A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda

نویسندگان

  • Christine N. Zanghi
  • Heather A. Lankes
  • Birgit Bradel-Tretheway
  • Jessica Wegman
  • Stephen Dewhurst
چکیده

Bacteriophage lambda (lambda) permits the display of many foreign peptides and proteins on the gpD major coat protein. However, some recombinant derivatives of gpD are incompatible with the assembly of stable phage particles. This presents a limitation to current lambda display systems. Here we describe a novel, plasmid-based expression system in which gpD deficient lambda lysogens can be co-complemented with both wild-type and recombinant forms of gpD. This dual expression system permits the generation of mosaic phage particles that contain otherwise recalcitrant recombinant gpD fusion proteins. Overall, this improved gpD display system is expected to permit the expression of a wide variety of peptides and proteins on the surface of bacteriophage lambda and to facilitate the use of modified lambda phage vectors in mammalian gene transfer applications.

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

Construction of the Recombinant Plasmid Expressing AID under the Control of Temperature-sensitive Promoter of Bacteriophage Lambda

Background and purpose: Activation-induced cytidine deaminase (AID) is a B-cell specific enzyme responsible for somatic hypermutation (SHM) and class switch recombination (CSR) of antibody genes within the B-cell follicle of peripheral lymphoid organs. Ectopic overexpression of the enzyme leads to mutations in non-B cells and Escherichia coli (E.coli) genes. However, induction of mutations in E...

متن کامل

استفاده از باکتریوفاژ لامبدا به‌عنوان حامل آپوپتین جهت رسانش موثر آن به درون تومور BT-474 سرطان سینه انسانی

Background: Apoptin is a protein from chicken anemia virus that could induce apoptosis specifically in the cancer cells but it has not any effect in the normal cells. Phage therapy is a novel field of cancer therapy and phage nanobioparticles (NBPs) such as λ phage could be modified to deliver and express genetic cassettes into eukaryotic cells safely in contrast with animal viruses. The bacter...

متن کامل

Simultaneous display of two large proteins on the head and tail of bacteriophage lambda

BACKGROUND Consistent progress in the development of bacteriophage lambda display platform as an alternative to filamentous phage display system was achieved in the recent years. The lambda phage has been engineered to display efficiently multiple copies of peptides or even large protein domains providing a powerful tool for screening libraries of peptides, proteins and cDNA. RESULTS In the p...

متن کامل

Improved Procedure for Screening Expression Libraries for Novel Autoantigens

The standard method for immunoscreening of a cDNA expression library is time-consuming becauseof the production of a large proportion of false positives during the first and second round of screening.This problem is more important when a sensitive chemiluminescence detection system is used. Due tothe high sensitivity of the detection system, there is a need to avoid false posi...

متن کامل

Arabidopsis leaf plasma membrane proteome using a gel free method: Focus on receptor–like kinases

The hydrophobic proteins of plant plasma membrane still remain largely unknown.  For example in the Arabidopsis genome, receptor-like kinases (RLKs) are plasma membrane proteins, functioning as the primary receptors in the signaling of stress conditions, hormones and the presence of pathogens form a diverse family of over 610 genes. A limited number of these proteins have appeard in pr...

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:
  • Nucleic Acids Research

دوره 33  شماره 

صفحات  -

تاریخ انتشار 2005