surrounding pre-S residue 102 (Arg-Glu-Ala-Phe-Arg-Arg-Tyr; residue 102 is underlined) fulfills the requirement for cleavage by furin, which processes many viral envelope protein precursors including human immunodeficiency virus (7Nakayama K. Biochem. J. 1997; 327: 625-635Crossref PubMed Scopus (701) Google Scholar). Thus, depending on the subcellular compartment of endopeptidase cleavage, p120 may serve as a cell surface co-receptor or an intracellular binding partner facilitating the disassembly of viral particles.Further support of the involvement of p120 in the DHBV life cycle is proposed by 1) exclusive expression in the liver, kidney, and pancreas of known DHBV tissues susceptible to infection, contrasting sharply with widespread duck carboxypeptidase D tissue distribution (2Tong S. Li J. Wands J.R. J. Virol. 1995; 69: 7106-7112Crossref PubMed Google Scholar, 3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar, 4Kuroki K. Cheung R. Marion P.L. Ganem D. J. Virol. 1994; 68: 2091-2096Crossref PubMed Google Scholar); 2) the p120 binding site, mapped to pre-S residues 98–102, where a mouse monoclonal antibody blocks DHBV infection in primary duck hepatocytes (PDH) (8Lambert V. Fernholz D. Sprengel R. Fourel I. Deleage G. Wildner G. Peyret C. Trepo C. Cova L. Will H. J. Virol. 1990; 64: 1290-1297Crossref PubMed Google Scholar, 9Chassot S. Lambert V. Kay A. Godinot C. Roux B. Trepo C. Cova L. Virology. 1993; 192: 217-223Crossref PubMed Scopus (28) Google Scholar); 3) a short pre-S peptide (residues 80–102) with affinity for p120 but not duck carboxypeptidase D substantially inhibited productive DHBV infection of PDH. Similarly, double-point mutations within the p120 binding site severely hampered viral infection in PDH (3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar). In the present investigation, the cDNA of p120 was cloned, and the protein was expressed to characterize its binding properties to pre-S peptides. More important, available protein on the surface of transfected cells was detected.DISCUSSIONThe p120 pre-S-binding protein (2Tong S. Li J. Wands J.R. J. Virol. 1995; 69: 7106-7112Crossref PubMed Google Scholar) has now been established as the p protein of DGD following cDNA cloning. The partial amino acid sequences purified from p120 duck liver matched the translated cDNA sequences, and comparison from different species validated p120 as the p protein component of the glycine decarboxylase complex. The tissue distribution of DGD and, specifically, unique patterns of binding to truncated DHBV pre-S and mutants confirmed the identity of DGD as p120.Although the duck p protein is highly homologous to that of the corresponding chicken molecule, there is significant divergence in the N terminus encoding the putative mitochondrial-targeting domain. Interestingly, the DGD protein not only is distributed in the cytoplasm but is also available on the cell surface as described previously (3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar) and confirmed in the present study (Fig. 7); these DGD findings differ from CGD described as solely a mitochondrial protein. Whether the divergent 5′ sequence is responsible for subcellular and cell surface localization warrants further study.The duck glycine decarboxylase p protein is translated from an AUU codon based on extensive cDNA mutational analysis followed by expression of the mutant constructs in a cell-free system. An in-frame nonsense mutation (Asn2) placed immediately downstream of AUU346 abolished 125-kDa protein production and was similar to a point mutation that converted AUU346 into an AGU codon (Fig. 4, B and C). Moreover, use of the non-AUG codon for initiation also occurred in transfected DGD27/2.3.1 construct in mammalian cells (Fig. 5), indicating that translation from cell lysates was not merely a result of relaxed specificity caused by high potassium concentration. Whether AUU codon selection (compared with other nearby AUG-like codons) requires structural motifsi.e. hairpin structure downstream to slacken the passage of scanning ribosomes, warrants further study.Initiation from an internal AUU codon of the DGD cDNA was apparently not optimal in either reticulocyte lysates or transfected