Inhibition of Apoptosis by the African Swine Fever Virus Bcl-2 Homologue: Role of the BH1 Domain
The function of the African swine fever virus (ASFV)bcl-2homologue, geneA179L,in the regulation of apoptosis was investigated using as a model system the human myeloid leukemia cell line K562 induced to die by apoptosis with inhibitors of macromolecular synthesis, a process that is prevented by over...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1997-02, Vol.228 (2), p.400-404 |
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| container_title | Virology (New York, N.Y.) |
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| creator | Revilla, Yolanda Cebrián, Ana Baixerás, Elena Martı́nez-A, Carlos Viñuela, Eladio Salas, Marı́a L |
| description | The function of the African swine fever virus (ASFV)bcl-2homologue, geneA179L,in the regulation of apoptosis was investigated using as a model system the human myeloid leukemia cell line K562 induced to die by apoptosis with inhibitors of macromolecular synthesis, a process that is prevented by overexpression of humanbcl-2.It is shown that transfection of K562 cells with the ASFVA179Lgene protects these cells from apoptotic cell death induced by a combination of cycloheximide and actinomycin D or by treatment with cytosine arabinoside. To test the functional role of the highly conserved BH1 domain present in the A179L protein, the Gly residue at position 85 was mutated to Ala, since it has been shown that substitution of the corresponding Gly in human Bcl-2 abrogates its death-repressor activity. It was found that the Gly-to-Ala mutation in the BH1 domain of the viral protein abolished its capacity to protect the K562 cells from apoptosis, indicating that this Gly is essential for A179L action. This finding stresses the functional similarity of the BH1 domains of the viral protein and cellular Bcl-2. |
| doi_str_mv | 10.1006/viro.1996.8395 |
| format | Article |
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To test the functional role of the highly conserved BH1 domain present in the A179L protein, the Gly residue at position 85 was mutated to Ala, since it has been shown that substitution of the corresponding Gly in human Bcl-2 abrogates its death-repressor activity. It was found that the Gly-to-Ala mutation in the BH1 domain of the viral protein abolished its capacity to protect the K562 cells from apoptosis, indicating that this Gly is essential for A179L action. 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This finding stresses the functional similarity of the BH1 domains of the viral protein and cellular Bcl-2.</description><subject>African Swine Fever Virus - genetics</subject><subject>African Swine Fever Virus - physiology</subject><subject>Alanine</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Binding Sites</subject><subject>Cycloheximide - pharmacology</subject><subject>Cytarabine - pharmacology</subject><subject>Dactinomycin - pharmacology</subject><subject>Glycine</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Proto-Oncogene Proteins c-bcl-2 - genetics</subject><subject>Proto-Oncogene Proteins c-bcl-2 - physiology</subject><subject>Rabbits</subject><subject>Tumor Cells, Cultured</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - physiology</subject><subject>VIRUS DE LA PESTE PORCINA AFRICANA</subject><subject>VIRUS PESTE PORCINE AFRICAINE</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM1P3DAQxS3Uii6Uaw-VkHzilsXjOB_ubRdKFwmpUim9urYzBqMkXuxkK_57Eu2qN06j0XvzRu9HyBdgS2CsvNz5GJYgZbmsc1kckQUwWWYsF_CBLBgTPCtrzj-Rk5Se2bRXFTsmxxJ4Xgu5IH9v-ydv_OBDT4Ojq23YDiH5RM0rHZ6Qrlz0Vvf0_p_vkd7gDiP94-OY6Nq2Gaeb0IU2PI74jf4KLc4Z89l6A_Q6dNr3n8lHp9uEZ4d5Sh5uvv--2mR3P3_cXq3uMitkMWRNw3kDKIALIYVzwppGm5wJJ53VFRisBEBdFsZiw02tawamqJgWUFopivyUXOxztzG8jJgG1flksW11j2FMCkpeAythMi73RhtDShGd2kbf6fiqgKkZqZqRqhmpmpFOB-eH5NF02Py3HxhO-te97nRQ-jH6pB7uZZXzifYk1nsRp-47j1El67GfSviIdlBN8O_9fQNoYYyl</recordid><startdate>19970217</startdate><enddate>19970217</enddate><creator>Revilla, Yolanda</creator><creator>Cebrián, Ana</creator><creator>Baixerás, Elena</creator><creator>Martı́nez-A, Carlos</creator><creator>Viñuela, Eladio</creator><creator>Salas, Marı́a L</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>19970217</creationdate><title>Inhibition of Apoptosis by the African Swine Fever Virus Bcl-2 Homologue: Role of the BH1 Domain</title><author>Revilla, Yolanda ; 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| ispartof | Virology (New York, N.Y.), 1997-02, Vol.228 (2), p.400-404 |
| issn | 0042-6822 1096-0341 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals |
| subjects | African Swine Fever Virus - genetics African Swine Fever Virus - physiology Alanine Amino Acid Sequence Animals Apoptosis Binding Sites Cycloheximide - pharmacology Cytarabine - pharmacology Dactinomycin - pharmacology Glycine Humans Molecular Sequence Data Mutagenesis, Site-Directed Proto-Oncogene Proteins c-bcl-2 - genetics Proto-Oncogene Proteins c-bcl-2 - physiology Rabbits Tumor Cells, Cultured Viral Proteins - genetics Viral Proteins - physiology VIRUS DE LA PESTE PORCINA AFRICANA VIRUS PESTE PORCINE AFRICAINE |
| title | Inhibition of Apoptosis by the African Swine Fever Virus Bcl-2 Homologue: Role of the BH1 Domain |
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