Translate this page to:
Turkish
In JoVE (1)
Other Publications (2)
Automatic Translation
This translation into Turkish was automatically generated.
English Version | Other Languages
Articles by Sabarish V. Indran in JoVE
JoVE Immunology and Infection
Rift Vadisi Ateşi Virüsü Aşı Güvenliği ve Etkinliği Artırmak İçin MP-12 Gerinim NSS Gen işleyin Ters Genetik kullanma
Department of Pathology, University of Texas Medical Branch
Rift Vadisi ateşi virüs MP-12 aşı suşu için ters genetik sistemi ek MP-12 mutantlar artan zayıflama ve immünojenite oluşturmak için yararlı bir araçtır. Biz NSS mutant suşlar oluşturmak ve karakterize etmek için protokol açıklar.
Other articles by Sabarish V. Indran on PubMed
Bicaudal D1-dependent Trafficking of Human Cytomegalovirus Tegument Protein Pp150 in Virus-infected Cells
Human cytomegalovirus (HCMV) virion assembly takes place in the nucleus and cytoplasm of infected cells. The HCMV virion tegument protein pp150 (ppUL32) is an essential protein of HCMV and has been suggested to play a role in the cytoplasmic phase of HCMV assembly. To further define its role in viral assembly and to identify host cell proteins that interact with pp150 during viral assembly, we utilized yeast two-hybrid analyses to detect an interaction between pp150 and Bicaudal D1 (BicD1), a protein thought to play a role in trafficking within the secretory pathway. BicD1 is known to interact with the dynein motor complex and the Rab6 GTPase. The interaction between pp150 and BicD1 was confirmed by coimmunoprecipitation and fluorescence resonance energy transfer. Depletion of BicD1 with short hairpin RNA (shRNA) caused decreased virus yield and a defect in trafficking of pp150 to the cytoplasmic viral assembly compartment (AC), without altering trafficking to the AC of another essential tegument protein, pp28, or the viral glycoprotein complex gM/gN. The C terminus of BicD1 has been previously shown to interact with the GTPase Rab6, suggesting a potential role for Rab6-mediated vesicular trafficking in HCMV assembly. Finally, overexpression of the N terminus of truncated BicD1 acts in a dominant-negative manner and leads to disruption of the AC and a decrease in the assembly of infectious virus. This phenotype was similar to that observed following overexpression of dynamitin (p50) and provided additional evidence that morphogenesis of the AC and virus assembly were dynein dependent.
A Role for the Small GTPase Rab6 in Assembly of Human Cytomegalovirus
In human-cytomegalovirus (HCMV)-infected cells, the localization of the viral protein pp150 to the virus assembly compartment (AC) is dependent on its direct interaction with the cellular protein Bicaudal D1 through a dynein- and microtubule-dependent mechanism. We found that the small GTPase Rab6 also interacts indirectly with pp150 through its interaction with Bicaudal D1. Inhibition of Rab6 activity in HCMV-infected cells interrupted the intracellular trafficking of pp150, significantly reducing infectious virus production without affecting the formation of the AC, arguing for an important function for this cellular GTPase in the intracellular localization of pp150 during virus assembly.