mammalian cells, since conversion of the AUU into the AUG codon and deletion of the 5′-nontranslated region greatly enhanced protein yield. The low efficiency of protein expression is due, in part, to the presence of the nontranslated sequence at the 5′ end, since the DGD27/2.3.1 construct produced a higher yield of protein than DGD24a/2.3.1. Whether such an inhibitory effect is caused by the translation of the upstream small open reading frames or by the presence of a secondary structure impeding the entry of scanning ribosomes remains unknown.Victorin, the toxin produced by the fungus Cochliobolus victoriae, uses the p protein of the oat glycine decarboxylase as the binding protein (16Wolpert T.J. Navarre D.A. Moore D.L. Macko V. Plant Cell. 1994; 6: 1145-1155PubMed Google Scholar); inhibition of the enzymatic function by victorin is believed to account for the blight of oats (6Navarre D. Wolpert T.J. Plant Cell. 1995; 7: 463-471PubMed Google Scholar). The identification of glycine decarboxylase as the binding partner for DHBV pre-S protein and truncated species will allow us to directly test the role of glycine decarboxylase as a DHBV co-receptor or co-factor facilitating productive viral infection by cDNA transfection experiments. The human hepatitis B virus and related animal viruses form hepatotropic DNA viruses or hepadnaviruses (1Ganem D. Fields B.N. Knipe D.M. Howley P.M. Fields Virology. Lippincott-Raven Publishers, Philadelphia1996Google Scholar); because the early events of hepatocyte infection are unclear, studies were initiated via the duck hepatitis B virus (DHBV)1 model in a multifold approach to identify candidate cell surface receptor proteins. Interactive proteins for the pre-S domain of DHBV large envelope protein (the assumed ligand to viral receptor) were identified and cDNAs cloned to verify their potential role as DHBV receptor/co-receptor in nonsusceptible cell lines. Two pre-S interacting proteins, p170 (2Tong S. Li J. Wands J.R. J. Virol. 1995; 69: 7106-7112Crossref PubMed Google Scholar) and p120 (3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar), were classified using DHBV pre-S domain fused to glutathione S-transferase (GST); p170 was analogous to the gp180 DHBV-binding protein characterized by Kuroki et al. (4Kuroki K. Cheung R. Marion P.L. Ganem D. J. Virol. 1994; 68: 2091-2096Crossref PubMed Google Scholar) and, based on its similarity to carboxypeptidases (5Kuroki K. Eng F. Ishikawa T. Turck C. Harada F. Ganem D. J. Biol. Chem. 1995; 270: 15022-15028Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar), was renamed duck carboxypeptidase D. Transfection of duck carboxypeptidase D cDNA into liver- and kidney-derived cell lines, conferred efficient DHBV binding and entry 2S. Tong, J. Li, and J. R. Wands, submitted for publication. 2S. Tong, J. Li, and J. R. Wands, submitted for publication., indicating p170 (duck carboxypeptidase D) pre-S-binding protein served as a primary DHBV receptor. Optimal p170 binding requires an entire pre-S domain (residues 1–161) (2Tong S. Li J. Wands J.R. J. Virol. 1995; 69: 7106-7112Crossref PubMed Google Scholar). Although p120 interacts with this pre-S peptide, it also binds with high affinity to several cleaved pre-S polypeptides (92–161, 98–161, 1–102) (3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar); of these, 1–102 may be generated in vivo by cleavage of the large envelope protein present on virion particles by a dibasic endopeptidase. The sequence surrounding pre-S residue 102 (Arg-Glu-Ala-Phe-Arg-Arg-Tyr; residue 102 is underlined) fulfills the requirement for cleavage by furin, which processes many viral envelope protein precursors including human immunodeficiency virus (7Nakayama K. Biochem. J. 1997; 327: 625-635Crossref PubMed Scopus (701) Google Scholar). Thus, depending on the subcellular compartment of endopeptidase cleavage, p120 may serve as a cell surface co-receptor or an intracellular binding partner facilitating the disassembly of viral particles. Further support of the involvement of p120 in the DHBV life cycle is proposed by 1) exclusive expression in the liver, kidney, and pancreas of known DHBV tissues susceptible to infection, contrasting sharply with widespread duck carboxypeptidase D tissue distribution (2Tong S. Li J. Wands J.R. J. Virol. 