Studies of the silencing of baculovirus DNA binding protein.

نویسندگان

  • Ilja Quadt
  • Jan W M van Lent
  • Dagmar Knebel-Mörsdorf
چکیده

Baculovirus DNA binding protein (DBP) binds preferentially single-stranded DNA in vitro and colocalizes with viral DNA replication sites. Here, its putative role as viral replication factor has been addressed by RNA interference. Silencing of DBP in Autographa californica multiple nucleopolyhedrovirus-infected cells increased expression of LEF-3, LEF-4, and P35. In contrast, expression of the structural genes coding for P39 and polyhedrin was suppressed while expression of genes coding for P10 and GP64 was unaffected. In the absence of DBP, viral DNA replication sites were formed, indicating replication of viral DNA. Electron microscopy studies, however, revealed a loss of formation of polyhedra and virus envelopment, suggesting that the primary role of DBP is viral formation rather than viral DNA replication.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Recombinant Expression of the Non-glycosylated Extracellular Domain of Human Transforming Growth Factorβ Type II Receptor Using the Baculovirus Expression System in Sf21 Insect Cells

Transforming growth factor beta (TGFβ1, β2, and β3) are 25 kDa disulfide-linked homodimers that regulate many aspects of cellular functions, consist of proliferation, differentiation, adhesion and extracellular matrix formation. TGFβs mediate their biological activities by binding of growth factor ligand to two related, functionally distinct, single-pass transmembrane receptor kinases, known as...

متن کامل

Cloning and Expression of Simian Rotavirus Spike Protein (VP4) in Insect Cells by Baculovirus Expression System

Background: VP4 protein is as spikes on rotavirus outer capsid shell which is responsible for virus attachment to the host. VP4 induces production of neutralizing antibodies which could be used for serotyping of different isolates. Methods: Simian rotavirus SA11 gene 4 cDNA was cloned into a cloning plasmid pDONRTM by recombination reaction using clonase II enzyme mix. The resulting clone was c...

متن کامل

Construction of Recombinant Bacmid DNA Encoding Newcastle Disease Virus (NDV) Fusion Protein Gene

Background and Aims: Newcastle disease virus (NDV) is one of the major pathogen in poultry. Vaccination is intended to control the disease as an effective solution nevertheless this virus is a growing threat to the poultry industry. F gene open reading frame (ORF) from NDV is 1650 bp, encoding a protein of 553 amino acids that can induce protective immunity alone. The F glycoprotein on the surf...

متن کامل

Expression of the Herpes Simplex Virus Type 2 Glycoprotein D in Baculovirus Expression System and Evaluation of Its Immunogenicity in Guinea Pigs

Background: Herpes simplex virus type 2 (HSV-2) is highly prevalent and major cause of genital herpes in humans. The life-long nature of infection and the increasing prevalence of genital herpes imply that vaccination is the best strategy for controlling the spread of infection and limiting HSV disease. HSV glycoprotein D (gD) is one of the most important viral immunogen which has an essential ...

متن کامل

Rapid purification of HU protein from Halobacillus karajensis

The histone-like protein HU is the most-abundant DNA-binding protein in bacteria. The HU protein non-specifically binds and bends DNA as a hetero- or homodimer, and can participate in DNA supercoiling and DNA condensation. It also takes part in DNA functions such as replication, recombination, and repair. HU does not recognize any specific sequences but shows a certain degree of specificity to ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Journal of virology

دوره 81 11  شماره 

صفحات  -

تاریخ انتشار 2007