Structural elements in glycoprotein 70 from polytropic Friend mink cell focus-inducing virus and glycoprotein 71 from ecotropic Friend murine leukemia virus, as defined by disulfide-bonding pattern and limited proteolysis
| Autor: | Dietmar Linder, Monica Linder, V Wenzel, Stephan Stirm |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Proteolysis
Molecular Sequence Data Retroviridae Proteins Oncogenic Immunology Biology Microbiology Viral Envelope Proteins Viral envelope Mink Cell Focus-Inducing Viruses Virology Murine leukemia virus medicine Amino Acid Sequence Cysteine Disulfides Protein secondary structure Peptide sequence chemistry.chemical_classification medicine.diagnostic_test Hydrolysis biology.organism_classification Friend murine leukemia virus chemistry Biochemistry Insect Science Glycoprotein Research Article |
| Zdroj: | Journal of Virology. 68:5133-5141 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.68.8.5133-5141.1994 |
| Popis: | The disulfide-bonding pattern of glycoprotein 70 (gp70), the surface glycoprotein (SU) encoded by the envelope gene of polytropic Friend milk cell focus-inducing virus, was elucidated and compared with that of glycoprotein 71 (gp71), the corresponding glycoprotein of the ecotropic Friend murine leukemia virus, which had previously been determined (M. Linder, D. Linder, J. Hahnen, H.-H. Schott, and Stirm, Eur. J. Biochem. 203:65-73, 1992). In the carboxy-terminal constant domain, in which these glycoproteins have about 97% sequence homology, the location of the four disulfide bonds was found to be analogous. In the amino-terminal differential domain, with about 37% sequence homology, 8 of the 12 cysteine residues of the ecotropic SU are conserved in the polytropic SU. In this domain, a similar clustering of disulfide bonds was detected, which led to the identification of three distinct disulfide-bonded regions in both glycoproteins. However, because of deletions and sequence deviations, the glycoproteins must have significantly different three-dimensional structures in these regions. Since the receptor-binding functions of both glycoproteins have been attributed to their amino-terminal domains and since each binds to a different receptor, these disulfide-bonded structures are likely candidates for receptor-binding functions. Limited proteolysis of both glycoproteins with various endoproteinases led to the identification of preferential proteolytic sites between disulfide-bonded regions, at the beginning of the hypervariable proline-rich region, and between differential and constant domains, further confirming the structural organization of the folded glycoproteins. |
| Databáze: | OpenAIRE |
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