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Interaction between human cytomegalovirus UL136 protein and ATP1B1 protein
Cui, Xin; Sun, Zheng-Rong; Ren, Gao-Wei; Wang, Gui-Li; Qi, Ying; Ma, Yan-Ping; Ruan, Qiang.
Affiliation
  • Cui, Xin; China Medical University. Virus Laboratory, the Affiliated Shengjing Hospital. Shenyang. CN
  • Sun, Zheng-Rong; China Medical University. Virus Laboratory, the Affiliated Shengjing Hospital. Shenyang. CN
  • Ren, Gao-Wei; China Medical University. Virus Laboratory, the Affiliated Shengjing Hospital. Shenyang. CN
  • Wang, Gui-Li; China Medical University. Virus Laboratory, the Affiliated Shengjing Hospital. Shenyang. CN
  • Qi, Ying; China Medical University. Virus Laboratory, the Affiliated Shengjing Hospital. Shenyang. CN
  • Ma, Yan-Ping; China Medical University. Virus Laboratory, the Affiliated Shengjing Hospital. Shenyang. CN
  • Ruan, Qiang; China Medical University. Virus Laboratory, the Affiliated Shengjing Hospital. Shenyang. CN
Braz. j. med. biol. res ; 44(12): 1251-1255, Dec. 2011. ilus
Article в En | LILACS | ID: lil-606539
Ответственная библиотека: BR1.1
ABSTRACT
Interplay between the host and human cytomegalovirus (HCMV) has a pivotal role in the outcome of infection. A region (referred to as UL/b’) present in the Toledo strain of HCMV and low passage clinical isolates contains 19 additional genes, which are absent in the highly passaged laboratory strain AD169. Products of the UL/b’ genes may determine the manifestations of HCMV infection in vivo. However, little is known about the host factors, which interact with UL/b’ proteins. This study was conducted to investigate the function of the HCMV UL136 protein. By yeast two-hybrid screening, the β1 subunit of the host Na+/K+-ATPase (ATP1B1) was identified to be a candidate protein, which interacts with the HCMV UL136 protein. The interaction was further evaluated both in vitro by pull-down assay and in vivo by immunofluorescent co-localization. The results showed that the UL136 protein can interact with ATP1B1 in vitro. Co-localization of UL136-EGFP and ATP1B1-DsRed in cell membranes suggests that ATP1B1 was a partner of the UL136 protein. It can be proposed that the HCMV UL136 protein may have important roles in processes such as cell-to-cell spread, and in maintaining cell osmotic pressure and intracellular ion homeostasis during HCMV infection.
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Полный текст: 1 База данных: LILACS Основная тема: Viral Envelope Proteins / Sodium-Potassium-Exchanging ATPase / Two-Hybrid System Techniques / Cytomegalovirus / Protein Interaction Mapping Тип исследования: Prognostic_studies Пределы темы: Humans Язык: En Журнал: Braz. j. med. biol. res Тематика журнала: BIOLOGIA / MEDICINA Год: 2011 Тип: Article

Полный текст: 1 База данных: LILACS Основная тема: Viral Envelope Proteins / Sodium-Potassium-Exchanging ATPase / Two-Hybrid System Techniques / Cytomegalovirus / Protein Interaction Mapping Тип исследования: Prognostic_studies Пределы темы: Humans Язык: En Журнал: Braz. j. med. biol. res Тематика журнала: BIOLOGIA / MEDICINA Год: 2011 Тип: Article