1995; 69: 7106-7112Crossref PubMed Google Scholar, 3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar, 4Kuroki K. Cheung R. Marion P.L. Ganem D. J. Virol. 1994; 68: 2091-2096Crossref PubMed Google Scholar); 2) the p120 binding site, mapped to pre-S residues 98–102, where a mouse monoclonal antibody blocks DHBV infection in primary duck hepatocytes (PDH) (8Lambert V. Fernholz D. Sprengel R. Fourel I. Deleage G. Wildner G. Peyret C. Trepo C. Cova L. Will H. J. Virol. 1990; 64: 1290-1297Crossref PubMed Google Scholar, 9Chassot S. Lambert V. Kay A. Godinot C. Roux B. Trepo C. Cova L. Virology. 1993; 192: 217-223Crossref PubMed Scopus (28) Google Scholar); 3) a short pre-S peptide (residues 80–102) with affinity for p120 but not duck carboxypeptidase D substantially inhibited productive DHBV infection of PDH. Similarly, double-point mutations within the p120 binding site severely hampered viral infection in PDH (3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar). In the present investigation, the cDNA of p120 was cloned, and the protein was expressed to characterize its binding properties to pre-S peptides. More important, available protein on the surface of transfected cells was detected. DISCUSSIONThe p120 pre-S-binding protein (2Tong S. Li J. Wands J.R. J. Virol. 1995; 69: 7106-7112Crossref PubMed Google Scholar) has now been established as the p protein of DGD following cDNA cloning. The partial amino acid sequences purified from p120 duck liver matched the translated cDNA sequences, and comparison from different species validated p120 as the p protein component of the glycine decarboxylase complex. The tissue distribution of DGD and, specifically, unique patterns of binding to truncated DHBV pre-S and mutants confirmed the identity of DGD as p120.Although the duck p protein is highly homologous to that of the corresponding chicken molecule, there is significant divergence in the N terminus encoding the putative mitochondrial-targeting domain. Interestingly, the DGD protein not only is distributed in the cytoplasm but is also available on the cell surface as described previously (3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar) and confirmed in the present study (Fig. 7); these DGD findings differ from CGD described as solely a mitochondrial protein. Whether the divergent 5′ sequence is responsible for subcellular and cell surface localization warrants further study.The duck glycine decarboxylase p protein is translated from an AUU codon based on extensive cDNA mutational analysis followed by expression of the mutant constructs in a cell-free system. An in-frame nonsense mutation (Asn2) placed immediately downstream of AUU346 abolished 125-kDa protein production and was similar to a point mutation that converted AUU346 into an AGU codon (Fig. 4, B and C). Moreover, use of the non-AUG codon for initiation also occurred in transfected DGD27/2.3.1 construct in mammalian cells (Fig. 5), indicating that translation from cell lysates was not merely a result of relaxed specificity caused by high potassium concentration. Whether AUU codon selection (compared with other nearby AUG-like codons) requires structural motifsi.e. hairpin structure downstream to slacken the passage of scanning ribosomes, warrants further study.Initiation from an internal AUU codon of the DGD cDNA was apparently not optimal in either reticulocyte lysates or transfected mammalian cells, since conversion of the AUU into the AUG codon and deletion of the 5′-nontranslated region greatly enhanced protein yield. The low efficiency of protein expression is due, in part, to the presence of the nontranslated sequence at the 5′ end, since the DGD27/2.3.1 construct produced a higher yield of protein than DGD24a/2.3.1. Whether such an inhibitory effect is caused by the translation of the upstream small open reading frames or by the presence of a secondary structure impeding the entry of scanning ribosomes remains unknown.Victorin, the toxin produced by the fungus Cochliobolus victoriae, uses the p protein of the oat glycine decarboxylase as the binding protein (16Wolpert T.J. Navarre D.A. Moore D.L. Macko V. Plant Cell. 1994; 6: 1145-1155PubMed Google Scholar); inhibition of the enzymatic function by victorin is believed to account for the blight of oats (6Navarre D. Wolpert T.J. Plant Cell. 1995; 7: 463-471PubMed Google Scholar). The identification of glycine decarboxylase as the binding partner for DHBV pre-S protein and truncated species will allow us to directly test the role of glycine decarboxylase as a DHBV co-receptor or co-factor facilitating productive viral infection by cDNA transfection experiments. The p120 pre-S-binding protein (2Tong S. Li J. Wands J.R. J. Virol. 1995; 69: 7106-7112Crossref PubMed Google Scholar) has now been established as the p protein of DGD following cDNA cloning. The partial amino acid sequences purified from p120 duck liver matched the translated cDNA sequences, and comparison from different species validated p120 as the p protein component of the glycine decarboxylase complex. The tissue distribution of DGD and, specifically, unique patterns of binding to truncated DHBV pre-S and mutants confirmed the identity of DGD as p120. Although the duck p protein is highly homologous to that of the corresponding chicken molecule, there is significant divergence in the N terminus encoding the putative mitochondrial-targeting domain. Interestingly, the DGD protein not only is distributed in the cytoplasm but is also available on the cell surface as described previously (3Li J. Tong S. Wands J.R. J. Virol. 1996; 70: 6029-6035Crossref PubMed Google Scholar) and confirmed in the present study (Fig. 7); these DGD findings differ from CGD described as solely a mitochondrial protein. Whether the divergent 5′ sequence is responsible for subcellular and cell surface localization warrants further study. The duck glycine decarboxylase p protein is translated from an AUU codon based on extensive cDNA mutational analysis followed by expression of the mutant constructs in a cell-free system. An in-frame nonsense mutation (Asn2) placed immediately downstream of AUU346 abolished 125-kDa protein production and was similar to a point mutation that converted AUU346 into an AGU codon (Fig. 4, B and C). Moreover, use of the non-AUG codon for initiation also occurred in transfected DGD27/2.3.1 construct in mammalian cells (Fig. 5), indicating that translation from cell lysates was not merely a result of relaxed specificity caused by high potassium concentration. Whether AUU codon selection (compared with other nearby AUG-like codons) requires structural motifsi.e. hairpin structure downstream to slacken the passage of scanning ribosomes, warrants further study. Initiation from an internal AUU codon of the DGD cDNA was apparently not optimal in either reticulocyte lysates or transfected mammalian cells, since conversion of the AUU into the AUG codon and deletion of the 5′-nontranslated region greatly enhanced protein yield. The low efficiency of protein expression is due, in part, to the presence of the nontranslated sequence at the 5′ end, since the DGD27/2.3.1 construct produced a higher yield of protein than DGD24a/2.3.1. Whether such an inhibitory effect is caused by the translation of the upstream small open reading frames or by the presence of a secondary structure impeding the entry of scanning ribosomes remains unknown. Victorin, the toxin produced by the fungus Cochliobolus victoriae, uses the p protein of the oat glycine decarboxylase as the binding protein (16Wolpert T.J. Navarre D.A. Moore D.L. Macko V. Plant Cell. 1994; 6: 1145-1155PubMed Google Scholar); inhibition of the enzymatic function by victorin is believed to account for the blight of oats (6Navarre D. Wolpert T.J. Plant Cell. 1995; 7: 463-471PubMed Google Scholar). The identification of glycine decarboxylase as the binding partner for DHBV pre-S protein and truncated species will allow us to directly test the role of glycine decarboxylase as a DHBV co-receptor or co-factor facilitating productive viral infection by cDNA transfection experiments." @default.
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• W2001518910 title "Identification and Expression of Glycine Decarboxylase (p120) as a Duck Hepatitis B Virus Pre-S Envelope-binding Protein" @default.
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